Circadian Biology determines health, not food! DHA, Blue light and nnEMF

[Keyhole]

Below are some excerpts from a paper which can be accessed in full here. Keep in mind that much of the information in this paper deals with physics and complex chemistry. I am not trained in either discipline and I know that most of the people on this forum are not either. So I will include only the pieces of information that are comprehensible for the average reader.

“A quantum theory for the irreplaceable role of docosahexaenoic acid in neural cell signalling throughout evolution”

Six hundred million years ago, the fossil record displays the sudden appearance of intracellular detail and the 32 phyla. The ‘‘Cambrian Explosion’’ marks the onset of dominant aerobic life. Fossil intracellular structures are so similar to extant organisms that they were likely made with similar membrane lipids and proteins, which together provided for organisation and specialisation. While amino acids could be synthesised over 4 billion years ago, only oxidative metabolism allows for the synthesis of highly unsaturated fatty acids, thus producing novel lipid molecular species for specialised cell membranes. Docosahexaenoic acid (DHA) provided the core for the development of the photoreceptor, and conversion of photons into electricity stimulated the evolution of the nervous system and brain. Since then, DHA has been conserved as the principle acyl component of photoreceptor synaptic and neuronal signalling membranes in the cephalopods, fish, amphibian, reptiles, birds, mammals and humans. This extreme conservation in electrical signalling membranes despite great genomic change suggests it was DHA dictating to DNA rather than the generally accepted other way around. We offer a theoretical explanation based on the quantum mechanical properties of DHA for such extreme conservation. The unique molecular structure of DHA allows for quantum transfer and communication of p-electrons, which explains the precise depolarisation of retinal membranes and the cohesive, organised neural signalling which characterises higher intelligence.


DHA abundance controls brain size and function

Comparative evidence on brain composition gave us the first clue to consider both proteins and lipids in six dimensions, and that lipids may specify proteins just as proteins specify lipids. In some animals DHA is present either in the diet or as a product of the strongly rate limited synthesis from plant-derived a –linolenic acid (C18:3n-3). If the velocity of body growth is small then adequate synthesis of DHA for brain growth can occur, resulting in a brain/bodyweight ratio of 4/2% (e.g. small rodents). As the velocity of body growth or protein acquisition increases, the rate limitation of DHA synthesis dominates and relative brain size diminishes. In the largest land-based mammals the ratio shrinks to 0.1% (rhinoceros, Cape buffalo) despite abundant a –linolenic acid in the tissues. An abundant source of preformed DHA, as in the diets of marine mammals, can obviate low biosynthetic capabilities. Such evidence suggests that nutrition, especially with regard to DHA, was a determinant of brain size. For example, the dolphin has a 1.8 kg brain, compared with a land based zebra of a similar bodyweight with only 360 g brain. The rate limitation for DHA with its tortuous synthetic route to its synthesis requiring its import, metabolism and export from the peroxisomes, explains how very small mammals like squirrels with a high metabolic rate and a reasonably efficient biosynthesis achieve a maximally high brain to bodyweight ratio of 2.4%. Incorporation of (isotopically labelled) preformed DHA into the developing rat pup brain was found to be more than an order of magnitude greater than incorporation of DHA synthesised from a-linolenic acid. Humans are much less capable; we can only count on about 1% conversion of a-linolenic acid to DHA. Yet across all mammal species, brain size decreases logarithmically with increase in bodyweight with two exceptions — the dolphin and the human. Clearly we were doing something different during our evolution.

Lipids play a key role in signalling and DHA is involved in the expression of several hundred genes in the brain. The genomic evidence means that an abundant dietary source of preformed DHA, as provided in littoral habitats, would actually stimulate the evolution of the brain, and a lack of DHA would be restrictive. What we were doing differently is that we were a very small group of individuals who consistently ate marine and lacustrine food sources. The superabundance of DHA (and Zn, Cu, I, Se, protein etc.), with its irreplaceable role in neural cell signalling, allowed the synaptic evolution of self-awareness and symbolic thinking and behaviour. Thus began our cultural evolution, very much faster and pervasive than biological evolution : most cultural evolution is dependent on teaching and adaptation rather than pure innovation and hard genetic changes. Yet we remain essentially the same beings, dependent on DHA for 600 million years and unable to move towards a new and improved species without the raw material. Quite apart from any technical arguments, the late Philip Tobias summarised the argument succinctly: ‘‘wherever humans were evolving, they had to have water to drink’’! In other words we did not evolve (especially with our highly dependent infants and children) on the arid savannah.

The curious facet of DHA dominance in evolution is that it's DPA precursor differs by only two protons and would have been more readily available. The difference in fluidity between DHA and DPA is very small; certainly not enough to explain 600 million years of conservation of DHA in photoreception and neural signalling systems. Alternatively, Bloom and colleagues suggested that DHA might have unique electromagnetic properties which have little to do with membrane fluidity. Gawrisch and colleagues have also attempted to explain the DPA/DHA paradox. Using solid-state NMR measurements and molecular simulations they provide an image of DHA as a uniquely flexible molecule with rapid transitions between large numbers of conformers on the time scale from picoseconds to hundreds of nanoseconds. The low barriers to torsional rotation about C–C bonds that link the cis-locked double bonds with the methylene carbons between them are responsible for this unusual flexibility. Both the amplitude and frequency of motion increase towards the terminal methyl group of DHA. Like us, these authors understand that classical biophysics does not have a ready explanation for the irreplaceable DHA.

DHA and quantum mechanics

The van der Waals equation hints that DHA will have both stereochemical and electromagnetic properties. Quantum mechanics can predict the existence of energy levels inside lattices, whereby any electron in that level can be effectively spread across the whole structure, thus becoming a quasi-particle or a wave. Albert Szent Gyorgyi postulated that common energy levels could exist in protein structures, as they contained ‘‘a great number of atoms, closely packed with great regularity’’. He considered the communication of energy between molecules in biological systems could be achieved through coherence of electrons raised to a higher energy state. The formation of a triplet state of the p-electrons around double bonds in aromatic amino acids was the basis for this mechanism. Since Szent-Gyorgyi, the electron transfer of the energy production system in mitochondria has become well known. Bendall considered the conformal dynamics of proteins to be reliant on the long range transfer of electrons. The method of transport is quantum mechanical tunnelling, a feature of proteins demonstrated by Hopfield. Hackermuller et al. obtained evidence that tetraphenylporphyrin exhibits wave like behaviour, indicating quantum coherence in nature. Hammeroff and Penrose proposed a model based on quantum mechanics that can explain consciousness and is testable. In the ‘‘Orchestrated Objective Reduction’’ model of consciousness, quantum coherence exists in the microtubules found in neurons. It is hypothesised that microtubules are capable of quantum computing, and quantum computations are translated to classical outputs—hence consciousness. Hammeroff then proposed the connections between neurons were linked to consciousness. Gap junctions are small enough for quantum objects to cross by quantum tunnelling, allowing cohesion across regions of the brain and creating consciousness. The brain can contain numerous proteins but is absolutely dysfunctional without DHA and AA. We hypothesise that the p-electrons in DHA could behave in similar quantum manner, explaining the unique and irreplaceable role of DHA in neuronal signalling. We must also consider that beyond consciousness, cohesion across regions of the brain drove the evolution of symbolic thinking and behaviour, which is the hallmark of humanity.

[..]

Incoming light hits the back end of the photoreceptors and has to squeeze through the slits between the cell structures. This may split the light into a wave form interference pattern as in Young’s double slit experiment. Acting as a wave, the incoming photon has a far better chance of activating the very specific location of the retinal cis-double bond than as a discreet particle which could easily miss such a small target. A photon wave form also raises the question as to whether or not the incoming wave could activate retinal and DHA simultaneously. Visible light ranges from about 380 to 740 nm; the distance between the retinal and the DHA phosphoglycerides is within this range. Although it is unlikely that there is sufficient energy for a photon to energise both retinal and DHA electrons simultaneously, more than one photon is usually involved in what we see. This situation raises the possibility of cohesion between the retinoid and DHA p-electron activation. In this theory, the energy released in the signalling would be absolutely and precisely quantised by tunnelling, giving us the clear vision, high acuity necessary for reading, fine motor skills, and three-dimensional vision; together with smooth mental processing of our external environment upon which we depend. A similar process might take place in the synapse where the DHA is also densely packed. There DHA might act as a quantum gate controlling the signal in a fashion reminiscent of semi-conduction (Anyone interested should read the work of Robert. O. Becker on bodily DC electric current generation and semi-conduction within bodily cells. Specifically “Cross Currents” or “The Body Electric”).
[..]
Conclusion
As far as our knowledge goes, DHA has been the dominant fatty acid in the membrane phosphoglycerides of the photoreceptors, neurones and synapses for all 600 million years of animal evolution. Even today, the composition of the photoreceptor and brain varies little between species despite large scale species variation in the lipid composition of the diet, liver and muscle. This consistency is despite the fact that its DPA precursor, which differs by only two protons, is more readily available, requires significantly less energy to synthesise, and is more resistant to peroxidation. Moreover, the difference in membrane liquidity by substituting DPA is minimal. By contrast over 600 million years animal genomes underwent countless mutations with enormous variation in protein composition and structures. We suggest that DHA is one Darwin’s ‘‘Conditions of Existence’’ which made DHA the master of DNA since the beginning of animal evolution. Proteins are selected to function with the constancy of DHA: it was the ‘‘selfish DHA’’ not DNA that ruled the evolution of vision and the brain. We propose protein–lipid interactions operate in a multi-dimensional fashion similar to what has been described for proteins. This relationship has to be a two way system. During cell differentiation, the specialist proteins that arrive will seek a lipid match and vice versa. If the matching lipids are not present the system may fail. A practical point is that random mutation and selection for survival have little predictive power. However, has powerful predictive power because it predicts human biological evolution slows or reverts if DHA is not superabundant.
[..]
The extraordinary conservation and irreplaceable nature of DHA in neuronal signalling and its high concentration in the photoreceptor can be explained if it functions as an electron tunnelling device providing quantised signals. Quantum mechanical treatment explains the absolute precision of the membrane depolarisation in phototransduction. This precision is essential to visual acuity and synaptic signalling. Quantum mechanics also explains the photoreceptor oriented counter-intuitively away from incoming light.
We have established that energy minimised structures, molecular polarisation and moment of inertia allow for the theoretical possibility of DHA operating in the realm of supra-molecular chemistry with electron quantum coherence but we clearly acknowledge that further investigation is required.

 

[Keyhole]

Here is some of what Jack Kruse has to say about the quantum effects of DHA and mitochondria + circadian function (in no particular order) taken from Transegrity#5 blog post:

To borrow a phrase from Intel, magnetism is the integrated circuit board that organizes that current of electrons………from sunlight captured by the quantum abilities of DHA. DHA captures that current of electron flow carrying the sun’s light and sends it to every square millimeter of our body over our water and collagen networks. Food and hormones are just proxies for the addition or subtraction of electrons from our cell membranes and proteins within our tissues. The brain is the navigator that derives the environmental electromagnetic spectrum signals to allow our mitochondrial DNA speak to our nuclear DNA using a language both understand. Optimal requires all systems working in concert, if one is off the entire system doesn’t work properly or efficiently.

Without DHA in our brains we cannot properly receive the environments signals in our suprachiasmatic nucleus (SCN) (Our circadian clock!!!!) and in our cell membranes. The SCN needs DHA in its neurons to decipher these signals. Remember DHA is needed to turn sunlight to an electric signal too. When you lack DHA in the SCN you have lost that fundamental ability. That electric signal is transferred from the SCN to the inner mitochondrial membrane over water and collagen topologic insulators. Here, DHA is designed to transfer the electric signal back into light. That light is in the form of heat of infra red light. When we can’t tell time properly in the SCN, we uncouple cellular metabolism from cell growth cycles. - This is where all modern illness begins.

What about modern light? Modern blue light is a real problem for us when you understand scientific scale. Our brain can’t tell the difference between blue light or sun light well. It turns out blue light, which is a type of non EMF, destroys melatonin levels in the brain. As melatonin drops, less DHA can enter our brain’s SCN where circadian rhythms are set. This signaling controls the release of many hormones designed to keep us asleep and wakes us up. As signaling declines even further this leads to serious diseases, like obesity, T2D, and cancer. When we use blue light to excess we destroy melatonin levels in the brain and the pineal gland calcifies. This decreases oxygen tensions in the pineal gland and all our tissues because we become chronically and slowly hypoxic and sleep deprived.

This immediately slows and eventually stops DHA from entering the brain. DHA needs oxygen tensions to remain high to get into our brain and make us human. We are now losing that ability because our current environment we live in is stealing electrons from us.
DHA is fundamentally designed to turn light to an electric signal and then back to light to signal our mitochondria what is going on in the world around us. DHA has never been replaced in 600 million years of eukaryotic evolution for a deep reason. You now know why. Without DHA in cell membranes of neurons you cannot have any proper circadian signaling in your suprachiasmatic nucleus.


Mitochondria act as small nano-electromagnets when they are fully charged with DHA and this draws paramagnetic substance to the tissues with mitochondria. Mammalian red blood cells also lose their mitochondria during erythropoiesis at phase 3.
Magnetic field strength increases only two ways in nature. One is by increasing the current of flow and the other way is by lowering the temperature. Lowering the temperature increases the magnetic effect of tissue by invoking something called the Curie temperature. Since DHA and oxygen both are paramagnetic they are dramatically affected by the innate strong magnetic field of a mitochondria when it is fully charged with electrons. The transfer or DHA and oxygen goes to the tissue with the stronger magnetic field effect because they are paramagnetic. Paramagnetism makes chemical very reactive to the local magnetic effect. This should also point out why an eternal magnetic field stronger than the one creating inside of your mitochondria is deadly chronically.
Moreover, this quantum magnetic effect within mitochondria is why the brain and heart get the highest amounts of blood flow to them. Magnets draw paramagnetic chemicals to them. It is also a natural effect requiring no external energy input. It is a magnetic effect of mitochondrial density or capacity of the tissues. DHA naturally increases the electric and magnetic fields in all of our mitochondria because of its ability to carry a high semiconducting charge of electrons due to its pi-electron clouds. It also needs iodine to generate the large current of flow.

 

[Keyhole]

Taken from a paper titled "Docosahexaenoic Acid (DHA): An Ancient Nutrient for the Modern Human Brain by Joanne Bradbury - link: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3257695/

Modern humans have evolved with a staple source of preformed docosahexaenoic acid (DHA) in the diet. An important turning point in human evolution was the discovery of high-quality, easily digested nutrients from coastal seafood and inland freshwater sources. Multi-generational exploitation of seafood by shore-based dwellers coincided with the rapid expansion of grey matter in the cerebral cortex, which characterizes the modern human brain. The DHA molecule has unique structural properties that appear to provide optimal conditions for a wide range of cell membrane functions. This has particular implications for grey matter, which is membrane-rich tissue. An important metabolic role for DHA has recently been identified as the precursor for resolvins and protectins. The rudimentary source of DHA is marine algae; therefore it is found concentrated in fish and marine oils. Unlike the photosynthetic cells in algae and higher plants, mammalian cells lack the specific enzymes required for the de novo synthesis of alpha-linolenic acid (ALA), the precursor for all omega-3 fatty acid syntheses. Endogenous synthesis of DHA from ALA in humans is much lower and more limited than previously assumed. The excessive consumption of omega-6 fatty acids in the modern Western diet further displaces DHA from membrane phospholipids. An emerging body of research is exploring a unique role for DHA in neurodevelopment and the prevention of neuropsychiatric and neurodegenerative disorders. DHA is increasingly being added back into the food supply as fish oil or algal oil supplementation.
[..]
Animal cell membranes consist of a thin bilayer of phospholipids that is continuous over the whole cell. Critical functions of the cell membrane may be grouped (1) maintenance of membrane fluidity, (2) ligand binding to receptors, (3) cell signaling and gene expression, (4) eicosanoid and docosanoid synthesis [42]. The predominate polyunsaturated fatty acids incorporated into cellular membranes are the longer-chain polyunsaturated fatty acids; AA, dihomogammalinolenic acid (dGLA), EPA and DHA [43]. The types and distribution of fatty acids within the cell membrane phospholipids vary according to the cell type [44].

Experimental and evolutionary evidence supports the notion of a unique role for DHA in cell membranes. Salem et al. [45] report that the loss of a single double bond from the hydrocarbon chain significantly alters the properties of the membrane. Computerized three-dimensional energy-minimized structures of DHA (22:6 n-3) compared with DPA (22:5 n-6) demonstrated that the final double-bond in DHA (not present in DPA n-6) enables the molecule to take a slightly spiral (helical) structure [5]. This property is thought to provide the membrane with a certain molecular order or “fluidity” that may be required for optimal functioning [46].

Recent molecular dynamic modeling of phospholipids bilayers have consistently demonstrated increased membrane flexibility when DHA is present compared with other fatty acids. Feller et al. [47] demonstrated over 100 alternative likely configurations for DHA in phospholipids. In fluid the molecule is constantly changing, when extended it takes a twisted, helical configuration, but often takes a “hairpin” shape where the terminus end is back-folded close to the bilayer. These properties were shown in molecular dynamic studies to result in more highly flexible membranes which were less sensitive to mechanical stress than saturated fatty acids [48]. Other modeling studies have shown that the lower melting point for the less unsaturated arachidonic acid was associated with increased disorder in fluid compared with DHA [49]. Unsaturated chains have been associated with thinner, more permeable membranes with increased water permeation when compared with saturated fatty acids [50]. Huberet al. [48] speculate that the long highly unsaturated chain of DHA in membrane phospholipids may facilitate solvation in hydrophobic areas for the benefit of G-coupled membrane proteins such as rhodopsin.

These recent advances in understanding the influence of the highly unsaturated DHA molecule in the membrane phospholipids has fuelled speculation that it may work as a metabolic “pacemaker” for cells, and perhaps influence the metabolism of the whole organism via an impact on the basal metabolic rate [51]. This theory was tested by Turner et al. [52], who demonstrated a positive linear relationship between the high molecular activity of the enzyme Na+K+ATPase (the sodium-potassium pump) and membrane concentration of DHA in the surrounding phospholipids in brain, heart, and kidney tissue of samples from both mammals and birds. Further, the highest concentration of DHA was found in the mammalian brain as was the highest activity rate of the pump. This is significant as the sodium-potassium pump accounts for some 20% of the basal metabolic rate but approximately 60% of the energy utilization in the brain.

[..]
NF-κB is a protein that resides in the cytoplasm of immune cells (particularly B and T lymphocytes). In its latent form it is bound to an inhibitory protein (IκB) but after activation by an inducer, IκB is degraded and NF-κB is released. It moves rapidly into the cell nucleus where it up-regulates the expression of the genes for many proinflammatory mediators, such as the cytokines IL-2, IL-6, and IL-8. These events mediate a cascade of inflammatory processes both locally and if produced in sufficient quantities, systemically. NF-κB activation is extremely sensitive to oxidative stress. For instance, raised levels of reactive oxygen species (ROS), which are natural bi-products of metabolic activity, activate NF-κB through the degradation of IκB. This mechanism can be inhibited by antioxidants [56] and DHA

DHA is a potent regulator of NF-κB via multiple mechanisms [57]. DHA itself was shown to directly inhibit NF-κB activation [58]. Mice macrophage cells that were stimulated with the bacteria LPS and interferon, increased nitric oxide (NO) production. Pre-treatment with various polyunsaturated fatty acids demonstrated that DHA had a marked dose-dependent inhibitory effect on NO production. Further, DHA prevented the activation of NF-κB by up-regulating intracellular glutathione to a level high enough to effectively balance the oxidative stress. It is interesting to note that these anti-inflammatory effects of DHA are mediated via increasing the availability of intracellular antioxidants.

Indirect mechanisms for DHA include mediation of anti-inflammatory effects via its oxidation to potent signaling molecules, resolvins and protectins, collectively known as docosanoids. During conditions of tissue stress, both EPA and DHA may be released from phospholipids to undergo conversions to “resolution phase interaction products”, known as resolvins [12]. Two distinct resolvin molecules have been identified for EPA (E1 and E2) and four for DHA (D1-D4). Oxidation occurs via the LOX enzymes. During local tissue inflammation, cells in blood vessel walls convert DHA to 17S-HDHA via 15-LOX. The molecule is secreted from vascular cells and taken up by neighboring neutrophils for conversion via 5-LOX to its family of D-series resolvins. The actions of the resolvins are similar to those of the lipoxins, oxidized from arachidonic acid and EPA substrates, in that they actively promote resolution of inflammatory processes. Known anti-inflammatory mechanisms for the resolvins include the down-regulation of NF-κB and the removal of neutrophils from inflammatory sites [57].

In addition to resolvins, DHA has recently been discovered as the precursor for a newly identified docosanoid called protectin, or neuroprotectin when it is found in the central nervous system. Protectin is synthesized by peripheral blood mononuclear cells and CD4 cells in response to oxidative stress and has been found in neurons, astrocytes, peripheral blood and lung tissue [12]. As the first protectin identified, it was designated D1 or NPD1 when found in nervous tissue [59]. NPD1 induces nerve regeneration, reduce leukocyte infiltration and maintains homeostasis through ageing by reducing pro-apoptotic and pro-inflammatory signaling [60]. NPDI is induced by oxidative stress and protects retinal and neuronal cells from oxidative stress-induced apoptosis. Many mechanisms have been implicated, including suppression of the IL-1β induced stimulation of COX [61]. The discovery of NPD1 offers new therapeutic opportunities for a range of neurodegenerative conditions, such as Alzheimer’s disease. It also provides an exciting potential for DHA in helping to delay or minimize the “normal” cognitive decline during ageing [62].

DHA is also associated with other neuro-protective factors. Mice fed a DHA-rich diet had significantly higher levels of brain-derived neurotrophic factor (BDNF) in the striatum, an area of the brain involved in Parkinson’s Disease [63]. Mice fed an omega-3 deficient diet for 4 weeks after weaning had reduced levels of striatum DHA and BDNF compared with control mice [64]. The neurotrophic family of proteins, including BDNF, are integral for neurogenesis but it has also been suggested they continue in the long-term maintenance of the function, shape and plasticity of neurons, especially in high electrical areas, during ageing [65].

 

[Keyhole]

Blue light's relationship with DHA

Blue light hazard: New Knowledge, New approaches to Maintaining Ocular health

link: http://www.crizalusa.com/content/dam/crizal/us/en/pdf/blue-light/Blue-Light-Roundtable_White-Paper.pdf

Blue light damage occurs when a photosensitizer absorbs photon energy of a specific wavelength, setting in motion a series of intracellular chemical reactions. Rods, cones, and RPE cells of the outer retina—the cells responsible for photon absorption and visual transduction—are rich in photopigments and therefore susceptible to photochemical damage. Blue light can cause damage to both photoreceptor and RPE cells in primates. Cumulative exposure to light in the 380 nm to 500 nm range can activate all-trans-retinal accumulated in the photoreceptor outer segments (Figure 5). The is blue light photo-activation of all-trans-retinal can induce production of reactive oxygen species (ROS), such as singlet oxygen, hydrogen peroxide, and other free radicals, in the photoreceptor outer segments. The ROS attack many molecules, including polyunsaturated fatty acids, a major component of cell membranes. The large concentration of cell membranes in the retina makes it highly sensitive to oxidative stress. In particular, this stress may disrupt the membranous structures of the photoreceptor outer segments, causing incomplete phagocytosis and digestion of oxidized outer segments in the RPE. The consequence is an accumulation of the waste product lipofuscin in RPE cell granules. In the eye, lipofuscin… is highly susceptible to photochemical changes that can produce permanent cellular damage.

Lipofuscin accumulation has been implicated in the pathogenesis of AMD, and intense lipofuscin autofluorescence is frequently observed in regions surrounding the leading edges of geographic atrophy lesions in the retina.

A2E (N-retinylidene-N-retinylethanolamine) is a key photo-sensitive fluorophore that mediates lipofuscin phototoxicity. (A fluorophore is a chromophore that can re-emit light after excitation.) With maximum absorption at around 440 nm, A2E is excited by blue light. The photosensitization of A2E leads to the formation of ROS and to an inhibition of lysozyme’s ability to break down cellular structures for recycling. Excessive oxidative stress can cause dysfunction in the RPE cells and, eventually, cell death by apoptosis. Without the supportive functions of the RPE, photoreceptors cannot function properly and will degenerate as well. Lipofuscin accumulation and
A2E photosensitization are involved in this cascade of phototoxic effects, which has been implicated in the pathogenesis of AMD.

A brief summary : Artificial blue light exposure causes a release of Reactive Oxygen Species (free radicals) in the photoreceptors of the eye. These ROS cause oxidative stress and damage to the cell membranes of the retina. Remember that the retina holds the body's largest concentraton of Docosahexaenoic acid. In simple terms, blue light destroys DHA in the eye.

How does this link with the possible quantum effects of DHA? = look back at the paper on the quantum theory for DHA by Crawford et al. (It is possible that) DHA converts photonic energy from the sun into a DC electric current through the process of "quantum tunnelling" of electrons past the cell membrane. This electric current is then useable by the human body. Blue light degrades the body's stores of DHA, and therefore diminishes all of DHA amazing abilities within the body.

But not only does blue light affect DHA in the eye - it also affects DHA in the skin and in doing so greatly diminishes mitochondrial efficiency!

Blue Light Induces Mitochondrial DNA Damage and Free Radical Production in Epithelial Cells* by Godley et al - link: http://www.jbc.org/content/280/22/21061.full

Blue light damage is not an uncommon feature of the skin and eye. This is perhaps not surprising because whereas both tissues will be afforded protection against UV through natural (e.g. cornea, lens, and melanin) or artificial (e.g. sunscreen) filters, they are constantly exposed to the visible spectrum, of which the blue light region is the most energetic. In the eye, blue light damage is considered predominantly photochemical in origin and to arise largely from eye-specific chromophores (e.g. retinoids, melanin, and lipofuscin). In the skin, the situation is less clear but is likely to involve chromophores associated with mitochondria (e.g. cytochromes and flavins) that absorb in the blue region of the visible spectrum to contribute significantly to ocular toxicity.
In this study, we have demonstrated that blue light is able to photogenerate ROS from isolated mitochondria. This confirms that mitochondria possess blue light-sensitive chromophore(s). Studies have shown that blue light is able to cause ultrastructural damage and mitochondria-dependent cell death in lipofuscin-free RPE cells (23–25), which suggests that other chromophores, rather than lipofuscin, in the RPE cells mediate these light effects. It has been postulated that blue light-induced retinal damage is mediated by mitochondrial respiratory enzymes (26, 27), and it has been shown that inhibiting the mitochondrial respiratory chain blocks ROS generation (25, 28). This is further supported by the finding that H2O2 production is significantly increased in kidney epithelial cells overexpressing flavin-containing oxidases (11), which are concentrated in mitochondria (29). Flavin-containing oxidases absorb throughout the UVA-blue spectrum, with peak at 370 and 450 nm. In addition, it has been demonstrated that the content of cytochrome c oxidase was reduced in the RPE cells following exposure to blue light (30). Cytochrome c oxidase is an important mitochondrial respiratory enzyme involved in oxidative phosphorylation. It has peak absorption at 440 nm in the reduced form (31). Together, these data implicate the involvement of mitochondrial respiratory enzymes in phototoxicity.
[..]
In conclusion, the vulnerability of mtDNA to mitochondria-derived ROS in response to blue light strongly supports a role for visible irradiation in cellular dysfunction. Such dysfunction will be maximal in tissues such as skin and eye, which are regularly exposed to blue light and thus ROS throughout life (54, 55). The accumulation of stochastic oxidative damage in mitochondria supports a number of hypotheses of aging in which the mitochondrion plays a central role (33, 56–58). Furthermore, the ROS-induced aging is also likely to contribute to a variety of age-related pathologies such as skin cancer and age-related macular degeneration.

 

[Keyhole]

Blue light's effects on the human brain and circadian biology - Very important!

Some information from Jack Kruse's "Brain Gut: 11" blog post.

So you might be wondering what exactly does artificial light do to a human brain?

In a word, it destroys its ability to properly signal environmental signs to our cellular machinery. It affects this molecular machinery pretty quickly by fast forwarding our circadian chemical clocks to light. These clocks are all biologically tied to the cell cycle that controls growth. How does this happen? The first clinical sign is a change in a hormone’s secretion in the brain. It dramatically alters the surge of the pituitary secretion of Prolactin. This happens after 4 hours of darkness or after a really big release of oxytocin.

The surge of Prolactin is normally quite large in normal darkness but is significantly diminished in artificially lit environments after sunset. This was shown in the CT 2 video. This has big implications for modern humans. The reason is that prolactin release is coordinated with sleep cycles where autophagy is at its highest efficiency and where Growth Hormone is released. If this is diminished we generally see lower DHEA levels clinically and higher IL-6 levels on cytokine arrays. Remember when we see lowered DHEA levels this sends a signal to our gut flora that something is amiss. It allows more permeability of our intestinal brush border to inflammation that destroys signaling.

For evolution to work, a cell first must adapt to its environment. So the first thing a cell would encounter in an earth day is a period of day and night. The cell also has to make energy and it also has to control its own cellular division. In essence the circadian cycle has to “yoke” to the metabolic cycle and its growth cycle. Evolution harnessed these environmental signals to control both metabolism and cellular growth. When it is dark at night time, the cell becomes more reduced chemically and electrically. (A lower redox state like we saw in the mitochondrial series). During a low redox time, cells are usually recycling their components using autophagy. During the day with sunlight, energy is being made to explore the environment, the cell is more oxidized because of increased leakiness of the mitochondria at cytochrome number one. This is how the environmental light signal is coupled to the chemical signal in the mitochondria. Another interesting coupling occurs between the circadian cycle with the cell cycle. They are linked via the PER 1 and PER 2 genes. PER 2 directly effects the cell cycle in mitosis. Mitosis is the phase in the cell that occurs just before cell division to generate an offspring. The mammalian period 2 gene plays a key role in tumor growth in mice; mice with a mPER2 knockout show a significant increase in tumor development and a significant decrease in apoptosis (levee 19). This is thought to be caused by mPER2 circadian deregulation of common tumor suppression and cell cycle regulation genes, such as Cyclin D1, Cyclin A, Mdm-2, and Gadd45, as well as the transcription factor c-myc, which is directly controlled by circadian regulators through E box-mediated reactions. E-box reactions involve regulation of the hTERT gene encoding the telomerase catalytic subunit. Here is where circadian biology directly impacts telomere biology. Because the telomerase enzyme is altered in these E box reactions, light, especially artificial light during sleep cycles, plays an important role in human cell senescence, immortalization, and carcinogenesis.

This implies that sleep is tied directly into to cell cycle functioning and directly into cell mediated immunity at some level. It appears that sleep directly effects the chronic diseases of aging and likely plays a role in cancer development.

The main 'take home' points from this section
1. Our cellular activity is regulated by circadian cycles - this includes growth, metabolism and repair functions. These processes are affected by artificial light exposure.
2. Artificial blue light exposure after sunset lowers DHEA(hormone) levels >> which send signals to the gut to increase intestinal permeability and therefore make the gut leaky.
3. Specific genes (PER1 + PER2) are important in regulating cell division cycles. The action of these genes can become dysregulated by artificial light exposure and subsequently lead to tumor development.

Humans have the largest brain of any mammal. We have 8 lobes in our brain. We have 2 frontal, parietal, temporal, and occipital lobes. The Occipital lobes in the back of brain control most of the neuron circuits for light and vision. This implies that 25 % of our brain is tied to light circuits. It gets more interesting for us. The other six lobes have areas within them called the association cortex. Light also wires directly to these areas too! What does this mean? It means if you’re a human with a big ass brain 45-48% of your brain is wired to light circuits. We recently discovered two visual systems in humans. There are two pathways for sight in the retina. One is based on classic photoreceptors (rods and cones) for regular vision, and the other, newly discovered, based on photoreceptive ganglion cells which act as rudimentary visual brightness detectors. These circuits are very important for circadian signaling of day and night. Your hypothalamus is in control of accounting for energy by accounting for electrons from food. These electrons are sent to your mitochondria’s inner membrane to generate energy. Your hypothalamus integrates and yokes sleep and metabolism as I laid out here a year ago. The hypothalamus only makes up 1% of the total volume of your brain. Moreover, the outflow tracts of the leptin receptors in the hypothalamus only project to ten percent of the rest of the neurons in your entire brain.

What does this imply? It means that the conventional wisdom that diet is the main controller of metabolism might be dead wrong. Maybe, light is the master controller of how you account for calories after all? It also means light is tied to body composition, cancer, illness, and our gut flora composition.

Just to clarify: According to Kruse, 45-48% of neural circuits in the brain are respondent to light/darkness and depend on them to function properly. In contrast, only 10% of neural circuits are reliant on food stimulus. Understandable, Kruse is suggesting that light exposure has the most powerful influence on controlling cellular processes, not food.

Ideal hormonal processes during sleep

The first step is leptin levels rise slowly for four hours post dinner. At midnight leptin then enters the hypothalamus. Once it binds to the receptor two things occur. The first is a second messenger is sent to the thyroid to up regulate free T3 production to stimulate uncoupling protein 3 in muscles to burn fat liberated as we sleep at a higher metabolic rate. These fats are burned not as energy but as free heat at the muscles. We do this as well, in the cold, as I taught you in the CT series.

The key take home is it requires leptin sensitivity and ideal thyroid function at the muscle level. How do we maintain ideal thyroid function? The Epi-paleo template should be the obvious answer to you now. The reasons should be even more obvious. The Epi-paleo Rx makes sure that everything the brain needs and thyroid needs are in the same evolutionary food packages. It also lowers inflammation and leptin levels best. It also provides ample iodine resources to maintain your free T3 levels regardless of your carbohydrate intakes.
[..]
The second effect of leptin is via another second messenger: the coupled receptor with leptin bound to it, sends a message to the anterior pituitary to release prolactin from 12-2 AM. The prolactin release is required for proper control of sleep stages and yoking sleep and metabolism…..but the real benefit is this is the signal the hypothalamus uses to release pulsatile growth hormone release from 2 AM to 5 AM during sleep stages 2-4. This allows the process of AUTOPHAGY (homeostatic process by which defective cells and proteins are recycled) to be of maximal efficiency as we sleep. At sunrise, cortisol rises and so does ghrelin, a gut hormone. What does ghrelin do during the day to growth hormone secretion? It stimulates it pulsatile release during daylight hours. This means that proper growth hormone release is completely tied to proper circadian signaling. It is also means that an IGF-1 level is instructive to a mismatch to a clinician. When IGF-1 is low, this usually signals an alteration in the cortisol/DHEA/melatonin axis. This is why a lowered AM cortisol is tied to T2D and most neolithic disease states. T2D have some of the lowest IGF-1’s measured in clinical medicine. When IGF-1 is low this means the person body composition is also dramatically altered. Low growth hormone levels signal higher body fat levels (especially visceral fat) and lowered levels of lean muscle mass. People with low IGF-1’s tend to also have sleep disorders like obstructive sleep apnea. When your AM/PM cortisol levels is off because of artificial light you can not make growth hormone and your body composition declines rapidly. This is why people get fat and lose muscle mass when their light cycle is off.

The most important thing to understand here, is that this whole process can only occur properly if your are sensitive to Leptin. Circadian mismatches actually cause leptin resistance, so there is a good chance that many people are leptin resistant to some extent, therefore cannot go through a proper sleep cycle.

Blue light's effects on these hormones

Blue light after sunset reduces the prolactin surge we normally see in humans. When we see chronic lowered prolactin surges we also see lower growth hormone secretion during the anabolic phases of sleep. Lowered chronic GH secretion directly affects cardiac and skeletal muscle function because the process of autophagy is made less efficient as our life continues. Lowered GH and the sex steroid hormones at sleep lead to loss of cardiac function. This is why heart failure is strongly associated with low IGF-1 and low sex steroid hormone levels. When growth hormone is not released in normal amounts, it also decreases our lean muscle mass, and increases our body fat percentage in all our organs and in our body. This leads to slowly declining organ dysfunction and poor body composition. We can measure this process clinically by looking for falling DHEA level (bad) and a falling Growth Hormone level (also bad) as we age.

 

[Keyhole]

Molecular clocks

Almost every single cell in the body contains circadian clocks. The molecular clocks are responsible for determining when the cell performs functions such as DNA replication and repair, energy metabolism, and when to rest. These functions are highly specific, and must be completed within certain periods of time to be rendered successful. Every function in the body is dependent on circadian signalling via molecular clocks. The clock mechanism is not only regulated by natural light cycles, but also accounts for food electron-density. In simple terms, this means that eating fruit in northern-hemisphere winter completely destroys the circadian system and results in faulty signalling. It also means that focusing solely on dietary changes may not be sufficient to reverse Neolithic disease when one is placed in an artificially lit environment for the majority of each day. In my opinion, circadian factors should be the main focus when dealing with illness.

Interestingly, the article below states that cancer cells are one of the only types of cell that do NOT have circadian clocks. What does this suggest? Consider the fact that the cellular clock’s main function is to synchronise individual cellular activity with the rest of the body functions. Each cellular clock’s “timing” mechanism MUST be in sync with the rest. In cancer, we see rapid, uncontrolled cellular division which is unresponsive to feedback-signalling regulation systems. It would therefore make sense that cancer cell proliferation originates from circadian signalling defects that result in clock gene mutations and subsequent molecular clock suppression. The result is that there are no clocks contained within the cancer cell to regulate their own timing, therefore we see rapid overgrowth and eventual tumor development.

What is the route cause of this? Probably multiple factors: Environmental toxicity, dietary choices, but IMO the main factor is circadian dysregulation, and I think this info acts as a decent evidence for this conclusion.


Exerpts taken from an article titled: How the Body’s Trillions of Clocks Keep Time

“Almost every cell in our body has a circadian clock,” said Satchin Panda, a clock researcher at the Salk Institute. “It helps every cell figure out when to use energy, when to rest, when to repair DNA, or to replicate DNA.” Even hair cells, for instance, divide at a particular time each evening, Panda has found. Give cancer patients radiation therapy in the evening rather than in the morning and they might lose less hair.
[..]
Researchers have found that peripheral clocks are based on CLOCK and a protein called BMAL1, as is the clock in the suprachiasmatic nucleus. Clasping each other tightly, this pair attaches to the genome and recruits other proteins to start the transcription of nearby genes, including per. Many of these genes are behind certain physiological rhythms — the production of liver enzymes around mealtime, for instance, and the daily rise and fall of blood pressure.

But some proteins, including PER, serve as counterbalances. As PER and its partners gradually build up in the cell over a period of 12 hours, they inhibit the activity of CLOCK and BMAL1. Over the next 12 hours, the counterbalances are slowly degraded, and CLOCK and BMAL1 surge back. Just before dawn and just before dusk, John Hogenesch, a chronobiologist at University of Pennsylvania, has found, there are “rush hours” of gene expression, perhaps the body preparing for the different demands of surviving in the light and in the darkness.

It’s a tidy, self-governing system, and it’s tempting to call it ubiquitous. But these studies have revealed too that not everything has a clock. Embryonic stem cells, which can develop into almost any cell type, don’t keep time. The testes, almost alone among the organs that have been tested, don’t seem to have a clock either. And many cancer cells do not keep a regular rhythm. What could these things have in common? This is where Partch’s discovery comes in.

One of the first things Partch learned about PASD1 was that it appears in very few tissues. But the ones where it does are intriguing: the testes and cancers. When Partch became a professor at the University of California, Santa Cruz, she and her students began adding PASD1 to cells equipped with glowing PER. They found the cells’ usual light was damped down to a faint glimmer, indicating that PASD1 was interfering with the normal operation of the clock. And the more PASD1 they added, the dimmer the cells were.

Next, Partch and her students grew cells with glowing PER and got all the cellular clocks synchronized. The glow would get brighter and dimmer like a sine wave with a 24-hour period, with defined peaks and troughs for as long as the cells stayed synchronized. Partch then caused some of those cells to produce PASD1. In these cells, the glow became more of a wobble than a wave — the peaks low and the troughs shallow — and very soon it faded away. The cells could not maintain their rhythm.

The team is still working to pin down exactly how PASD1 calls a halt to the cells’ cycling. But one specific part of the protein gives them a hint. This section of PASD1 looks like a part of CLOCK that is absolutely essential for circadian rhythms. “But no one still to this day knows quite exactly what it does,” Partch said. She hopes that by understanding how the key piece of PASD1 works — perhaps, for instance, it binds to BMAL1 itself and keeps CLOCK from doing so — they can learn the role of this key piece of CLOCK.

So far, the work has confirmed Partch’s initial hunch that PASD1 would stop the clock. And it suggests that in the tissues where PASD1 is present, it is part of the reason why the cells don’t oscillate. That finding opens the door to deeper questions: With the clock directing so many aspects of cellular behavior, and with mutations in clock genes leading to illness — they’ve been fingered in cancers and metabolic disorders — why would some types of cells lack a clock or have a weakened one?

“It seems like there’s some really interesting and still unexplored connection between some perfect pluripotency,” meaning the cellular ability to develop into any cell type, “and running a clock,” Partch said. She recounts experiments from Kazuhiro Yagita’s lab, in which embryonic mouse stem cells are spurred into development. “At first, it’s like come on, come on, no ticking, no ticking… and then, at some point in the differentiation of these cells, the clock comes on.” When the process is reversed, the clock turns off.

The lack of a clock in stem cells may be because the precise genes controlled by the clock vary so much from tissue to tissue, Partch speculates. Work from Charles Weitz’s lab has shown that liver and heart tissues share only 8 to 10 percent of genes that oscillate daily, for instance. “[Stem cells] have to be everything and nothing at once,” Partch said. “Maybe in a cell that doesn’t know what it is yet, it’s not ideal” to have a clock. It’s a notion that could encompass the testes, where mature sperm are far outnumbered by stem cell precursors, and where PASD1 has been spotted. She has yet to look for PASD1 in other stem cells.

In cancers, the protein’s other known hangout, the reasons for its presence are likely to be different. “It may be the reason why the clock is not operational in most solid tumors,” said Hogenesch, who was not involved in the work. “If you’re a tumor, and you want to keep dividing and dividing and dividing, maybe you don’t want to be confined to dividing at one time of the day. Maybe there’s an evolutionary advantage — to tumors at least — to disrupt the clock so they can divide whenever they have sufficient resources rather than being nudged and nuanced to divide at a particular time of day.” Partch’s group found that interfering with PASD1’s production in two cancer cell lines made their oscillations stronger and more regular. That suggests that future work should look to see whether knocking PASD1 down might also rein in the cancer cells’ out-of-control reproduction.

 

[Keyhole]

Is ATP the body’s real source of energy? Or did mainstream biology get it completely wrong….

To answer this question, we need to begin with a little bit of background information. Dr Gilbert Ling is cell physiologist and biochemist who has focused on cell-membrane physiology and is known for his controversial views on the theory of ATP’s function and the sodium-potassium pump. Unfortunately, the mainstream scientific community completely shunned Ling, and he was considered a “loony”. Ling’s theories challenged prominent theories (which went on to become dogma) and upset a few people who were “high up” among scientific authorities, and eventually in 1988 he had he laboratory shut down and funding cut from the National Institute of Health. I have been trawling through one of his books titled “Life at the Cell and Below-Cell level: The hidden history of a fundamental revolution in biology” and think some of the information really needs to be laid out here. It seems that Ling was wayyyy ahead of his time and science is only just beginning to catch up.

For those who aren’t sure about those terms:

ATP (Adenosine Tri-Phosphate): a chemical commonly understood to be the main product of energy metabolism and the fuel for pretty much all cellular activities – the body’s ‘energy currency’.

Sodium-potassium pump: commonly understood to be a “pump” embedded in a cell’s membrane which pumps potassium and sodium ions (charged particles) into and out of the cell, maintaining a membrane potential (charge). These “pumps” are considered crucially important for cellular function.

To quote Ling:

“Like all pumps, ceaseless activity requires a ceaseless supply of energy.
[..]
Meyerhof and Lohmann measured the heat of dephosphorylation of ATP (to ADP) and obtained a value of -12.0 Kcal/mole.318 Based upon this and other relevant data, Lipmann then offered a new major cell physiological hypothesis,132 in which each one of the two terminal phosphate bonds in the ATP molecule contains an extra amount of free energy. This energy can be liberated to perform biological work with the aid of an ATP-splitting enzyme known as ATPase. These unusual phosphate bonds are given the name, "high energy phosphate bonds'" and represented as ~P.

Danish biochemist, Jens C. Skou found that the "membrane fraction" of a crab nerve homogenate contains a special kind of ATPase, which requires both K+ and Na+ for maximum activity—hence the name Na,K-ATPase. Skou then postulated that this and similar enzymes located in other cell membranes can liberate, and use the "high energy" in the high-energy-phosphate bonds of ATP to transport Na+ out of the cell, and K+ into the cell, both against concentration gradients. In other words, this membrane Na,K-activated ATPase is the postulated Na pump.”

Three facts that disprove the idea that ATP drives cellular reactions via sodium-potassium pumps

1.The minimum energy requirement for the postulated sodium pump in frog muscle to function rigorously has been shown to be at least 15 to 30 times the maximum available energy from “ATP hydrolysis”. See table below

2. Ling found 18 other pumps located elsewhere in the cell, including the sodium pump on the sarcoplasmic reticulum – which requires 50 times more energy than a similar pump at the cell membrane. Consider the fact that one membrane pump alone requires more energy than the cell has in TOTAL (including all of the energy needed for every other cellular function)

3. “To wit, the so-called "high energy phosphate bond" does not contain high energy. Podolsky and Morales's conclusion was based on the more precise measurement of the heat of hydrolysis of ATP and a (judicious) correction for the heat of neutralization of the acid liberated during the hydrolysis. Thermodynamic analyses led George and Rutman to a similar conclusion: that there is no high energy in the so-called high-energy phosphate bond.

“With the truth about the "high energy phosphate bond" concept brought to light, even the 1500% to 3000% energy disparity figures for the postulated sodium pump in frog muscle cited appear to be serious underestimations.”

In simple terms, the theory of ATP as the cellular "energy currency" was put forth and accepted by science without anyone actually doing the mathematical calculations. Gilbert Ling showed on a number of occasions that energy expenditure clearly outweighed energy availability. He concluded that ATP simply can not be the body's energy currency.

 

[Keyhole]

Gilbert Ling's Association-Induction Hypothesis

Ling understood that ATP was not the source of cellular energy, however he also understood that ATP clearly played an important role in energy transfer somehow. He was lead to the conclusion that ATP's real function was to alter the configuration of intracellular proteins, and in doing so, to expose binding sites which allowed water to bind to them. When this occured: Water changed drastically, transitioning from free-bulk water to a liquid crystalline state capable of storing and transmitting vast amounts of energy. Hence, water was the genuine source cellular energy, and ATP merely facilitates the process of energy extraction

Ling's theory is extensive, and there is no need to go into the nitty-gritty science. For anyone who's interested, you can grab one of his books or access one of the many shorter reviews of the theory online. Below is a short review as part of a paper written by Dr Mae-Wan Ho which can be found here. It is fairly technical at some points, but certainly worth the read:

Ling’s answer is that the proteins are in a very different state inside the cell, and so is the water, and the main reason is the ubiquitous presence of ATP [4].

Proteins are long linear polymers of amino-aids joined end to end in a peptide bond (-CONH-). Peptide bonds on the same chain can form hydrogen bonds with one another, giving rise to secondary structures of a-helices or b-pleated sheets. Most proteins in solution are also folded up in further globular tertiary structures. That’s the conventional textbook story.

However, that story does not apply to the cell, according to Ling. In his fully developed association-induction (AI) hypothesis, he proposed that the major components of living protoplasm – water, proteins, and K+ - exist in a closely associated, high-energy state at ‘rest’. Within the resting cell, most if not all proteins are extended so that the peptide bonds along their polypeptide backbone are free to interact with water molecules to form ‘polarized multilayers’ (PM) of aligned water molecules, while the carboxylate side chains preferentially bind K+ over Na+. Both are due to the ubiquitous presence of ATP in living cells.

In the absence of ATP, proteins tend to adopt secondary structures – a-helix, or a b-pleated sheet - as hydrogen bonds form between peptide bonds in the same chain, so they don’t interact with water (Figure 1 left). In this state, the carboxylate and amino side chains are also unavailable for binding ions, as they can pair up with each other. And the water next to the protein is not too different from the bulk phase outside the cell.

However, when ATP is bound to the ‘cardinal site’ of the protein, it withdraws electrons away from the protein chain, thereby inducing the hydrogen bonds to open up, unfolding the chain, exposing the peptide bonds on the backbone, and enabling them to interact with water to form polarized multilayers (PM) . At the same time, the carboxylate and amino side chains are opened up to interact with the appropriate inorganic cation X+ and anion Y-. The protein ‘helper’ Z bound to the polypeptide chain is now also fully exposed. In muscle, the polypeptide chain binding ATP is myosin, and Z could well be actin. The cation X+ is K+ in preference to Na+, because ATP binding turns the carboxylate group into a strong acid that prefers K+ over Na+.

When ATP is split into ADP and Pi, and detaches from the protein, the reverse change takes place, the protein reforms its secondary structure and expels the PM water. This switching between states is the elemental ‘living machine’. It is what animates and energizes the living cell.

Notice that the state change involves a major change in the water between an ordered PM to a relatively disordered state. (Something like this could well be the basis of how actin and myosin function in muscle contraction.)

Recent corroboration of Ling’s hypothesis and the liquid crystalline cell

The interaction of unfolded protein chains with water is particularly significant. When protein chains are unfolded, their peptide bonds -CONH- become exposed, forming an alternating chain of negative (CO) and positive (NH) fixed charges that is very good at attracting polarized multilayers (PM) of oriented water molecules (see Figure 2). I have referred to this water as ‘liquid crystalline water’ on grounds that it forms dynamically quantum coherent units with the macromolecules ([17] The Rainbow and the Worm, The Physics of Organisms, ISIS publication), enabling them to transfer and transform energy seamlessly with close to 100 percent efficiency. And it is this liquid crystalline water that gives the cell all its distinctive vital qualities (see [18] Life is Water's Quantum Jazz, ISIS Lecture).

Many recent findings lend support to Ling’s hypothesis and the liquid crystalline cell, and I shall mention them in context.

PM water molecules are highly polarized and oriented. According to Ling [4], they are restricted in motion, and have shortened nuclear magnetic resonance relaxation times. (This is the basis of nuclear magnetic imaging that detects cancerous tissues by their longer relaxation times, as indicative of less structured water.) PM water does not freeze at the temperature of liquid nitrogen, and it tends to exclude solutes, which accounts for the apparent diffusion barrier for many molecules that are erroneously attributed to the cell membrane. In fact, the cell membrane offers very limited restriction to diffusion, and it is the PM water that excludes them.

PM water resembles supercooled water that has been identified in recent years as hydration water of proteins (see [19] Dancing with Macromolecules, SiS 49). A similar phase of water has been found on surfaces of hydrophilic gels, most recently by Gerald Pollack’s research team at University of Washington, Seattle in the United States (see [20] Water Forms Massive Exclusion Zones, SiS 23), which indeed excluded all solutes tested: including albumin, and pH sensitive dyes.

In addition, though not mentioned by Ling, PM is expected to be extremely good at resonant energy transfer over long distances, even better than bulk water at ambient temperatures, and to conduct positive electricity by jump conduction of protons (see [21] Positive Electricity Zaps Through Water Chains, SiS 28).

A cell with 80 percent water content would have polarized multilayers of water some 4 molecules thick that anastomose and surround the abundant cytoplasmic proteins such as those of the ubiquitous cytoskeleton. This is also precisely the thickness of the highly polarized water around proteins identified in Terahertz absorption spectroscopy within the past several years [22].

Surprisingly, an opinion review article published in 2005 stated [23]: “Recent progress in predicting protein structures has revealed an abundance of proteins that are significantly unfolded under physiological conditions. Unstructured, flexible polypeptide are likely to be functionally important and may cause local cytoplasmic regions to become gel-like.” This is another indication that Ling may well be right.

Ling sees his proposed ‘cardinal sites’ on proteins to include the ubiquitous receptor sites of cell biology, but going beyond them [4]. For example, ATP and 2,3 diphosphoglycerate (2,3 DPG), are essential for the action of haemoglobin, the iron-containing oxygen carrier protein in red blood cells. Binding of ATP and 2,3 DPG reduces the affinity of haemoglobin for oxygen, so that haemoglobin can deliver the oxygen to the lungs [24, 25]. ATP is therefore not the only cardinal adsorbent. Drugs, hormones, 2,3-DPG, Ca2+, and other potent agents at very low concentration may interact with cardinal sites to sustaining the resting living state of the protoplasm or bring about changes [16].

Thus, electronic induction is essentially the mode of action in cell [4]. The ‘cardinal adsorbents’ are electron-donating or electron-withdrawing. Induction happens via the polypeptide chain, which possesses a partially resonating structure as the peptide bond is 40 percent double bond and 60 percent single bond [26] (see Figure 3), and is therefore highly polarisable, enabling it to transfer energy and information over long distances [16].

As the PM water is highly ordered and polarized if not quantum coherent, I would expect it, too, to be equally adapt at resonant energy and information transfer, if not more so, and over the widely anastomosing networks that ultimately connect up the whole cell via the cytoskeleton.

Indeed, the major cytoskeletal proteins – actin, tubulin and intermediate filament proteins - polymerize into extended fibrous networks throughout the cell in the presence of ATP (GTP, guanosine triphosphate in the case of tubulin) [28, 29], and hence expected to support polarized multilayers of water. The cytoskeletal proteins are also all highly acidic, with glutamate and aspartate carboxylate side-chains and termini exposed and organised in clusters that are expected to show considerable preference for binding K+ over Na+ [7] in the resting polymerized state, not unlike the picture Ling had in mind. When stimulated into activity, the depolymerisation of the cytoskeletal proteins would release ATP or bound ADP and Pi, thereby bringing about a change in protein conformations that also alters the state of cell water, and with that, membrane depolarization and new chemistry due to influx of previously excluded solutes and ions [4, 7, 30] (The Importance of Cell Water, SiS 24).

 

[Keyhole]

The Fourth Phase of Water

The topic of structured water is discussed briefly in this thread, along with some considerations. For those of who are not familiar with the concept of structured water, I would highely recommend Gerald Pollacks book "The Fourth Phase of Water".

Below is also an interview presented the main points:

https://youtu.be/M3Sy1SZNebk

How does this link in with Gilbert Lings work? Ling was ostracized and his theories completely ignored by the scientists of his time, so there were very few people who could gather any experimental evidence as proof. Gerald Pollack was mentored by Ling, and has gone on to conclusively show that water has some amazing capabilities, very similar to what Ling hypothesised.

In short: Water acts as a battery for electromagetic energy. Water absorbs radiant energy (mostly infra-red light) and holds the capacity to transmit this energy in the form of electrons and protons to fuel the processes which drive living systems. What Pollack's team found was: When water makes contact with any hydrophillic (water-loving) surface, it begins to charge-separate. Charge separation in this context basically means that negatively charged electrons form a layer next of the surface, and that layer expels the positive charged protons so that they are separated. The term "exclusion zone" refers to the negatively charged section of the water because it acts to exclude all other substances.

The result looks something like this:

The negatively charged "exclusion zone" can be composed of potentially millions of layers. The structure of these layers are highly uniform, coherent, and structured honeycomb-like lattices of liquid crystaline water-gel. The consistency of this water literally changes from a liquid to a semi-solid gel, hence it's 'fourth phase'. So, the water in your body is NOT anything like the water in your glass, and interestingly does some interesting things. Since the exclusion zone is negatively charged and the surrounding water is positively charged, this creates and electrical current which is readily available as useable energy.

Again, the point that really is so important here is that the energy source that fuels the water battery is Light.

The body is predominantly made up of water. Light is what electrically energizes that water, and that energy is what is drives cellular processes in the body. We are no different to plants in that sense. Light is our source of energy. We are essentially beings of Light

Science is beginning to shed a whole new light on what the C's have said: "Love is Light is Knowledge"

For a brief review of this topic, I have included a short paper by Dr. Mae-Wan Ho below:

Put some water next to any hydrophilic (water-loving) surface and expose it to sunlight, or even light from an ordinary light bulb, and the water will charge up with electricity all by itself. This is the latest in a series of extraordinary discoveries about water from the laboratory of US bioengineer Gerald Pollack at the University of Washington in Seattle.

Water forms massive exclusion zones of ordered molecules next to gel surfaces

It began when Pollack and his student Zheng Jian-ming discovered that suspensions of colloids and dissolved substances are excluded from a region extending some hundreds of micrometres from the surfaces of hydrophilic gels. An ‘exclusion zone’ (EZ) of this magnitude is in direct contradiction to the generally held assumption that interfacial water forming at liquid-solid, or liquid-air interfaces can be no more than a few layers of molecules thick. Instead, what’s observed is a million layers or more.

Similar exclusion zones were found next to any hydrophilic surface including surfaces coated with a monolayer of hydrophilic molecules, and around ion exchange resin beads. Electric charge appears to be important, as EZ failed to form around charge-exhausted resin beads. Although EZ can form in pure water, it is enhanced and stabilized by low concentrations of buffer (2 to 10 mM at pH 7).

The EZ was characterized by several spectroscopic methods, all of which showed that it had features very different from the bulk water, suggesting an unusually ordered crystalline phase where the molecules are less free to move. The UV and visible absorption spectrum gave a single absorption peak at ~270 nm in the UV region, which is completely absent in the bulk phase. The infrared emission record showed that the EZ radiates very little compared with bulk water, as would be expected on account of the reduced mobility of water molecules. The magnetic resonance imaging mapping similarly gave a transverse relaxation time (T2) of 25.4 + 1 ms, which is shorter than the 27.1 + 0.4 ms recorded for the bulk water phase, again indicative of restricted motion.

Such coexistence of distinctly different phases has been demonstrated in 1999 in by Japanese water researcher Norio Ise and colleagues in Kyoto University using a dispersion of colloid latex particles in water and digital video recording. They captured a random phase, in which thermal motion of the particles is of the anticipated magnitude, right next to a crystal-like phase where the particles had separated regularly from one another by several micrometres and the deviations from their average positions are lower by an order of magnitude

Water electricity

Most surprisingly, Pollack and colleagues discovered that the EZ had a different electrical potential from the bulk phase, by as much as 100 – 200 mV, depending on the hydrophilic surface. With a negatively charged surface such as polyacrylic acid or Nafion (widely used as a proton exchange membrane), the potential is negative compared with the bulk water away from the EZ. Simultaneously, the hydrogen ion (proton, H+) concentration is high just outside the EZ, decreasing in a gradient away from it. This clearly indicates that the formation of the EZ is accompanied by a separation of positive and negative electrical charges, which led to the build up of electrical potential between the EZ and the bulk water. In effect, the water has become an electrical battery, and can provide electricity through an external circuit.

Separating H+ from e- (electron) is the first step of photosynthesis in green plants which provides energy for most of the biosphere. But where does the energy come from in the case of EZ? It turns out to have more in common with photosynthesis.

Light charges water

A clue came after having inadvertently left the experimental chamber with the EZ on the microscope overnight. Next morning, the EZ had shrunk considerably. But after turning on the microscope lamp, it began to immediately grow again, restoring itself within minutes to its former size. The energy for EZ formation comes from light, as in photosynthesis, but it can use the low energy part of the solar spectrum that photosynthesis cannot.

Although the entire spectrum of visible light appeared effective in making the EZ grow, the most effective part is in the infrared region, peaking at ~3 100 nm. A 10 minute exposure at that wavelength expanded the width of an EZ 3.7 times, and after an hour of exposure, the expansion was more than 6 times.

After the light was turned off, the EZ remained constant for about 30 minutes before beginning to shrink, reaching halfway to its baseline level in about 15 minutes.

When the UV and visible range was tested, a peak in the degree of EZ expansion was detected at 270 nm in the UV region, corresponding to the characteristic absorption peak of EZ that was identified before. However, as the optical power used in the UV and visible region was 600 times that in the IR, the most profound effect was identified in the IR region, particularly at 3 100 nm.

The mechanism of EZ formation is still unknown. But the two wavelengths that expand the EZ most effectively may offer some hint. The UV 270 nm is close to the 250 nm (~5 eV) required to ionize water under standard state conditions and taking into account the hydration of the resulting ions. The 3 100 nm peak, on the other hand is close to the OH stretch of the ring hexamer identified as the most abundant species in infrared predissociation spectroscopy of large water clusters, and also in neon matrices by infrared spectroscopy . These results suggest that photoexcitation of ring hexamers and photoionisation followed by ejection of protons play synergistic roles in the assembly of the EZ phase. Pollack and colleagues believe that the infrared radiation, though normally insufficient to break OH bonds, can nevertheless work via resonance induced dissociation of large hydrogen-bonded networks.
Implications of the findings

What do these findings mean outside the lab? The 3 100 nm IR source is about 0.6 percent of the sun’s overall energy, which is ~8.4 W/m2. By comparison, the power density of the LED light source used in the lab was 1.2 mW/m2, almost seven thousand times lower. Chai Binghua, Yoo Hyok and Pollack speculate that nature may contain a whole lot more EZ water than most people think. In other words, an appreciable fraction of the sun’s energy may be stored as charged EZ water. What this means for aquatic life is a large open question.

The earth is known to have a large negative surface charge, resulting in an electric field on the order of 100V/m at the earth’s surface. Perhaps this arises from the earth’s surface water under the influence of radiant energy from the sun.

Finally, the widespread occurrence of EZ within living cells and tissues is bound to have a drastic effect on bioenergetics. After all, organisms are energized by nothing more than the exquisitely orchestrated flows of electrons and protons that enable them to do everything it means to be alive.

 

[Keyhole]

Below are some sections of another paper by Mae-Wan Ho on the possible connections between collagen and the chinese medicinal meridian system via water channels. Fascinating research:

The Acupuncture System and The Liquid Crystalline Collagen Fibres of the Connective Tissues

According to traditional theory, the acupuncture system is an active circulatory system for mobilizing energy and for intercommunication throughout the body. So, it is unlikely to be completely understood in terms of the passive responses of skin conductances to electrodermal stimulation. The most promising functional correlate of the acupuncture system, as Becker (1990) suggests, is the direct current (DC) electrodynamical field that he and others have detected in the body of all organisms. This DC body field is involved in morphogenesis during development, in wound-healing and regeneration subsequent to injury. The direct currents making up the body field are not due to charged ions but instead depend on a mode of semi-conduction characteristic of solid state systems (Becker, 1961). The acupuncture points, moreover, may act as "booster amplifiers" of the very weak currents that typically flow along the meridians.

According to Becker (1990), the DC body field is not located in the nervous sytem itself, but in "perineural" tissues such as the glial cells in the brain and spinal cord, and the schwann cells encasing the peripheral nerves. This hypothesis would seem to conflict with the suggestion that the DC body field is correlated with the acupuncture system. The acupuncture system is clearly not directly associated with the perineural tissues, although it may have functional interconnections with the central and peripheral nervous system (Gunn, 1976; Wang and Liu, 1989; Pan et al, 1988). Also, an electrodynamical field can be detected in all early embryos and in plants and animals which do not have neural or perineural tissues (Burr and Northrup, 1935). It is likely that the DC field is functionally interconnected with the nervous system, and yet exists, to a large degree, outside the nervous system. In fact, it is widely recognized that under a variety of conditions, the speed of communication in our body is much faster than can be accounted for by the known speed of nerve conduction (see Ho, 1997a), and nerves simply do not reach all parts of our body.

We propose that both the DC electrodynamical field and the acupuncture system have a common anatomical basis. It is the aligned, collagen liquid crystalline continuum in the connective tissues of the body with its layers of structured water molecules supporting rapid semi-conduction of protons. This enables all parts of the body to intercommunicate readily, so the organism can function as a coherent whole. This liquid crystalline continuum may mediate hyperreactivity to allergens and the body's responsiveness to different forms of subtle energy medicine. Furthermore, it constitutes a "body consciousness" that is functionally interconnected with the "brain consciousness" of the nervous system (Ho, 1997a). We review supporting evidence from biochemistry, cell biology, biophysics and neurophysiology, and suggest experiments to test our hypothesis.


The organism is a liquid crystalline continuum

One requirement for an intercommunication system is a continuum which can carry the signals for intercommunication. For example, a continuum of air, liquid or solid, can all serve as medium for sound and mechanical waves. If the medium is electrically polarizable, it will also transmit polarization waves. Electromagnetic waves are thought to be an exception, as they can travel through empty space. But to this day, physicists are still debating the nature of the vacuum, which carries not only electromagnetic waves but also gravity waves (see Laszlo, 1995). The living organism is a continuum. Not only is the entire cell now known to be mechanically and electrically interconnected in a "solid state" (Clegg and Drost-Hansen, 1991) or "tensegrity system" (Ingber, 1993, 1998); all the cells in the body are in turn interconnected to one another via the connective tissues (Oschman, 1984, 1996).More accurately, perhaps, we recently discovered that the living continuum is liquid crystalline, with all the properties that make liquid crystals ideal for intercommunication (Ho et al, 1996; Ho, 1997a).

Liquid crystals are states or phases of matter in between solid crystals and liquids, hence the term, mesophases. Unlike liquids which have little or no molecular order, liquid crystals have orientational order, and varying degrees of translational order. But unlike solid crystals, liquid crystals are flexible, malleable, and responsive (De Gennes, 1974; Collings, 1990). There are many kinds of liquid crystals, from those which are most like liquids, to ones that most resemble solid crystals. Those that are like liquids can flow in the way water does, and even though all molecules tend to be aligned in one direction, individual molecules can move quite freely and change places with one another while maintaining their common orientation. The ones that resemble solid crystals will have order in all three dimensions, and molecules may even be extensively covalently cross-linked together, but they will remain flexible and responsive.

Liquid crystals typically undergo rapid changes in orientation or phase transitions when exposed to electric (and magnetic) fields - which is why they are widely used in display screens. They also respond to changes in temperature, hydration, shear forces and pressure. Biological liquid crystals carry static electric charges and are therefore also influenced by pH, salt concentration and dielectric constant of the solvent (Collings, 1990; Knight and Feng, 1993).George Gray (1993), who has studied liquid crystals for many years, refers to liquid crystals as "tunable responsive systems", and as such, ideal for making organisms.

It is already widely recognized that all the major constituents of living organisms may be liquid crystalline (Collings, 1990) - lipids of cellular membranes, DNA, possibly all proteins, especially cytoskeletal proteins, muscle proteins, and proteins in the connective tissues such as collagens and proteoglycans (Bouligand, 1972; Giraud-Guille, 1992; Knight and Feng, 1993). Recent nuclear magnetic resonance (nmr) studies of muscles in living human subjects provide evidence of their "liquid-crystalline-like" structure (Kreis and Boesch, 1994). However, very few workers have yet come to grips with the idea that organisms may be essentially liquid crystalline.

The importance of liquid crystals for living organization was actually recognized a long time ago, as pointed out by Joseph Needham (1935). Hardy suggested in 1927 that molecular orientation may be important for living protoplasm, and Peters, two years later, made the explicit link between molecular orientation and liquid crystals. Needham, indeed, proposed that organisms actually are liquid crystalline. But direct evidence for that has only recently been provided by Ho and coworkers ( Ho and Lawrence, 1993; Ho and Saunders, 1994; Ho et al, 1996). who successfully imaged live organisms using an interference colour technique that amplifies weak birefringences typical of biological liquid crystals. They further discover that all organisms so far examined are polarized along the anterior-posterior or oral-adoral axis, so that when that axis is properly aligned, all the tissues in the body are maximally coloured; the colours changing in concert as the organism is rotated from that position. Not only live organisms, but also fresh-frozen or well-fixed sections of the skin, cartilage and tendons, all exhibit the same brilliant interference colours typical of living organisms.

Collagens and Intercommunication

There are many kinds of collagens, all sharing a general repeating sequence of the tripeptide, (gly-X-Y) - where X and Y are usually proline or hydroxyproline. They also share a molecular structure in which three polypeptide chains are wound around one another in a triple-helix, with the compact amino acid glycine in the central axis of the helix, while the bulky amino-acids proline and hydroxyproline are near the surface (Van der Rest and Garrone, 1991).In the fibrous forms, the triple-helical molecules aggregate head to tail and side-by side into long fibrils, and bundles of fibrils in turn assemble into thicker fibres, and other more complex three-dimensional liquid crystalline structures. Some collagens assemble into sheets constructed from an open, liquid crystalline meshwork of molecules. All these structures are formed by self-assembly, in the sense that they need no specific "instructions" other than certain conditions of pH, ionic strength, temperature and hydration. The process seems to be predominantly driven by hydrophilic interactions due to hydrogen-bonding between water molecules and charged amino-acid side-chains (Leikin et al, 1995). However, the precise mesophase structures resulting from different conditions of self-assembly show endless variations (Zhou et al, 1996; Haffegee et al, 1998). The different kinds of collagen assemblies in different connective tissues are generally well-suited to the mechanical tasks performed by the connective tissue concerned, because they were shaped by the prevailing conditions and the relevant mechanical forces.

Recent studies reveal that collagens are not just materials with mechanical properties. Instead, they have dielectric and electrical conductive properties that make them very sensitive to mechanical pressures, pH, and ionic composition (Leikin et al, 1993, 1995),and to electromagnetic fields. The electrical properties depend, to a large extent, on the bound water molecules in and around the collagen triple-helix. X-ray diffraction studies reveal a cylinder of water surrounding the triple-helix which is hydrogen-bonded to the hydroxyproline side-chains (Bella et al, 1994). Nuclear magnetic resonance studies have provided evidence of three populations of water molecules associated with collagen. These are interstitial water, very tightly bound within the triple helix of the collagen molecule, and strongly interacting with the peptide bonds of the polypeptide chains; bound water, corresponding to the more loosely structured water-cylinder on the surface of the triple helix; and free water filling the spaces between the fibrils and between fibres (Peto and Gillis, 1990). Evidence for bound water in collagen also comes from studies using another popular physical measurement technique, Fourier Transform Infra Red (FTIR) spectroscopy (Renugopalakrishnan et al, 1989).

The collagenous liquid crystalline mesophases in the connective tissues, with their associated structured water, therefore, constitutes a semi-conducting, highly responsive network that extends throughout the organism. This network is directly linked to the intracellular matrices of individual cells via proteins that go through the cell membrane. The connective tissues and intracellular matrices, together, form a global tensegrity system (Oschman, 1984; Ingber, 1998), as well as an excitable electrical continuum for rapid intercommunication throughout the body (Ho, 1997a).
[..]

Conclusion

We have proposed that the acupuncture (meridian) system and the DC body field detected by Western scientists both inhere in the continuum of liquid crystalline collagen fibres and the associated layers of bound water that make up the bulk of the connective tissues of the body. Acupunture merdians may be associated with the bound water layers along oriented collagen fibres, which provide proton conduction pathways for rapid intercommunication throughout the body; while acupuncture points may correspond to gaps in the fibres or fibres oriented at right angles to the surface of the skin. The sum total of the electrical and electromechanical activities of the liquid crystalline continuum constitutes a "body consciousness" that works in tandem with the "brain consciousness" of the nervous system.

 

[Keyhole]

So, what does Dr. Kruse say about all of this?

Did you know sunlight is life’s main battery?

...Sunlight is all that is need to charge separate water to create and negative and positive charge that the Earth’s magnetic field lines up and then the electric charges become controlled by the electromagnetic force. Sunlight alone can make a semiconductor supercharged. This is precisely how photovoltaic cells work. Life di

Gerald Pollack and colleagues discovered that water structured as massive exclusion zones on hydrophilic surfaces not only have a high degree of (liquid crystalline) order, but also a large negative electric potential resulting from a macroscopic charge separation so that an excess of protons end up outside the exclusion zone. And it is sunlight (photoelectric effect) that causes the charges to separate, providing an instant ‘water battery’ for energizing life.
[..]
These actions occur simultaneously to allow water to become coherent for energy transfers that all power the biochemical reactions we all learn about. To understand the concept of coherence, stop for a moment and think about light. A light bulb in your lamp turns light on in your room so you can see, but a laser beam is a stream of focused photons that can cut through a diamond. At their core, both are just made of the same thing, light. But how they are structured changes their physical capabilities. The same thing happens to water, collagen, and proteins in your quantum cell. Water in a cell, also has some of the unusual properties that a laser has and your lamp bulb does not. ATP is made from electrons from food and those electrons originally came from the sun’s light. Water and protein contains protons to provide energy to this water semiconductor. In this way, ATP electronically induces water to polarize and animate life. This is what Gilbert Ling said in 1952. No one heard him.

In the last 55 years guess what biology has found? This is exactly how plants do it too, but on chloroplast membranes. The quantum chemistry uses different proteins but the mechanism of action is the same. It turns out humans have also been found to use quantum electrodynamic principles too, in bone, eye sight, and along their inner mitochondrial membranes in those 55 years. Since Ling’s theory, biophysicists have now experimentally proven that water in polarized in this fashion happens to be extraordinarily good at being able to conduct resonant energy transfers over long distances. Remember the electromagnetic force is the strongest natural physical force, and it has infinite range of action. Polarized water is also excellent at conducting positive electricity (protons) by allowing protons to “jump conduct”. It has been shown that polarized water can allow proton migration along its hydrogen bonding network 40 times the capacity found in bulk water that is not polarized by these peptide binding sites.

Ling experimentally found found that ATP’s main function is not that of a high energy substrate when it is hydrolyzed, as modern cell theory teaches us. ATP is designed to unfold proteins fully to open their carbonyl and imino side chain groups to intracellular water, to allow binding and polarization to separate water into subatomic particles that are positively and negatively charged. This allows water to form polarized layers and the Earth’s magnetic field then orients these polarized crystals to allow for the formation of massive super conducting proton cables all over your body. This gives you alternating positive and negative poles around these proteins. He found that the orientation of positive to negative water molecule binding was 3.1 Angstroms apart when theses conditions are met. These alternating charged poles ADSORB water and polarize and orient the water correctly for super conduction. This is where the main source of energy in a cell comes from. It is not from the hydrolysis of ATP.

 

[Keyhole]

Another recent paper highlighting the possibility that humans may be "photosynthetic"

Title: The role of human photosynthesis in predictive, preventive and personalized medicine

The discovery of the intrinsic property of melanin to dissociate and re-form the water molecule, a fact previously unknown, may be a factor that significantly facilitates the integration of current knowledge in relation to the sequence following biomolecules in an organism alive.

So far no reaction could consider some intracellular as number 1 or very first of all, but have identified the process very similar to the first reaction of plants implies a breakthrough in this regard. In plants, the first reaction of photosynthesis is through dissociation of the water molecule by chlorophyll, a reaction that is irreversible, since the oxygen is expelled into the atmosphere. The reaction is outlined as follows:

2H 2 O → 2H 2 + O 2

And it is considered the world's most important reaction since it is the beginning of the food chain. Therefore, a plant without water will not hatch, since the free chemical energy that is released with the breakdown of the molecule of water is essential to boost consequential reactions finally reaches the fusion of CO2 and H2O into glucose, a process that unable to replicate in the laboratory. We could say that every last leaf of the tree stems depends on and is governed by photosynthesis.

Our discovery of the intrinsic property of the Melanin molecule to dissociate and re-form the water molecule breaks the paradigm, humans also have the amazing ability to transform the photon energy into chemical energy free [4], and the reaction is outlined in the following form:

2H 2 O ↔ 2H 2 + O 2 + 4e -

Melanin is thousands of times more efficient to dissociate the water molecule of chlorophyll, it suffices to note that chlorophyll does so irreversible and can only use purple and red light, visible both, for our side, melanin absorbs the entire electromagnetic spectrum, apart from splitting water, also has the amazing ability to re-shape it, which is a unique example in nature. And just as in the plants until the last leaf of the tree stems, depends on and is governed entirely by photosynthesis, in humans is the same.

That is why we think we can assign as number 1, the dissociation reaction of water molecule also in humans. And in doing so, the cloud of unknowns surrounding the self-sustaining chemical system we call life, so substantially modified. Well now it has a beginning, and the intrinsic property of melanin to dissociate the water molecule has the appropriate requirements for considering the ab initio life [5].

So the real source of energy of the eukaryotic cell is water, so the sacred role of glucose as an energy source now breaks into a thousand pieces. We ended up saying that if the energy source was glucose, diabetic patients would fly.

The human body with four billion years of evolution is far beyond our ability to abstraction, but in origin the body is relatively simple: everything comes, everything is soaked, and everything is governed by photosynthesis, both in plants and in us.

If we want to maintain health, the answer is also simple: just keep the balance equation.

2H 2 O ↔ 2H 2 + O 2 + 4e -

 

[Keyhole]

• Light as fuel for the cell
  
  Below I have summarised the information from the past few posts. Apologies it was pretty dense reading, but this information is pretty fascinating. I have tried simplify some of the main points so that everyone can understand exactly what this research means:
  
  • According to Gilbert Ling's calculations, ATP could not possibly provide enough activation energy for biochemical reactions. He hypothesised that life was animated by electrical induction, and that water played a key role in this process
  • Gerald Pollack's recent work on water definitively shows that water is an electrical battery when in close proximity to hydrophillic surfaces
    
  • In the presence of radiant energy (mostly Infra-Red light), water splits into a negatively charged zone (abundant electrons) and a positively charged zone (abundant protons). This is the water battery.
    
  • Water forms a liquid crystalline matrix, which can function as an N-type semiconductor (similar to Robert O Becker's work on bone)
  • Both positive and negative charges can be used as a source of electrical energy by the surrounding environment
  • This electrical energy from light is the actual fuel for the cell. Not ATP from food
  • ATP's real function is not as an energy substrate. ATP is tool the body uses to maximally unfold proteins to expose sidechain water-binding sites. When water binds to hydrophillic surface of protein - the EZ build up begins and electrical energy is transferred in the form of protons and electrons
  • Collagen is the most abundant protein in the body, and possesses electrical qualities which allow it to semi-conduct and transfer energy at much more efficient speeds than neuronal communication.
  
  Seasonal changes/ Food and Light as information
  
  Food seems to be natures way of codifying light energy/information into a condensed package, to allow the body to further extract and organise the information into a more complex, coherent system. Seasonal fluctuations carry with them different information, and it is the body's job respond to this changes in the appropriate manner.
  
  Natural Infra Red light photon intensity is greatly increased in the summer months, therefore provides the body with an abundant source of energy via EZ water. This is probably why people 'feel great' in the summer, and don't often become sick.
  
  In the winter however, IR levels are lower. Low IR = Smaller exclusion zones in water = Lower energy yield.
  
  So how do we get energy?
  
  The role of Nutritional Ketosis : In contrast to carbohydrate metabolism (which yields 36 ATP), beta-oxidation of fats yields a total of 147 ATP. To make up for the lack of IR light, the body produces more ATP to unfold more proteins to create more EZ, and this is the natural function of nutritional ketosis. It is designed to work in cold and low light environments to compensate for the lack of Light! In essence however, eating fat does not provide the body with energy. Eating fat simply allows the body to make use of what little light it manages to get. This means that even in the winter light is very, very important for all diseases and maintaining health.
  
  Light information is encoded in food and is different depending on which time of year it was grown in. This may shine light on why eating foods out of season may cause a mismatch in the system. Below is an excerpt from Kruse's Energy and Epigenetics 10 blog post and for simplicity I have summarised some of the main points that I took from it:
  • Food is fundamentally a carrier of information in the form of photons and electrons, and the way in which the body decodes this information is controlled by electromagnetic forces detected by mitochondrial cytochrome complexes
  • On the mitochondrial membrane are protein complexes called cytochromes. Cytochrome's functions are to facilitate oxidation-reduction reactions which allow electrons to pass into the mitochondria to produce ATP
  • The electromagnetic force is stronger in summer: High powered photons energize electrons in foods grown in long light cycles (e.g fruit) via the photoelectric effect. Therefore foods grown in summer time contains 'high energized' information.
    This high energy signal (summer time carbohydrate) is detected and then initiates release of insulin by the pancreas.
    Once insulin is made, food electrons are shuttled to NADH at cytochrome complex 1 to produce 36 ATP. Fatty acid oxidation is prevented by insulin, so we are limited to burning sugar.
    
  • Electromagnetic force is weaker in winter: Low light levels mean less photon power in food sources, and food is naturally sparse. The only food available is low-photon powered electron dense fat and protein. When we starve (ketosis), electron current of flow slows down at Complex 1, and cold temperatures terminate the insulin receptor. Free fatty acids are liberated from adipose stores and the metabolised electrons begin to flow through mitochondrial complex 2 via FADH2. This is otherwise known as burning fat.
    
    When the environmental EMF are increased (WiFi, cell phone, artificial light at nighttime), one way the mitochondria respond to these energies is by producing excessive NADH! NADH is the mitochondrial redox chemical associated with carbohydrate metabolism, not fat metabolism. Therefore, by producing more NADH, it is providing your mitochondria with "summer electrons" even if it is winter time.
  
  

  The electromagnetic force changes as seasons change. This powers the energies of electrons in foods up or down depending upon the season the food grows in. It turns out this is precisely how insulin evolved and is regulated in our mitochondria. It is tied to “where” electrons and protons are being fed into the chain. When electromagnetic energies in the environment are altered, we appear to harbor two basic possible mechanistic states that the electron transport chain can choose between based on the two states we face.
  
  1. No food and a subsequent lack of electrons and increased protons from fat storage,
  2. or an excess of food, with the result of too many electrons or too much energy from photons and a lot of protons.
  
  Therefore the electron transport chain has to have a built-in mechanism to deal with both situations. This is just like a simple circuit being controlled on a laptop semiconductor chip. When we starve, we have poor electron flow or current and very few electrons enter in cytochrome 1. Insulin’s action would be low during this time.
  
  In the mitochondria at complex 1, when the current is low, we deliver plenty of endogenous electrons from FFA to flow through the FADH2 input at cytochrome 2. This happens through the action of electron transporting flavoprotein dehydrogenase coming from the first step of beta oxidation of real fats from our fat stores. For example, this could be a fatty acid like palmitic acid.
  When food is sparse in winter, the current of flow is low, and it is near impossible to generate reverse electron flow through complex 1, so activation of insulin signalling is rapidly aborted by the continuing action of tyrosine phosphatase. This yokes insulin action to environmental temperatures. The photoelectric current signals phosphorylation of pathway proteins to change “where electrons” enter our mitochondria.
  
  I told you 2 years ago food clearly has a quantum electron effect. Most biochemists and those in the paleosphere fail to realize the effect is tied to the electrons’ energy state and nothing else. Foods grown in longer light cycles have higher energized electrons and they are handled very differently than electrons from low light level foods because of where they enter the electron transport chain in our mitochondria. Our mitochondrial cytochromes are proteins that can decipher the differences in energies, and this why they enter the ETC at different cytochromes and provide different levels of ATP and oxygen generation. Here you can begin to see how the electromagnetic force directly impacts the proteins in the insulin signaling pathway.
  
  The next possible state a cell can face is when the light cycle is long and electrons are present from foods. This is the state when insulin levels would be high. The electron chain then alters its functioning under the influence of insulin. Since the electromagnetic force is stronger in summer, and those photons can energize the electrons created from food, where they enter the ETC is at cytochrome 1. This is a different situation than electrons from food face in winter, when the electrons are more numerous but not well energized. The mitochondrial proteins of the electrons chain are designed to “catch” these electrons and they can “sense” the difference in the energy and the environmental information contained within these electrons. Any protein that catches electrons or protons is called a Maxwell demon. Generally these are coded for by DNA and RNA.
  
  How is insulin’s action quantized?
  When energies of electrons are higher because of the action of the photons of the sun, that signal is transduced by the cytochromes in the electron chain transporter. The energy is given off to these mitochondrial proteins and this causes specific phosphorylation of these proteins to alter their ability to function.
  This means that the highly energized summertime electron signal is coded for by the hormone insulin. When these types of electrons are sensed, insulin is made by the pancreas. When insulin is made, we see electrons being shuttled to complex 1 of the ETC, with a resultant large supply of NADH also being made at complex 1. When this occurs, we also have a restricted supply of fatty acids being delivered to our mitochondria from our fat cells because of the action of insulin on adipocytes. When this happens, it generates a high membrane voltage. This voltage is a charged energy that the electromagnetic force controls.
  If you watched the electromagnetic force video, you see that the electromagnetic force controls particles of atoms when they carry a charge. Protons have a positive charge and electrons have a negative charge. These are the particles that the force acts upon in our mitochondria.
  Ling was 100% pre-occupied with finding out where the high membrane voltages came for in life because he knew they were quite important for many processes. He was the first to find out that it was not due to the membrane pumps that biochemistry still thinks is the source. It is a function of Lady Evolution’s semiconductor design. Life’s battery is all about the charge separation of water.
  
  This voltage is what the electromagnetic force pays deep attention to, as I mentioned to you in Energy and Epigenetics 6. This voltage is directly linked to the cell’s ultimate redox power. When the voltages are high in membranes anywhere, but especially in the mitochondria, the result is a “relatively stronger current of electrons down the ETC via complex 1. Just like the vortex in the CSF is bidirectional for sleep, so is the current of flow in mitochondria of electrons from food. Because the current is strong in one only direction during summer, no reverse electron flow can happen at complex 1 because there is a minimal electron current simultaneously occurring via electron transporting flavoprotein dehydrogenase’s FADH2 at complex 2. This is how we store excess electrons, or highly energized electrons, which are elevated in their energies by the photoelectric effect of the summer light’s power in fat stores. When the electromagnetic force is stronger in your environment from non-native sources, the results can be easily explained using the above two paragraphs. Non-native EMF causes us to make excessive NADH in our mitochondria.
  
  After the electronic signal has been produced in a cell, termination of signaling is then needed. Insulin is degraded by endocytosis and degradation of the receptor bound to insulin as a main mechanism to end signaling. It turns out at the center point of insulin molecular structure is an atom of Zinc, a transition metal, surrounded by 4 specific amino acid residues. The interaction of the electromagnetic force and the interaction of Zinc and these specific amino acid residues causes a change in the electronic signal to induce dephosphorylation in insulin. This removes energy from electrons or it removes electrons from these proteins to induce dephosphorylation.
  
  If you watch the electromagnetic force video you will see semiconductor engineers add phosphate to silicon wafers to increase the sheer numbers of electrons to the silicon backbone to pre-load it for more optimal functioning. This makes an “N type” semiconductor. An N type semiconductor is negative because the added electrons from phosphate have a negative charge. The more phosphate you pre-load a semiconductor with, the more negative charge you get. In our excitable cells, our back bone of our semiconductors are not made of silicon, but of carbon surrounded by water. Being a bit more specific, our backbone is the triple helix of collagen surrounded by an ocean of intracellular water in our quantized cells to generate life. Water also happens to be the “N type” semiconductor. It collects electrons from all sources and distributes it throughout our cells and organelles. Health is a function of how many electrons your semiconductors have.
  
  Getting rid of insulin’s actions in a quantized fashion?
  The signaling of insulin is terminated by dephosphorylation of these tyrosine residues inside of insulin’s molecular structure. The process of dephosphorylation is tied to the flow of electrons on the tyrosine residues by tyrosine phosphatases. We have known for some time that serine/threonine kinases will also reduce the activity of insulin, but few people have realized how the control of electrons dictates the mechanism of action. This is a quantum effect on these electrons.
  It turns out that cold temperatures have the exact same effect on these residues by inducing the Hall effect on electrons. This helps explain why Gilbert Ling found in 1969 that insulin action on D-glucose varies inside of cells when the temperatures falls below 62 degrees F.
  
  The final action of insulin termination is associated with the reduction of the number of receptors on the plasma membrane. When cold is present or electronic induction altered, there is a decrease in the amount of insulin receptors present in our cell membranes which also brings to a termination of insulin signaling. This defines physiochemical thermoplastic control of a biologic response I spoke about long ago in the Cold Thermogenesis 6 blog post. This is an example of how the same molecular key can open both the door to heaven and the gates to hell depending upon the context in which the “key” is found.
  
  KEY POINT: If you are following this blog well, we would expect to see higher levels of NADH being delivered and developed in our mitochondria when non-native EMF is present to an excess. It would simulate a constant season of “summertime electrons” to our mitochondrial proteins 24/7. When we starve, we use our own fat stores to make ketones, which act to drop NADH levels because we are using protons at FADH2 and electrons at cytochrome 2. So this simply explains why non-native EMFs make you think you need carbs but also stimulate that need in the signaling mechanisms of your mitochondria proteins.
  
  This should explain to you what I wrote in the EMF 4 blog post now. It also explains why and how uncoupling proteins work in mitochondria. They are “Maxwell demons” who pay deep attention to the energies in the electrons and photons delivered to the inner mitochondrial membranes. When energy is high we should be able to uncouple to get rid of excess electrons or their energies as free heat. So uncoupling naturally increases when our mitochondrial membranes sense a higher voltage for any reason. This is why we burn free heat when we are healthy. It is also why our core temperatures are so linked with how well or ill we are clinically. The story is a bit more complex with uncoupling proteins because we can actually use insulin to uncouple in our species too!
  
  The electromagnetic force also turns on and off melatonin via the action of electrons contained in melanopsin in a similar manner. When this happens, quantum sleep is induced as I posted in Energy and Epigenetics 9. It is made most efficient when we are cold, ketotic, reduced. The cell becomes reduced by making large amounts of glutathione when melatonin is high in the absence of the electromagnetic force of light. Glutathione is the main chemical that provides for all redox reactions in the body. This means the redox potential is 100% tied to your ability to live a long life healthy.
  
  When you begin to understand how electrons are handled, you begin to see why biology has missed how insulin really acts in different electromagnetic fields. It is 100% tied to the electric field and magnetic field that is surrounding the organism. These fields always vary, especially between light and dark periods and within seasons.
  
  How electrons work from food seems to offend the “common sense of biology.” I find this concept to be a very good thing because the the principles of relativity, quantum mechanics and quantum vortices in black holes also offend biology. This is the way nature works in us, and across the whole universe.

 

[Keyhole]

Water holds Light energy and can fuel biochemical reactions when the cell is hydrated. When the cell is dehydrated, the current flow of energy stops. So what causes dehydration?


In short: Blue light, nnEMF, and dietary inflammation


This post will attempt to lay out the mechanisms behind intracellular dehydration. The most important take-home message that needs to be emphasised is that artificial light at night time and nnEMF exposure is equivalent to eating a high sugar diet 24/7. At the level of the mitochondria, the effects are exactly the same.

The post might seem complex at times, but is going to attempt to shine light on some new concepts. For external consideration I will summarise the main points below. I appreciate that the majority of people do not want to read the exact mechanisms behind these processes, but for those who are interested I will lay it all out from what I could understand. I'm not sure I got all of it down, but I have tried to make sense of some of the main concepts and will attempt to place them in an understandable format for those with little/no biology background. So beware that this is extremely simplified and may possibly be ‘butchered’ in parts. I have been studying this pretty much two weeks solid to make any sense out of it, so I apologise if anything is off-point.


Here are the main points that everyone should be able to understand:

How nnEMF/Blue light/Inflammation dehydrate the cell and lower redox potential

• Waters exclusion zone is a battery that holds the electrical capacity to fuel biochemical reactions. The exclusion zone forms when water touches a hydrophilic surface and is built by Infrared electromagnetic energy.
  
• In order to utilise this function of water:
  1. There must be sufficient amounts of water present
  2. There must be sufficient IR generated in the mitochondria to build EZs.
  3. Protein must remain hydrophilic and retain the ability to bind with water
  
• Non-native EMF (via calcium efflux), artificial blue light, and inflammatory/poor diet generate Reactive oxygen species (ROS)
• Non-native EMF and artificial blue light cause mitochondrial swelling via the permeability transition pore: this causes electrons to leak out, lowers DeltaPsim (mitochondrial membrane potential), and increases distance between respiratory proteins simultaneously
• Excessive ROS lowers electron flow in the mitochondria to lower ATP production.
• Low ATP prevents proteins from unfolding to expose water binding sites, water cannot bind.
• Redox potential diminishes
• Altered protein unfolding liberates transition metals from proteins, preventing them from functioning effectively and diminishing hydrophilicity.
• Chronic oxidation depletes glutathione/cysteine stores.
• Low glutathione/cysteine leads further oxidation and metal accumulation.
• Fenton reactions generate hydroxyl radicals, which further damage cell structures via oxidation. The cell systematically gets destroyed
• Transition metals absorb nnEMF, dehydrate cellular water further via reducing dielectric constant and destroying hydrogen bonds.
• Water is unable to bind to unzipped protein. Low redox potential is unable to counteract chronic oxidation and build exclusion zone. Free energy can no longer be transferred via water. This state is called intracellular dehydration
• Energy deficit occurs = low pH/acidic environment where proton quantities outweigh electrons = serious inflammation
• Cell death (apoptosis) is the only option for the cell since recycling (autophagy) cannot be initiated. This state depletes stem cells, reduces telomere length. State of oxidation/dehydration = aging and disease generation.
  

How it happens

Calcium Efflux

Calcium ions are essential biological signalling molecules involved it a variety of functions. They are released from a cellular component called the endoplasmic reticulum. This release is controlled by voltage gated calcium channels (VGCC’s). These are small channels which respond to electrical voltage stimulation. Evidence shows that electromagnetic frequencies interact with VGCC’s to abnormally trigger a surge of calcium to flow into the intracellular space.

Expert Martin Pall states in areview of EMF's effect of VGCC’s

• Twenty-three different studies have found that such EMF exposures act via activation of VGCCs, such that VGCC channel blockers can prevent responses to such exposures (Table 1). Most of the studies implicate L-type VGCCs in these responses, but there are also other studies implicating three other classes of VGCCs.
• Both extremely low frequency fields, including 50/60 cycle exposures, and microwave EMF range exposures act via activation of VGCCs. So do static electric fields, static magnetic fields and nanosecond pulses.
• Voltage-gated calcium channel stimulation leads to increased intracellular Ca2+, which can act in turn to stimulate the two calcium/calmodulin-dependent nitric oxide synthases and increase nitric oxide… It is also suggested that nitric oxide may act in pathophysiological responses to EMF exposure, by acting as a precursor of peroxynitrite, producing both oxidative stress and free radical breakdown products.

Some more evidence of this can also be found in the following studies: 1, 2,3, 4, 5, 6, 7,

Increased intracellular calcium mediates a few effects:

[list type=decimal]
[*]Stimulates the synthesis of Nitric Oxide, which is the precursor for peroxynitrite that then can easily generate ROS.
[*]Phosphate is required for calcium loading in the mitochondria, so calcium accumulation causes a build up of phosphate outside of the mitochondria.
[*]Altered calcium homeostasis drastically affects magnesium homeostasis and depletes magnesium stores. Supplementing magnesium probably does little to fix this, however. It also causes increased inflammatory cytokine production. All organs are affected by altered calcium homeostasis.
[*]Increased levels of calcium cause the mitochondria to swell and subsequently leak electrons via the permeability transition pore.This increases the distance between respiratory cytochrome proteins on the membrane (which lowers rate of electron flow), lowers DeltaPsim (membrane potential) and eventually causes apoptosis (cell death).
[/list]

One of these effects is that Calcium efflux has been shown to cause phosphate accumulation at the mitochondria:

Isolated mitochondria from a variety of sources possess a large but finite capacity to accumulate and retain Ca2+. When this limit is exceeded, mitochondria assemble a pore in their inner membrane that is non-selectively permeable to ions and solutes up to 1.4 kDa (for review see Ref. 3). It is unclear what exactly defines Ca2+ overload and how this triggers the permeability transition. Phosphate (Pi) is required for massive Ca2+ loading of the matrix and a variety of evidence suggests that a calcium phosphate complex is formed within the matrix once about 10 nmol of Ca2+/mg has been accumulated. First, phosphate is required for extensive matrix Ca2+ loading that can exceed 1 M total Ca2+concentration before swelling can be observed

Source

And so what effect does phosphate accumulation have on the cell? It is interesting to note that increased intracellular phosphate has been shown to causes the cell to accumulate transition metal ions:

We report here that pho80 mutants specifically elevate cytosolic and nonvacuolar levels of phosphate and this in turn causes a wide range of metal homeostasis defects. Intracellular levels of the hard-metal cations sodium and calcium increase dramatically, and cells become susceptible to toxicity from the transition metals manganese, cobalt, zinc, and copper. Disruptions in phosphate control also elicit an iron starvation response, as pho80 mutants were seen to upregulate iron transport genes. ~ Source

In cells, there exists a delicate balance between accumulation of charged metal cations and abundant anionic complexes such as phosphate. When phosphate metabolism is disrupted, cell-wide spread disturbances in metal homeostasis may ensue. The best example is a yeast pho80 mutant that hyperaccumulates phosphate and as result, also hyperaccumulates metal cations from the environment and shows exquisite sensitive to toxicity from metals such as manganese. ~ Source

Keep in mind that calcium efflux leads to metal accumulation because we will return to it later on. First we should focus on calcium efflux’s ability to generate free radicals (ROS).

Reactive oxygen species

ROS are powerful signalling molecules used by the body and play key roles in cellular communication and homeostasis. Their function is to “oxidise” (or reduce) molecules/atoms they come into contact with. Oxidation is when one molecule/atom “steals electrons” from other atoms/molecules. Oxidants are usually missing an electron from their outer shell (therefore house an un-paired electron), so search vigorously to take an electron from another structure in order to be ‘complete’. When the atoms contained in molecules are oxidised, it alters the structure of that molecule so that it can no longer function properly. This is called “oxidative stress”. On the other hand, “reduction” refers to the giving of electrons to another molecule. If a molecule is chemically reduced, it means that it has been given electrons by another molecule. An antioxidant is a substance characterised by its quality of having an extra electron (or more) that it can donate to oxidised molecules to restore their function. This is why antioxidants are so effective – they counteract the damaging effects of oxidation. This chemical reaction is known as an “oxidation-reduction reaction”. The efficiency and balance of these processes in the body is referred to as the “Redox potential”.

So, when a substance is oxidised, its charge is also altered. Protons are positively charged, and electrons are negatively charged. In the case of oxidation, a substance becomes less negative and more positively charged. In the case of reduction a substance becomes more negatively charged and less positively charged. One interesting piece of information is that all inflammation in the body is positively charged, meaning there are an abundance of protons at the site that is inflamed.

So, back to ROS. There are a variety of reactive oxygen species produced by the body for various reasons, and most of them can be neutralized by other molecules. For example, the ROS superoxide can be neutralized by the enzyme superoxide dismutase. However, there is one particularly dangerous variety of ROS that can not be neutralized by the body… it is known as the Hydroxyl free radical and is produced by a Fenton reaction. The hydroxyl radical is highly reactive and has a short half life, can react with practically any structure, and the reaction is exothermic (produces heat). It is usually produced as part of our immune system by the macrophage cells which fight off disease, and as a general rule, is not often meant to be produced otherwise. However, because we cannot contain this reaction enzymatically, when it IS produced it wreaks complete havoc on cellular structures and causes irreversible damage. This means that we need to expend more energy by recycling those damaged cellular components in order to remain metastable – at the detriment of other cellular processes which also require energy. Remember, oxidation DECREASES electrons. Read the past few posts before this current one: electrons are very important for maintaining the “redox potential” to build the water-battery’s exclusion zone to power all of life.

ROS in the cell begin to attack mitochondria, DNA, RNA, proteins and every other structure.

Some factors that generate ROS:

• Inflammation via poor diet and altered circadian rhythm - abnormal hormonal cycles (e.g cortisol rhythm)
• Artificial blue light on the surfaces of the skin and in the retina
• Calcium efflux via nnEMF – very important

At the level of the mitochondria

Mitochondria are designed to utilize electrons from food and light input, passing them across the inner mitochondrial membrane (via electron chain transport), to generate ATP and heat (infra-red energy). The output here is a steady stream of protons from the mitochondria. Within these protons is stored potential energy which can then be transferred to water hydration shells surrounding the mitochondria and other proteins . The exclusion zone of water consists of a negatively charged EZ, and positively charged hydronium ions. The stored potential energy of protons is stored in the hydronium ions. In order for these proton’s potential energy to be utilized, sufficient water must be available to build an exclusion zone. If there is insufficient water in the cell, mitochondrial protons have nowhere to go, and begin to build up in and around the mitochondria. Protons are positively charged, and in a solution are measured as the pH value. A low pH means something is more acidic. The proton accumulation causes the local/surrounding pH to fall, which acts as a signal to the mitochondria that there is rising inflammation in the cell. The response is an increase in ROS/RNS synthesis.

Mitochondria make ATP by funnelling electrons through a process called electron chain transport (ETC). ETC utilizes both electrons a protons and is facilitated by a variety of molecules situated on the inner mitochondrial membrane, including four respiratory complexes.

Here, we will focus on respiratory complex 1 (NADH:ubiquinone reductase). Understand that all food is broken down to electrons to be transported to the mitochondria. It begins with breaking down macromolecules into their constituent subatomic particles. For example, glucose is metabolized by the body via glycolysis reactions. The first step of glycolysis occurs outside the mitochondria, and basically removes the electrons from glucose and attaches them to an “electron carrier” redox molecule called NAD. NAD’s function is simply to receive electrons from metabolism of food, and then donate those electrons to the mitochondria. When NAD accepts these electrons from food, it becomes reduced to NADH, meaning it can later pass them on. NADH then enters respiratory complex 1 and, if it manages to successfully donate these electrons to the ETC process, it is oxidised (loses electrons) to become NAD+ ('+' representing positive charge due to lacking electrons).

Generally, a good indicator for mitochondrial efficiency is to measure the ratio of NADH : NAD+. High NADH is bad, high NAD+ is good. Why? Because high levels of NADH means that electrons are not being accepted by complex 1 to be used to fuel ATP production. Basically, in this case electron flow has slowed down. On the other hand, higher levels of NAD+ show that the mitochondria are receiving those electrons and putting them to good use! Two things to note are: 1. That carbohydrate/glucose metabolism increases NADH, and 2: That nnEMF upregulates glucose metabolism. By default, it is likely that nnEMF increases NADH at complex 1 and subsequently decreases NAD+. Meaning it slows down electron chain transport

Normally, complex 1 uses NADH/NAD+ to generate a small burst of ROS (superoxide) for signalling purposes. However, when NAD+ levels are significantly low (due to excessive carb metabolism/nnEMF) calcium ions are released to signal a “low energy (NAD+)” state. Calcium release triggers an abnormally large generation of ROS in the mitochondria via several different pathways. This subsequently causes the translocation of nuclear transcription factors NF-KB (Nuclear factor-Kappa Beta) and STAT-3 in the nucleus. These are molecules that control gene expression and are associated with pro-inflammatory pathways. This results in mitochondrial DNA genes responsible for constructing respiratory complexes (1, 3 & 4) not being expressed. Furthermore, as a result of this release of calcium there is a higher ratio of NADH to NAD+ made at complex 1. In other words, calcium inhibits to action of complex 1 and slows down the electron transport chain. On top of that, calcium is also hydrophobic. Hydrophobic substances are not conducive to building water exclusion zones. Think back to the above section on calcium efflux. Not native EMF increases all of the above processes due to the severely damaging effects of calcium efflux.

Together, these processes lower the efficiency of respiratory complexes so that electrons can no longer be transported (via ETC) across the mitochondria to make ATP and heat. The result? Protons build up in the local area and positive charge dominates. The lack of ATP fails to properly unfold protein structures, and less heat generation diminishes the cell’s ability to build exclusion zones. The membrane potential difference decreases, and our ability to donate/accept/shuttle electrons is halted. This is the beginning of a low redox potential, and is the mechanism behind how the cell begins to become dehydrated of water.

The body’s remedy for oxidative stress..

Glutathione is one of the main antioxidant proteins and is composed of three amino acids: cysteine, glutamic acid and glycine. It acts to donate electrons to (reduce) structures that have gone through oxidative damage and is critical in maintaining oxidation-reduction balance. It enhances the antioxidant activity of vitamin C, facilitates the transport of amino acids and is critical in the detoxification of metals and oxidative chemicals. It also is involved in DNA repair and synthesis. Although despite its potent antioxidant effects, it cannot neutralize hydroxyl radicals. Luckily it can successfully help to mitigate some of the damage caused by these reactions. However, when structures in the cell are consistently in a state of oxidation, glutathione levels are gradually depleted. More toxic exposure leads to more rapid glutathione depletion.


Since cysteine is used to synthesise glutathione, chronic oxidation begins to also deplete cysteine stores. Cysteine can be synthesized by the body in a normal environment. However, when the body is constantly in a state of physiological stress due to ROS, the body struggles to produce sufficient quantities to keep up with the burden. Generally, a depletion of cysteine paves the way for modern disease at the cellular level.

Cysteine is a critical amino acid component of many proteins, and its action seems to be the main controller of the cell’s redox potential. Low cysteine levels inhibits glutathione recycling, which means that structures remain chronically oxidised in the cell. When this occurs, the redox potential decreases. This means that we can no longer donate enough electrons to balance out the damage cause by oxidative stress. The pH rises in the cell, and proton flows begin to slow down. This causes a ‘backlog’ of electrons in the mitochondria so that they are no longer available for redox reactions. It results in a subsequent decrease in the amount of ATP that is generated. Remember that ATP is a principle protein-unfolding molecule and our redox must remain stable to build exclusion zones in water to “charge the battery”.

From what I can gather from reading Kruse’s blogs, the main way that cysteine affects the redox potential has to do with its unique interactions with transition metals found within proteins. Transition metals always contain unpaired electrons in their outer shell that can be donated to facilitate redox reactions. However, the unpaired electron in transition metals can also be used to generate the powerful hydroxyl radical when they are not kept under strict control (contained within a protein). Cysteine seems to be the controller of metal’s activity in the cell. When the protein is in a fully open conformation (due to the successful action of sufficient ATP), cysteine’s thiol groups/sulfide bonds bind with metal ions to keep them contained within the protein. However, this cannot take place if protein unfolding is disrupted because of an ATP deficit. Cysteine also appears to bind with excess unbound metal ions to prevent metal toxicity in the cell – to be later detoxified by glutathione. Further, it is able to “sense” the levels of oxidative stress within the cell so it can respond accordingly. Kruse also explains that cysteine’s disulfide bonds are extremely important for forming the proper three dimensional structure of all proteins.

Here is an excerpt from one paper:

In biological systems, the amino acid cysteine combines catalytic activity with an extensive redox chemistry and unique metal binding properties. The interdependency of these three aspects of the thiol group permits the redox regulation of proteins and metal binding, metal control of redox activity, and ligand control of metal-based enzyme catalysis. Cysteine proteins are therefore able to act as “redox switches,” to sense concentrations of oxidative stressors and unbound zinc ions in the cytosol, to provide a “storage facility” for excess metal ions, to control the activity of metalloproteins, and to take part in important regulatory and signalling pathways.

According to Kruse, proteins containing cysteine act as molecular “Maxwell Demons” that have the ability to detect subatomic particle (electron/proton) concentrations in the cell to increase information transfer while decreasing entropy. Remember that chronic oxidation rapidly depletes cysteine stores. With decreased ATP production and a lack of cysteine, glutathione can no longer be produced in adequate quantities. Glutathione recycling is the body’s main way of detoxifying excess metals from the system. Metals have a high affinity for thiol groups (found on cysteine), so rapidly accumulate in proteins in the absence of glutathione. Here we can see one of the mechanisms behind metal toxicity – it is directly linked to cysteine and the redox potential.

Transition metal protein link - Collagen

Transitional/co-factor metal ions (copper, iron, zinc etc) are used in a variety of vitally important biochemical reactions. They are used as a co-factor in oxidation-reduction reactions, in which they either donate electrons or accept electrons. Metal ions are usually stored within a special types of protein called metalloproteins which fulfil many different functions. One metalloprotein we will focus on here is Lysyl Oxidase. Lysyl oxidase is one of the enzymes used to “cross link” collagen. Collagen is the most abundant protein in the body, is surrounded by water everywhere it is found, and is ordinarily hydrophilic. Considering Pollack’s work (water + hydrophilic surface + radiant energy = electrical water battery), hydrated collagen (collagen bound to exclusion zone water) may be an extremely important component of the body energy-transfer system, since it is naturally so abundant. It is possible that collagen is capable of receiving information from waters exclusion zone, and then transmitting the information in a coherent manner to the whole of the system in the form of a weak DC electrical current (Rober O. Becker's findings). This is independent of hormonal/neuronal information systems and may be how the cell is electrified to produce life. When the cell is dehydrated, however, collagen’s structure begins to degrade and a lack of ATP means that it can no longer bind to water. Here we will focus on the mechanism behind how the structure of collagen is systematically destroyed.

Collagen’s formation and the maintenance of its structural integrity relies on the action of Lysyl oxidase. Lysyl oxidase contains copper in the form of Cupric (2+) ions. It functions by donating electrons (contained in copper’s outer shell) to catalyse a reaction in which cross-linkage occurs between collagen fibrils. Interestingly, Lysyl oxidase also contains a high content of cysteine.

Kruse goes on to explain:

when copper’s electrons are transferred from lysyl oxidase to the single chains of collagen made from the amino acids from DNA, the DC current electrifies the protein backbone. Electrons induce the formation of the triple helix of collagen from these three single chains, which brings the piezoelectric current in collagen to its mature form. The continued flow of this DC electron current induces the water hydration shell that surrounds collagen. This electronic induction maximizes collagen’s water binding sites on its triple helix simultaneously without any use of exogenous energy.

The above process is disrupted when consistent Reactive Oxygen Species are present. ROS (mentioned above) destroy proteins (such as lysyl oxidase) and gradually begin to “wear away” at collagen’s structure. Low amounts of ATP mean that lysyl oxidase cannot unfold correctly, therefore cysteine is unable to “bind” copper properly. When the ROS variant ‘Superoxide’ comes into contact with copper ions, Cupric (Cu[2+]) is reduced to Cuprous (Cu[1+]). Cu(1+) ions then proceed to participate in a fenton reaction that we mentioned earlier - to produce the notoriously destructive hydroxyl free radical.:

Arguably the most important set of copper redox reactions in vitro involve Haber-Weiss driven Fenton chemistry that results in the formation of hydroxyl free radicals. This free radical species is one of the most reactive and destructive molecules found in vitro. Under physiological conditions, cupric copper can be reduced to cuprous copper by superoxides or ascorbate anion. Cuprous copper catalyzes the formation of hydroxyl free radicals. ~ Source

This particular radical is then capable of severely damaging collagen (and other proteins) by stealing electrons via oxidation reactions. Low cysteine/glutathione levels are unable to counteract the damage. Overall this increases the protons and decreases electrons in the system, leading to chronic oxidation and further lowers redox potential. Lysyl oxidase is also now unable to donate electrons to cross-link collagen due to oxidation damage, therefore collagen begins to ‘unzip’ and can no longer form a surrounding hydration shell around itself. This effect increases the charge of collagen to be more positive (due to less electrons) and LESS hydrophilic (unzipping, damaging the water binding sites + accumulation of metals). The lack of available electrons leads to state in which exclusion zones cannot be formed. We begin to witness how collagen becomes “dehydrated”. Coherent, organising energy transfers can no longer take place, and entropy ensues.

This process is not limited to collagen, but also occurs in DNA, RNA, Lipids, and other organelles. Intracellular dehydration is a recipe for disaster, and is now my main focus in attempting to achieve optimal health.

To compound the problem, what direct effects does nnEMF have on these accumulated metals? And how does this affect water?

The biological effects of non-native EMF on biologically stored metals is under-studied, however there is significant evidence in physical sciences data supporting the idea that microwave radiation has a powerful effect on metal compact powders. From what I could find, it seems fairly well established that bulk metal sheets reflect microwave radiation. However, metal powders have been shown to absorb this radiation so that they become energised. Dr Kruse postulates that biologically stored metals are structurally similar to metal powders, they are of similar size and are also porous, so that EMF radiation has significant effects on the way cells containing these metals can function.

One article states:

“The most recent development in microwave applications is in sintering of metal powders, a surprising application, in view of the fact that bulk metals reflect microwaves. However, reflection by a metal occurs only if it is in a solid, nonporous form and is exposed to microwaves at room temperature. Metal in the form of powder will absorb microwaves at room temperature and will be heated very effectively and rapidly.” ~Source

Another paper states:

Microwave sintering of metal powders which have high electrical conductivity is a new area with growing interest. This was first reported in 1999 by Roy and co-workers that a porous, powder metal compact could be heated and sintered in a microwave field. This was at that time considered surprising because the electrically conducting materials were supposed to reflect microwave radiation. Later on other researchers also demonstrated that all powder metals at room temperature absorb microwaves and only bulk metals reflect the microwaves allowing only surface penetration. ~ https://www.mri.psu.edu/sites/default/files/file_attach/165.pdfSource

Consider that transition metals are stored in most of the proteins in the body. Then again consider that calcium efflux/phosphate buildup/cysteine+low glutathione causes the cell to accumulate those metals in excess. Might it be possible that those metals are absorbing nnEMF's and then radiating that energy back into the cell and interfacial water?

If this were the case, then what effects would this microwave “heating” radiation have on the interfacial water surrounding these accumulated metal ions in the cell?

Here are some excerpts on EMF effects on water structure:

Even partial alignment of the water molecules with the electric field will cause pre-existing hydrogen bonding to become bent or broken. The balance between hydrogen bonding and van der Waals dispersion attractions is thus biased towards van der Waals attractions giving rise to less cyclic hydrogen bonded clustering. An electric field also changes the molecular O-H bond lengths (25x109 V m-1 causing ~±6% change in a lone water molecule), H-O-H bond angle (25x109 V m-1 causing ~+1%/-0.2% change in a lone water molecule), vibrational frequencies and dissociation energy, depending on the relative orientation of the molecule to the field [1727]. This will affect the hydrogen bonded network in an anisotropic manner.

Electric fields also lower the dielectric constant of the water [616], due to the resultant partial or complete destruction of the hydrogen-bonded network.

If electromagnetic effects do indeed influence the degree of structuring in water [1323], then it is clear that they may have an effect on health. The biological effects of microwaves, for example, have generally been analyzed in terms of their very small heating effects. However, it should be recognized that there might be significant non-thermal effects (for example, [714]) due to the imposed re-orientation of water at the surfaces of biomolecular structures such as membranes [356]. Similar effects on membranes have been proposed to occur due to magnetic [657] and electric fields [1086] ~ Source

From another paper:

The results obtained suggest that treatment with weak electromagnetic fields induces structural changes of water solutions, and the manifestations of these changes depend on the conditions of chromatography and chemical composition of solutions under study ~ Source

And finally:

The structural-effect of various ions in dilute aqueous solutions has been studied by Nuclear Magnetic Resonance(NMR) and it has been observed that by increasing the magnetic field, the short-range hexagonal membered bonding and surface tension are changed. Similarly, an increase of water structure can be achieved by adding structure making ions or lowering the temperature.~Source

So, the microwave energies in nnEMF begin to damages water’s hydrogen bonding network and decreases the level of “structuredness”. Anyone who has read Gerald Pollack’s book should recall that water is more structured at lower temperatures. Infra-red builds exclusion zones, however microwaves seem to excite the water structure so that its structure becomes defunct. In other words, nnEMF absorbed and radiated by accumulated metal ions may directly dehydrate water.

Short clarification on ATP’s protein unfolding capabilities

Not much has been said in this post about ATP's ability to unfold proteins. Below I have copied some pertinent excerpts from a paper by the late Dr Mae Wan-Ho to cover the topic briefly.

According to Gilbert Ling’s association-induction hypothesis:

“Within the resting cell, most if not all proteins are extended so that the peptide bonds along their polypeptide backbone are free to interact with water molecules to form ‘polarized multilayers’ (added: Pollack's exclusion zone) of aligned water molecules, while the carboxylate side chains preferentially bind K+ over Na+. Both are due to the ubiquitous presence of ATP in living cells.

In the absence of ATP, proteins tend to adopt secondary structures – -helix, or a -pleated sheet - as hydrogen bonds form between peptide bonds in the same chain, so they don’t interact with water . In this state, the carboxylate and amino side chains are also unavailable for binding ions, as they can pair up with each other. And the water next to the protein is not too different from the bulk phase outside the cell.

However, when ATP is bound to the ‘cardinal site’ of the protein, it withdraws electrons away from the protein chain, thereby inducing the hydrogen bonds to open up, unfolding the chain, exposing the peptide bonds on the backbone, and enabling them to interact with water to form polarized multilayers (PM) (Added: Exclusion Zones!) (Fig. 1 right). At the same time, the carboxylate and amino side chains are opened up to interact with the appropriate inorganic cation X+ and anion Y-. The protein ‘helper’ Z bound to the polypeptide chain is now also fully exposed. In muscle, the polypeptide chain binding ATP is myosin, and Z could well be actin. The cation X+ is K+ in preference to Na+, because ATP binding turns the carboxylate group into a strong acid that prefers K+ over Na+.

This switching between states is the elemental ‘living machine’. It is what animates and energizes the living cell.

Recent corroboration in favour of Lings hypothesis by Dr Mae Wan-Ho:

The interaction of unfolded protein chains with water is particularly significant. When protein chains are unfolded, their peptide bonds -CONH- become exposed, forming an alternating chain of negative (CO) and positive (NH) fixed charges that is very good at attracting polarized multilayers (PM) of oriented water molecules . I have referred to this water as ‘liquid crystalline water’ on grounds that it forms dynamically quantum coherent units with the macromolecules ([17] The Rainbow and the Worm, The Physics of Organisms, ISIS publication), enabling them to transfer and transform energy seamlessly with close to 100 percent efficiency. And it is this liquid crystalline water that gives the cell all its distinctive vital qualities (see [18] Life is Water's Quantum Jazz, ISIS Lecture).

In addition, though not mentioned by Ling, PM is expected to be extremely good at resonant energy transfer over long distances, even better than bulk water at ambient temperatures, and to conduct positive electricity by jump conduction of protons (see [21] Positive Electricity Zaps Through Water Chains, SiS 28).

A cell with 80 percent water content would have polarized multilayers of water some 4 molecules thick that anastomose and surround the abundant cytoplasmic proteins such as those of the ubiquitous cytoskeleton. This is also precisely the thickness of the highly polarized water around proteins identified in Terahertz absorption spectroscopy within the past several years [22].

Surprisingly, an opinion review article published in 2005 stated [23]: “Recent progress in predicting protein structures has revealed an abundance of proteins that are significantly unfolded under physiological conditions. Unstructured, flexible polypeptide are likely to be functionally important and may cause local cytoplasmic regions to become gel-like.” This is another indication that Ling may well be right.

 

[Keyhole]

Some thoughts on heavy metal toxicity

I just want to add that the above information can provide us all with some valuable insight on whether or not to attempt "heavy metal" detoxes. Chelating heavy metals to release them into the system to be detoxified may only be effective/safe when the redox potential is high. Remember that glutathione is what detoxifies metals (mainly due to its high cysteine [metal binding] content). If there are inadequate levels of cysteine/glutathione due to a low redox potential, then when an external agent releases these metals into the system, they may cause more damage by seeping into surrouding, previously unaffected tissues. Low glutathione means that the metal cannot be detoxed. So unless someone has access to high levels of IV glutathione, it may not be worth attempting. Supplemental NAC etc may help slightly, but if the cell is already chronically oxidised, then the newly produced glutathione may have "too much work on its hands" to be able to deal with the metals. So in light of the above information, I believe anyone with metal toxicity may be best off to focus on increasing their redox potential before working on anything else.

Added: Important point: Think back to the above post. What causes heavy metal accumulation? Wouldn't it make sense to deal with the causative factor. Doing heavy metal detox may be effective temporarily. But if the causes are not addressed (low redox, Ca efflux, ROS in the motochondria), the metal may simply just continue to be accumulated, eventually leading to metal toxicity once more.