Hemochromatosis and Autoimmune Conditions

Hesper

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Psyche said:
This one is a very interesting article. He basically says that a poorly liganded iron is what makes taking vitamin C dangerous.

So from what I understand, unless there are chelators binding at each of the sites on iron, Vitamin C binds to it and turns it into OH, or a hydroxyl radical.

From Wikipedia:

_http://en.wikipedia.org/wiki/Hydroxyl_radical#Biological_significance

The hydroxyl radical can damage virtually all types of macromolecules: carbohydrates, nucleic acids (mutations), lipids (lipid peroxidation) and amino acids (e.g. conversion of Phe to m-Tyrosine and o-Tyrosine). PMID 7776173. The hydroxyl radical has a very short in vivo half-life of approximately 10−9 seconds and a high reactivity.[3] This makes it a very dangerous compound to the organism.[4][5]

Unlike superoxide, which can be detoxified by superoxide dismutase, the hydroxyl radical cannot be eliminated by an enzymatic reaction. Mechanisms for scavenging peroxyl radicals for the protection of cellular structures includes endogenous antioxidants such as melatonin and glutathione, and dietary antioxidants such as mannitol and vitamin E.[4]

If I'm following, it is the hydroxyl radical that we are concerned with with Vitamin C. But the problem is still that we have so much iron in our diets and in our tissues, especially our brain, wreaking havoc. And though we can detoxify the OH we're stuck with the iron unless we bleed it out.

Psyche said:
The HFE gene

Simon et al. (26) first demonstrated in the late 1970s that the gene responsible for HH is closely linked to the human leukocyte antigen (HLA) locus on a short arm of chromosome 6. Twenty years later, this gene was identified and termed as HLA-H gene by Feder et al. (27). The HLA-H gene, now renamed as the HFE gene, is comprised of 7 exons and is expressed widely or at low level in most tissues, including brain.


I think this is a key concept. There is a genetic predisposition where HLA-DQ genes located on chromosome 6 makes you vulnerable to gluten intolerance. HLA stands for the human leukocyte antigen (HLA) system which is also known as the major histocompatibility complex (MHC). The important thing to know about this system is that it contains a large number of genes related to immune system function in humans.

So if I'm understanding you correctly, damage to this particular area of the genetic code associates gluten intolerance with hereditary hemochromatosis. Healing the gut helps heal the immune system, but all of the meat eaten in order to heal the gut results in an increase in iron. Looks like we found a bug in the program!

I found the following at _http://ghr.nlm.nih.gov/condition/hemochromatosis

What genes are related to hemochromatosis?

Mutations in the HAMP, HFE, HFE2, SLC40A1, and TFR2 genes cause hemochromatosis.

The HAMP, HFE, HFE2, SLC40A1, and TFR2 genes play an important role in regulating the absorption, transport, and storage of iron. Mutations in these genes impair the control of iron absorption during digestion and alter the distribution of iron to other parts of the body. As a result, iron accumulates in tissues and organs, which can disrupt their normal functions.

Each type of hemochromatosis is caused by mutations in a specific gene. Type 1 hemochromatosis is caused by mutations in the HFE gene, and type 2 hemochromatosis is caused by mutations in either the HFE2 or HAMP gene. Mutations in the TFR2 gene cause type 3 hemochromatosis, and mutations in the SLC40A1 gene cause type 4 hemochromatosis. The cause of neonatal hemochromatosis is unknown.

More info on the genes and their locations:

From: _http://www.mlpa.com/WebForms/WebFormProductDetails.aspx?Tag=tz2fAPIAupKyMjaDF\E\t9bmuxqlhe/Lgqfk8Hkjuss|&ProductOID=47XncHLCo0I|

The HFE gene comprises 6 exons, spanning about 8 kb of genomic DNA on 6p22.1.
The SLC40A1 gene contains 8 exons, spanning 20 kb and is located on chromosome 2q32.2.
The TFR2 gene consists of 18 exons and has a length of approximately 21 kb on chromosome 7q22.1.
The HFE2 gene comprises 4 exons, spanning about 4 kb of genomic DNA on 1q21.1.
The HAMP gene contains 3 exons, spanning 3 kb and is located on chromosome 19q13.12.

After doing a little more digging it looks like the C282Y mutation on the HFE gene is the most common. I found some research pointing out the positive contribution of this genetic anomaly for populations (I have starvation in mind at this point in time):

_http://www.clinchem.org/content/44/12/2429.full

The C282Y mutation is believed to have originated in a Celtic population. We suggest that the importance of its biological advantage decreased over time because iron deficiency is now less common because of reduced birth rates, the use of oral contraceptives, oxytocic drugs, medical iron supplementation, and improved nutrition. Notwithstanding a putative importance of the C282Y mutation in the past, its protective effect may still be relevant in present times for conditions of enhanced iron demand that may result from recurring pregnancies. Influences of the mutation on iron metabolism are supported by our study, which showed a difference in iron supplementation between the heterozygous and wild-type subjects. In addition, a history of metrorrhagia was reported by a greater percentage of heterozygous individuals, and this group also contained a higher proportion of multiparous women. These facts could have attenuated genotypic effects on some indicators reflecting iron metabolism. Interestingly, the prevalence of iron deficiency and iron deficiency anemia was considerably lower in our study population, which consisted exclusively of healthcare workers, than in other study cohorts of women with comparable age (2). Conceivably, such a sample bias could have attenuated the relevance of our results.

In conclusion, our data strongly suggest a role of the C282Y mutation in the HFE gene in preventing iron deficiency in young females. Protection against iron deficiency and its morbid consequences may have conferred a selection advantage for heterozygous carriers of the mutation in the past and may explain the high prevalence of this particular mutation, which accounts for the most frequent genetic disorder with an autosomal mode of inheritance.


So my logic might be off but I'm thinking is it possible that these genetic changes came about at a time when everyone was forced to eat plants and grains due to huge die-offs/plagues, and they benefited from this biological "hoarding" of iron while their immune systems were damaged by anti-nutrients and viruses. That could be just me using what's in my toolbox instead of looking for a new tool though. In the end I just hope this information is already helping those with adverse reactions to the Vitamin C protocols. You're in my thoughts everyone.
 

Voyageur

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From Psyche post, thought that this was interesting:

Put another way, it is not simply enough to know that ‘iron’ is present at an adequate level but that it is available in a suitably liganded form. Anaemia can be caused by poor liganding as well as by an actual shortage of ‘iron’ itself. Note too that partial chelation in the presence of an antioxidant agent such as ascorbate (vitamin C) can in fact make ascorbate (or other reducing agent) act as a pro-oxidant and thus actually promote the production of OH• radicals in the presence of inappropriately or inadequately liganded Fe(II)

While reading the other night in this thread, came across possibly why iron also plays a role (or conversely the lack thereof) in cold adaptation (i.e. hypothermic conditions).

_www.biomedcentral.com/content/pdf/1471-2164-12-630.pdf

Proteomic analysis of endothelial cold-adaptation

In our studies of cold-adaptation, human coronary artery endothelial cells (HCAECs) cultured at 25°C become progressively more resistant over time to 0°C-injury and in particular to the oxidative stress induced by exposure to 0°C and rewarming [16]. The molecular basis of the adaptation remains largely unknown but the resulting protection at 0°C is due, in part, to the sequestration of catalytically active iron [16]. The protection may also be associated with an increase in intracellular glutathione, an important antioxidant and signaling molecule of the cell, at 25°C. Glutathione (GSH) reacts directly with free radicals, participates in the reductive detoxification of hydrogen peroxide and organic peroxides, serves as a co-factor in the enzymatic breakdown of xenobiotics and reacts with protein thiols to form mixed disulfides (P-SSG) under conditions of mild oxidative stress [20]. Protein glutathionylation is a reversible modification that provides a mechanism for protecting proteins from irreversible oxidative damage and for regulating protein function and thereby many diverse cellular processes such as cytoskeletal organization, ionic homeostasis and the expression of genes involved in antioxidant defenses [21].

From what has been read, catalytically active iron can be toxic and promote bacteria (a high source to feed on). If human changes (past mutation) resulted in a disrupted liganded (binding), and the protection to cold might be partially relent on the sequestration of catalytically active iron, and if it can't be properly sequestered, does that mean it is held (static) and would just pile up and be made more readily available for bacteria and for other interrelated immune disruptions?

Think i'm just clouding the waters here trying to soak all this in and make sense of it. Hope that information posted in this thread about these matters can bear fruit in helping to figure out what actions should be tried or taken.
 

shijing

The Living Force
I did a search on the correlation between iron and Parkinson's disease, and it appears that it's pretty established even if the specifics aren't clearly understood. Here are a few examples:

http://www.hindawi.com/journals/ijcb/2012/983245/

Abstract

Iron is an essential element in the metabolism of all cells. Elevated levels of the metal have been found in the brains of patients of numerous neurodegenerative disorders, including Parkinson's disease (PD). The pathogenesis of PD is largely unknown, although it is thought through studies with experimental models that oxidative stress and dysfunction of brain iron homeostasis, usually a tightly regulated process, play significant roles in the death of dopaminergic neurons. Accumulation of iron is present at affected neurons and associated microglia in the substantia nigra of PD patients. This additional free-iron has the capacity to generate reactive oxygen species, promote the aggregation of α-synuclein protein, and exacerbate or even cause neurodegeneration. There are various treatments aimed at reversing this pathologic increase in iron content, comprising both synthetic and natural iron chelators. These include established drugs, which have been used to treat other disorders related to iron accumulation. This paper will discuss how iron dysregulation occurs and the link between increased iron and oxidative stress in PD, including the mechanism by which these processes lead to cell death, before assessing the current pharmacotherapies aimed at restoring normal iron redox and new chelation strategies undergoing research.

http://phys.org/news169899879.html

Neurons that produce the neurotransmitter dopamine are the cerebral cells that most commonly die-off in Parkinson's disease. The cells in the so-called substantia nigra, which contain the dark pigment neuromelanin, are affected. It is also known that the iron content of these cells increases during the course of Parkinson's disease [...] Prof. Katrin Marcus concludes that - in the opinion of her research team - ferritin in the neuromelanin granules is a further significant element in the homeostasis of the iron content in the substantia nigra. This first direct proof of ferritin in neuromelanin granules in dopaminergic neurons is an important step towards an improvement in the comprehension of the iron metabolism in the human substantia nigra. It moreover supplies arguments for new hypotheses concerning the mechanisms of the iron-regulated degeneration of the substantia nigra in Parkinson’s disease. Currently the scientists are investigating further unclarified issues, such as how the composition of the neuromelanin granules changes with increasing age and during the course of the disease. Moreover, they are trying to elucidate the exact function of the neuromelanin in the cell, and why only the neuromelanin-containing cells in the substantia nigra die-off.

http://www2.cnrs.fr/en/1411.htm

Limiting the level of iron in dopaminergic neurons could help fight Parkinson's disease (PD). This is what CNRS researcher Etienne Hirsch1 together with a team at INSERM-UPMC2 have recently demonstrated.3 Iron plays an integral role inside neurons as a co-factor for enzymes that produce dopamine–the neurotransmitter found lacking in a specific region of the brain in PD patients. But while some iron is needed for dopamine production, too much results in oxidative stress and cell death. To elucidate the role of the iron transporter DMT1 in the development and evolution of Parkinson's disease, and to see whether the mechanism may represent a therapeutic target for neuroprotection, Hirsch and his co-workers used rodent animal models.

First, they observed that the induction of the disease in mice was correlated with a doubling of the level of expression of DMT1, leading to an increase of iron within dopaminergic neurons, and the expected ensuing oxidative stress and cell death. Then, they used a mice strain called “microcytic” where the DMT1 iron transporter was impaired, the result of a spontaneous mutation. When injected with a toxic chemical specific to dopaminergic cells, these mice showed a 20% neuronal cell death rate compared to the 40% in wild-type animals. A functional DMT1, with the resulting iron increase inside cells, thus seems to contribute to neuronal cell death, whereas a dysfunctional iron transporter confers protection from degeneration. “While there is now relatively good symptomatic treatment for Parkinson's disease, that consists in restoring the missing dopamine, we have no treatment to slow down the progression of neurodegeneration which evolves over decades,” says Hirsch. “We found that we could protect half of the dopaminergic neurons from degeneration by decreasing iron in the cells.” His main concern with targeting this transporter therapeutically is that it could prevent required levels of iron from entering the cells. “It is therefore important to achieve the right balance and prevent dysregulation,” he concludes.
 

Ennio

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Some years ago the iron levels in my blood were shown to be high so my doctor recommended my giving blood every few months, which I did for several years. The iron levels showed normal soon after I started so this is something to look out for again. I will be getting my blood tested this week to see where I am at.

Here is a bit about the use of DMSO as one possible way to help chelate iron:

http://healthoracle.org/downloads/D/DMSO-.pdf

DMSO (dimethyl sulfoxide) is a colorless, slightly oily liquid that is
primarily used as an industrial solvent.

Iron absorption is reduced by the host as a defence mechanism
during an infection.

Iron levels are elevated in the inflamed mucosa.

Oral iron supplements anecdotally exacerbate inflammatory
bowel disease

Mucosal iron may enhance hydroxyl ion production via Fenton
chemistry.

During inflammation, the superoxide anion (O-2) and
hydrogen peroxide (H2O2) are produced by stimulated
polymorphonuclear leukocytes and macrophages. The toxic
effects of these reactive oxygen intermediates increase when
traces of iron are present, because iron catalyzes the formation
of the hydroxyl radical (OH.).

Iron release from ferritin depends on O-2

DMSO


Dimethylsulfoxide (DMSO) induces hemoglobin synthesis and
erythroid differentiation of Friend erythroleukemia cells in
vitro. Induction is accompanied by increased transferrin-
binding activity which is necessary for the cellular acquisition of
iron from transferrin for hemoglobin synthesis.

dimethylsulfoxide (DMSO) and deferoxamine (DFX), the latter
being an iron chelator which prevents HO formation by
blocking the Fenton reaction, were found to inhibit TNF-alpha
production in LPS-stimulated human PBMC

Striking Resemblances:

Steroids (Prednisolon) inhibit the secretion of free radicals by
Polymorphonuclear neutrophils


5-ASA (Asacol) exhibit superoxide and hydroxyl-radical
scavenger properties.
The Inflammation Mechanism
During infection, the body makes considerable metabolic adjustment
in order to make iron unavailable to microorganisms.
As a result of infection, there is:
1. Decreased intestinal absorption of iron from the diet
2. Decrease of iron in the plasma and an increase in iron in
storage as ferritin
3. Increased synthesis of the human iron-binding proteins (iron
chelators), lactoferrin and transferrin which trap iron for use by
human cells while making it unavailable to most microbes.
4. Coupled with the febrile response, decreased ability of
bacteria to synthesize their own iron chelators called
siderophores.
5. Prior stationing of lactoferrin at common sites of microbial
invasion such as in the mucous of mucous membranes, and the
entry of transferrin into the tissue during inflammation.
This lack of iron, which is needed for the bacterial electron transport
chain, can inhibit the growth of many bacteria. However, this does
not help when the inflammation is in the intestines.

In the intestines the iron level is elevated and the Haber Weiss
reaction is very active.

The Haber Weiss Reaction (aka Fenton reaction)

Iron is a catalyzer in The Haber-Weiss reaction, ‘free’ iron can
catalyze the formation of very injurious compounds, such as the
hydroxyl radical (OH) from compounds such as hydrogen peroxide,
which are normal metabolic byproducts (Fenton reaction).
The hydroxyl radical is highly reactive, and attacks lipids, proteins and
DNA.
The initial reaction with each of these molecules is the formation of
peroxides (e.g., lipid peroxides) that can interact with other molecules
to form cross links. These cross-linked molecules perform their
normal functions either poorly or not at all.

Iron supplementation may aggravate inflammatory status of colitis.
Iron supplementation is one of the principal therapies in
inflammatory bowel disease. Iron is a major prooxidative agent;
therefore therapeutic iron as well as heme iron from chronic mucosal
bleeding can increase the iron-mediated oxidative stress in colitis by
facilitating the Fenton reaction, namely production of hydroxyl
radicals.

It was concluded that iron supplementation can amplify the
inflammatory response and enhance the subsequent mucosal damage
in a rat model of colitis. We suggest that the resultant oxidative stress
generated by iron supplementation leads to the extension and
propagation of crypt abscesses.

Reactive oxygen species may be pathogenic in ulcerative colitis. Oral
iron supplements anecdotally exacerbate inflammatory bowel disease
and iron levels are elevated in the inflamed mucosa. Mucosal iron
may enhance hydroxyl ion production via Fenton chemistry.
Conversely, the iron chelator, desferrioxamine, is reportedly
beneficial in Crohn's disease.

During inflammation, the superoxide anion (O-2) and hydrogen
peroxide (H2O2) are produced by stimulated polymorphonuclear
leukocytes and macrophages. The toxic effects of these reactive
oxygen intermediates increases when traces of iron are present,
because iron catalyzes the formation of the hydroxyl radical (OH).
Iron release from ferritin depends on O-2 because it can be
prevented by the addition of superoxide dismutase. Catalase and
dimethylsulfoxide have no inhibitory effect on iron mobilization.

It seems like DMSO can scavenge the H2O2 Hydrogen Peroxide
molecules. It cannot scavenge the Super Oxide Anion (O-2),
however.

Summary
1. Inflammation
2. Superoxide anion (O-2) and Hydrogen Peroxide (H2O2) are
produced.

3. The O-2 will release even more iron from the ferritin. Iron
overdose in the intestines
4. H2O2 and Iron will form Hydrogen free radicals (Fenton
Reaction).

DMSO will remove most of the H2O2 and will increase the iron
export by stimulating the transferrin receptors. The Super Oxide
Anion is still there, however. When the O-2 can release more iron
than the transferrin receptors can export, the vicious cycle is still not
broken.


Conclusion

Perhaps DMSO can stop the damage mechanism in the intestines,
but maybe it needs some help from an O-2 scavenger also.
DMSO can decrease the amount of free iron
The ability of Friend erythroleukemic cells to bind transferrin and
take up its iron increases substantially as a result of dimethyl
sulfoxide-stimulated differentiation.
Dimethylsulfoxide (DMSO) induces hemoglobin synthesis and
erythroid differentiation of Friend erythroleukemia cells in vitro.
Induction is accompanied by increased transferrin-binding activity
which is necessary for the cellular acquisition of iron from transferrin
for hemoglobin synthesis.

Hydroxyl radical scavengers inhibit TNF-alpha production
Dimethylsulfoxide (DMSO) and deferoxamine (DFX), the latter
being an iron chelator which prevents HO formation by blocking the
Fenton reaction, were found to inhibit TNF-alpha production in
LPS-stimulated human PBMC.
Desferroxamine and Copper/Zinc Superoxide Dismutase
DMSO does two things to stop the Fenton Reaction:

It neutralizes the H2O2 Hydrogen Peroxide molecules, which
are a necessary compound for the Fenton Reaction.

It activates the transferrin receptors, so the free iron is
removed, which is also a necessary compound for the Fenton
Reaction.

The article also mentions Desferroxamine, another possible chelator.

The parallel with Desferroxamine

Desferroxamine is also an antioxidant.
Desferroxamine binds the free iron to its molecule, so the Fenton
Reaction cannot work.
Mucosal iron may enhance hydroxyl ion production via Fenton
chemistry. Conversely, the iron chelator, desferrioxamine, is
reportedly beneficial in Crohn’s disease.
The parallel with Copper/Zinc Superoxide Dismutase

Copper/Zinc Superoxide Dismutase is also an H2O2
Hydrogen Peroxide scavenger.

82% is very close to the 80-90% success rate on David Gregg’s
Site.

Besides this, C/Z Sup.Ox.Dism. is also an O-2 (Superoxide)
scavenger
Bovine CuZnSOD was used during an 8-year period as an anti-
inflammatory drug in 26 patients with severe Crohn’s disease, usually
after failure of corticotherapy, or when this drug was avoided because
of side-effects or abscesses.
We obtained 19/26 very good short term responses, and 82% good
results on long term evolution.

These results indicate that the anti-inflammatory effects of
CuZnSOD were mainly the removal of oxygen free radicals and
indirectly the prevention of lipid peroxidation. This study suggests
that CuZnSOD may be beneficial in the treatment of patients with
ulcerative colitis.

The parallel with 5-ASA (5-aminosalicylic acid)

5-ASA is also an antioxidant (hydroxyl free radical scavenger).

5-ASA stops the flow of iron into the intestines by removing
O(-2)
(5-ASA), when used in therapy, exhibit superoxide and hydroxyl-
radical scavenger properties.

When tissue is inflamed, two things are created:

Hydrogen Peroxide

The Super Oxide O(-2)
Hydrogen peroxide is one of the elements on the left side of the
Fenton Reaction.
(H2O2 + Fe (+2) --> Fe(+3) + OH + Hydroxyl Free Radical)
O(-2) removes the iron from specific iron-carrying cells in the
intestine walls.
Fe (+2) (Iron) is the second element on the left side of the Fenton
reaction.

So, in fact, 5-ASA does two things:

1. It removes the Hydrogen Peroxide
2. It stops the flow of iron into the intestines by removing O (-2)
The parallel with steroids (like Prednisolon)
Steroids inhibit the secretion of free radicals by Polymorphonuclear
neutrophils. 5-ASA (aka Asacol) and Prednisolon are the most
effective conventional medicine used for treating Crohn's and UC.
Pretreatment with the iron chelator desferroxamine followed by
hydrogen peroxide treatment at 37°C gives a considerable sparing
effect.

In contrast, the response to X-rays is not modified by the above
chelators, with the exception of mutation frequencies: lower mutant
numbers are found in desferroxamine pretreated LY-R cells.
In manufacturing, DMSO is used as an industrial solvent for
herbicides, fungicides, antibiotics, and plant hormones.
 

Gandalf

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Laura said:
Regulattor said:
I've checked my serum Fe and Ferritin levels today.

Fe 19,2 µmol/L (ref: 11-32)
Ferritin 174,7 ng/mL (ref: males 23,9 - 336,2)

Both are looking good. However, since I'm still having troubles with KD I'm going to give a blood donation and report back.

Yeah. If the ideal ferritin level is around 25-50, you are a bit high. How old are you? If you are still young, maybe it means you have gradual accumulation going on.

Two of our crew gave today and another few will go on Tuesday, I think.

I gave today and my hemoglobin was 15,6 and my hematocrit was 48.
 

Laura

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Gandalf said:
I gave today and my hemoglobin was 15,6 and my hematocrit was 48.

Important to know ferritin level. Anyway you can get that?
 

Gandalf

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Laura said:
Gandalf said:
I gave today and my hemoglobin was 15,6 and my hematocrit was 48.

Important to know ferritin level. Anyway you can get that?

Will ask for that next time.

But I do know that there is a relation between iron and hemoglobin. More the hemoglobin is high, more you have iron in the blood.
 

nicklebleu

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Gandalf said:
More the hemoglobin is high, more you have iron in the blood.

That is not entirely correct ... Iron is a building block for hemoglobin. The more you turn over hemoglobin (e.g. menstruating woman), the more building blocks you need to replenish your hemoglobin, until there is not enough left of it and only then hemoglobin starts to drop. So you can have normal Hb and low iron stores (ferritin) - and that's what we would like to achieve. Apart from the fact that you can have low readings of Hb for other reasons and have entirely normal (or even high) iron stores.
 

lilies

The Living Force
Iron overload ? Hemochromatosis?

No wonder runners on KD should be protected from this. If KD in general may cause iron overload, running makes sure of iron loss, a balancing effect. How running combined with sprinting causes iron loss:

1. Blood usually gathers in the leg and feet during running. Feet full of blood strike the ground hard causing footstrike, destruction of red blood cells through mechanical damage[hypothesis] see below quote: loss of red blood cells equals loss of iron.


Red blood cells and the iron they contain, are recycled and replaced every 120 days
(Reference #1)

What about giving blood, that also surely causes iron loss?

EXERCISE-INDUCED HEMOLYSIS has been reported for more
than 50 years (11). In particular, distance running has
been associated with significant destruction of red
blood cells (RBC) with RBC turnover being substantially
higher in runners compared with untrained controls
(29). Several groups have suggested that mechanical
damage to RBC occurs as they pass through the
capillaries of the foot during the footstrike phase (5, 8,
10, 20, 29). However, studies on athletes involved in
sports in which foot impact does not occur have also
found evidence of exercise-induced hemolysis. These
activities include swimming (25), weight lifting (2, 24),
and rowing (9). Given that factors other than footstrike
cause hemolysis during exercise, these variables as
causes of hemolysis during running cannot be eliminated.
Thus the contribution of footstrike per se to
running-induced hemolysis is unclear.
Apart from footstrike, several other mechanisms
may contribute to hemolysis during exercise. Because
of their continuous exposure to high-oxygen flux, RBC
are extremely vulnerable to oxidative damage (3, 26).
Under normal conditions, the superoxide radical is
generated from the autooxidation of oxyhemoglobin to
methemoglobin in RBC at a rate of 3%/day (17). Because
superoxide generation appears to be proportional
to oxygen flux (26), oxidative stress may in turn
increase in proportion to the oxygen uptake (V˙ O2) associated
with exercise. Oxidative stress has been implicated
in the normal “aging” of RBC (3), and there are
numerous reports of increases in “footprints” of oxidative
damage and antioxidant depletion in RBC after
exercise (26).
(Reference #2)

2. Iron deficiency in runners: profuse sweating balances itself during running because of water loss. You stop sweating after a time or its greatly reduced. After sweating a lot, loosing iron.
http://runnersconnect.net/running-nutrition-articles/iron-deficiency-in-runners/

Footstrike if really causes red blood cell death, then it is especially so when running barefoot (the ancient way), which is recommended, because the ground - grassy earth, soil - effects a certain amount of sole massage and is super refreshing:

Sole massage
Acupressure or sole massage is a massage that uses fingers to exert pressure on bioactive points on the sole, which nowadays, in the era of shuffling slippers, have become neglected. A 15-minute massage is relaxing and pleasant and has an effect on the whole organism – it helps to relieve stress, cures chronic diseases, improves blood pressure, stimulates metabolism, relieves pain and relaxes the body.
Reference #3

3. Runner’s Anaemia
Anaemia seen in long-distance runners, which is macrocytic, and accompanied by plasma volume expansion, haemolysis from the pounding of feet on pavement, and hemoglobinuria.

Anemia: The condition of having a lower-than-normal number of red blood cells or quantity of hemoglobin.

Note: You should NEVER run on pavement or asphalt or concrete it destroys your joints!! Always look for grassy earth or forest walkways, where there is natural grass / soil, (days) after rain the soil is soft, running on that is the best. Thicker grass also reduces shock on harder soil. Use jogging shoes with super-shock-protection, for crossing those stone walkways or concrete surfaces.

Reference #1:
http://www.jctonic.com/include/minerals/iron.htm
http://www.jctonic.com/include/minerals/magnesiu.htm

Reference #2:
http://jap.physiology.org/content/94/1/38.full.pdf

Reference #3:
http://www.wasa.ee/en/therapy-relaxation/treatments/

Reference #4:
http://runnersconnect.net/running-nutrition-articles/iron-deficiency-in-runners/
 

LQB

The Living Force
FOTCM Member
Here's some blood test results for my mother and myself:

Test LQB Mother Range
Transferrin 214 243 200-370 mg/dl
Ferritin 81 64 (26-388) and (8-252) ng/mL
RBC 4.4 4.4 (4.4-5.9) and (3.8-5.2)
HGB 14.2 13.5 (13-18) and (12-16) g/dL
CRP-HS .1 .5 0. - .3 mg/dL

Looks like ferritin is reasonably low but CRP is pretty high for my mother.
 

Gawan

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Okay, I have some results too. May doc planned anyway to test for these two, so I hadn't to ask for it:

Ferritin: 164.4
Fe: 22.3

And liver results were okay too.

According to lab standards everything is in range (and nothing to worry) and could eventually get difficult to convince my doc for blood letting. I felt also a bit better after giving the blood for the lab yesterday and had much more energy than I used to have. But from lunch on, I was sleepy again which lasted then the rest of the day.
 

Laura

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Gawan said:
Okay, I have some results too. May doc planned anyway to test for these two, so I hadn't to ask for it:

Ferritin: 164.4
Fe: 22.3

And liver results were okay too.

According to lab standards everything is in range (and nothing to worry) and could eventually get difficult to convince my doc for blood letting. I felt also a bit better after giving the blood for the lab yesterday and had much more energy than I used to have. But from lunch on, I was sleepy again which lasted then the rest of the day.

It takes a few days to really feel the benefits. The plasma replaces fastest and then the RBCs.

You could possibly feel better at about 50 of ferritin. Since you are young, that number may represent a gradual accumulation. See if your doctor will agree to bringing it down.
 

birk

Padawan Learner
On my last bloodtest my S-ferritin was 224 ( male33 years) and I would like to try to lower it to see if that can help with my eczema.
I will not be allowed to give blood and I suspect my doctor to have issues with me having bloodletting.

This has led me to consider Hirudotherapy(leeches), which is supposed to have quite some health benefits beyond the bloodletting.
Does anyone here have any experience whit this therapy?

Here is a link for anyone interested: _http://www.amazingleeches.com/

My apologies if this is off topic or noise in any way, I did a search on Hirudotherapy on the forum with no hits.
 

Gaby

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birk said:
This has led me to consider Hirudotherapy(leeches), which is supposed to have quite some health benefits beyond the bloodletting.
Does anyone here have any experience whit this therapy?

:/

That is very courageous of you.
 

Laura

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Geeze, before I'd let a leech touch me, I'd find a friend who was a nurse or something and get help unloading about a pint every couple of weeks. Surely you know someone who is trained? Why can't you talk to your doctor about it? Take some papers for him to read?
 
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