Heat Shock Proteins and Infrared Frequencies: Natural Immune Responses Enhanced with Infrared
Robert A. Besner - Professor of Infrared and Applied Infrared Sciences - Anpan Business School
Prepared for: 28th World Conference on Infrared Infrared Medical Conference - Shenzhen, China November, 2014
For more than a century, scientists from different points of the globe have studied the positive influences of the Sun’s energy on all living things on Earth. Recently, medical research has been focusing on cellular health and the mechanisms within the body that protect and provide all the components to extend the health of the human cell. One aspect that has presented itself is the body’s own natural defenses against invaders (bacteria, microphages, parasites, pathogens etc.) and the immunological response of T-cells.
Heat Shock Proteins (hereinafter referred to as “HSP”) play an integral part in initiating and directing the body’s natural immune response. The recent discovery that Heat Shock Proteins can be produced by exposure to infrared thermal frequencies has launched a new campaign to define how these chaperones of the immune system serve and protect the integrity of cellular health.
This campaign commences with a series of introductory questions defining the biology and the functional biology involved.
- What are heat shock proteins ?
- When are heat shock proteins created by the human body?
- How do heat shock proteins influence cellular health?
- What are the long-term research needs of heat shock proteins?
The induction of HSP-directed T-cell reactivity can be triggered by various natural stress inducers, including fever and mechanical stress, natural exposure to microbial invasion or infection,
or through commensal gut micro-flora. In addition, non-natural stress inducers, including hyperthermia, HSP-inducing drugs (such as non-steroidal anti-inflammatory drugs and aspirin), whole cell vaccines, and HSPderived peptides, can also serve as factors in the initiation of the HSP response.
What are these things called Heat Shock Proteins?
By definition, heat shock proteins are a large family of inducible-expressed protein “chaperones” involved in assisting protein folding and unfolding within the cells. This folding and unfolding process is an aspect of cellular mechanics only recently occupying the interest and time of researchers. In brief, protein molecules are the yeomen responsible for virtually all cellular biological functions. 1
These specific protein molecules we call heat shock proteins are ubiquitous and are vital watchdog assistants to our living cells. But while the research in this area is still in an infancy stage as, the realization of the immunological significance of HSPs is growing as fast as HSP research is extensive.
As these proteins prepare for their various duties, they actually fold into exact three dimensional shapes. If these chain-like molecules fail to correctly fold, researchers are finding that
such incorrect folding may be the cause of a number of ailments such as Alzheimer’s and Parkinson’s.
We know from the research of genetic coding that most biological functions at the cellular level are the responsibility of proteins. Human cells contain an astoundingly diverse number of proteins, serving a variety of fundamental functions in cellular metabolism, cell development, and cell regulation. Each unique protein corresponds to a specific sequence of amino acids. However, notwithstanding its DNA/RNA coding, new protein chains are quite impotent.
It is only functionally active when it adopts an exact, defined three-dimensional pattern of fold. In order to complete the folding process when protein chains morph into unique three-dimensional models, protein chains require assistance of this cellular level function by “molecular chaperones.” Though there are many molecular chapeones, many of them are stress proteins or heat shock proteins. Their basic function is to assist those cells under conditions of stress to synthesize and unfold, creating a complex myriad of
protein quality control. Incorrect,
abnormal folding creates proteins that are toxic to cells and cell functions. General theory suggests that HSPs become present when a protein chain fails to fold correctly and thus fails to fulfill its biological function. The HSP chaperones appear and step in to assist the aberrant protein in self-correction. In the dense and highly congested cellular environment, HSPs also protect undeveloped proteins from ultimately misfolding and clumping together (also known as “aggregating”).
When are heat shock proteins created by the human body?
The timing and interaction of HSPs with an unhealthy cell structure is a current subject of much research.2 Part of that research includes the interaction of infrared heat as a trigger or an enhancement to the introduction of HSPs at the cellular level.
2. M.Y. Sherman and A. L. Goldberg, “Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases, Neuron 29, 15-32 (2001).
Studies have shown that the application of targeted, penetrative heat to the body, such as heat caused by thermal energy at the infrared frequencies, can stimulate a wide range of beneficial outcomes, including a strengthened immune system, stress relief, and even (to a degree) cancer management. The practical implications of HSPs are now being examined by a number of well-designed clinical trials. HSPs may play yet more fundamental roles in immune responses because of a series of surprising findings that
they can modulate the functions of antigen presenting cells, in a receptor-dependent manner.
HSPs are created by the human body when the body senses a fear, a biological change in the proper balance of cellular functioning. Though HSPs are normally found in cells under balanced conditions (primarily to assist and chaperone in molecular self-correction), they become present in higher levels when exposed to a sudden temperature jump or other stressors.
What differentiates HSPs from other proteins naturally formed by the body? As the name suggests, heat plays a critical role. Heat shock proteins are stimulated in response to abnormally high body temperatures and or the environmental and physiological stressors normally imposed. These special proteins, as molecular chaperones, are generated in part to help protect the cell from the stress of exposure to high temperatures and other influences, exposure that typically indicates a threat or danger to the overall body in general and the overall body’s homeostasis in particular.
Infrared frequencies can enhance the body’s internal natural healing mechanism,
by targeting cells with temperatures high enough to stimulate heat shock proteins but still low enough to avoid cell damage.
Infrared Frequencies and Temperature Rise
Many of the positive effects attributed to heat-based health therapies (also known as thermo-therapies or hyper-thermic treatments) can be traced back to specific stressor proteins including HSPs. These proteins are an integral part of the cell’s internal repair mechanism for once HSPs sense stress or a sudden temperature rise, their functional duty in our biology includes:
- Enhancing our immune system function by helping make healthy cells stronger and therefore more resistant to disease.
- Further coordinating with our immune system to create clear biomarkers, or a “road map” to damaged cells that are more likely to fall prey to infection. By expelling old, damaged or aberrant proteins from within the cell walls, HSPs allow the immune system to more accurately identify cells that are deteriorating, malfunctioning, or threatening overall cellular health. HSPs clearly influences the body’s expressed desire for homeostasis.
- Ensuring normal cellular proteins formation, growth, and function), serving as a cellular level type traffic engineer by transferring proteins to different parts of the cell.
- Assisting the cell to safely eliminate old, damaged proteins as waste products.
- Alerting the immune system to the presence of cells with damaged, unformed, or malformed proteins.
- Repairing mis-folded, damaged proteins thereby ensuring proteins have their proper structure and function.
- Providing preventative maintenance by directly scavenging free radicals and also by supporting cellular antioxidant capacity through its effects on maintaining glutathione.
How do HSPs influence cellular health?
The Body’s GPS for the T-Cells to Search and Destroy
Increasing evidence suggests that HSPs may play important roles in both innate and adaptive immunity. 3
In combating against infections, antigen-presenting cells (also known as accessory cells) serve to seek out antigen materials and bring it to the cell surface. Ultimately, this unwanted material is handed over to the T-Cells of the body’s immune system. This mechanism can be activated by a variety of microbial molecules, such as lipopolysaccharide, and un-methylated components of DNA, which then trigger adaptive Tcell and B-cell immunity reactants4. For generating immune responses against tumors, allografts, and other self-generated antigens, there is a need for endogenous non-microbial molecules that activate these accessory cells. Studies thus far suggest that HSPs could be such endogenous molecules that activate accessory cells. And HSPs would be triggered by a natural enhancement of infrared heat.
3 Javid Babak, Paul MacAry, and Paul Lehner, Paul, “Structure and Function: Heat Shock Proteins ad Adaptive Immunity”, J Immunol 2007; 179:2035-2040 4 Valentina Tremaroli, and Fredrick Backhed, Fredrik, ”Functional Interactions Between the Gut Microbiota and host Metabolism”, Nature 489, 242–249 (13 September 2012):
HSP Research Inspires Cancer Treatment Applications
The ability of heat shock proteins to flag diseased cells for the body’s immune system is of particular interest to cancer researchers. Some researchers speculate that heat shock proteins bind with protein fragments from dead malignant cells and present them to the immune system. The immune system is then able to dispose of these malignant cells more efficiently and completely. In addition, heat shock proteins can activate lymphocytes that promote the synthesis of anti-cancer interferons to strengthen the body’s immune system.5
HSP Stimulate HGH for Muscle Repair
Research has shown that when rats were exposed to intermittent heat sessions, they had a "robust" expression of heat shock proteins
that was associated with 30 percent more muscle regrowth compared to a control group.6 The expression of HSPs persisted for up to 48 hours after the heat session and may actually lead to a higher expression of heat shock proteins even when you are not exercising. When you do exercise, heat acclimation may prompt an even greater release in HSPs than normal.7
"This is a great example of how a person can theoretically use hyper-thermic conditioning to increase their own heat shock proteins and thereby reap the rewards," including muscle growth and more, according to Dr. Rhonda Patrick.8 Human Growth Hormone (HGH) is the foundational biochemical that addresses allserious muscle loss and muscle repair. The bio thermal induced by the resonance effect of Infrared frequency will initiate the HSP response that will in turn trigger the HGH that the body produces to repair and build muscle. Exposure to heat has been shown to increase lifespan (by up to 15% percent) in flies and worms, a benefit that is attributed to HSPs.9 One particular HSP (the HSP70 gene) has also been associated with increased longevity, which suggests there may be anti-aging benefits to regular infrared heat stress.10
5 Charu Kapoor, “Heat Shock Protein (HSP) and Cancer: an Overview,” Am. J. Med.Dent. Sci., 2013, 1(1): 31-34 6 Kimberly A. Huey, “Regulation of HSP25 expression and phosphorylation in functionally overloaded rat plantaris and soleus muscles,” J. App. Phys., 2006, 100(2): 451-456 7 Ibid. 8 http://www.fourhourworkweek.com/blog/2014/04/10/saunas-hyperthermic-conditioning/ itunes 9 Ibid. 10 Ibid.
Infrared Heat Supports Muscle Recovery After an Injury
Heat treatments even induce heat shock proteins HSPs that help protect against rhabdomyolysis, a serious degenerative muscle tissue condition that is one of the most common side effects associated with the use of statin cholesterol-lowering drugs.11 If you've had a muscle injury, you may be immobilized for lengthy periods, which generally will cause your muscles to begin to atrophy. Hyper-thermic conditioning with the use of infrared heat has been shown to slow muscle atrophy during disuse by up to 32 % percent in one animal study.12
Whole-body heat treatment both prevents muscle atrophy and increases muscle regrowth, courtesy of elevated HSP levels. During injury, you may be immobilized but you do not have to be very mobile to use an infrared heating pad or sit in the infrared sauna a few times a week to boost your HSPs. All indications suggest utilizing infrared frequencies to create a bio-thermal will enhance the injury and recovery process.
HSP Triggers Increased Insulin Sensitivity
Insulin performs multiple functions in your body. It helps mobilize or signal a certain kind of protein to mobilize glucose from outside your cells, and it is part of the mTOR (Mammalian Target of Rapamycin) mechanism, which causes protein to be created and build muscle.13 The mechanism that builds protein in your muscles is part of the insulin cascade pathway, and it cannot be bypassed.
While it is common knowledge that in order to build protein in the muscle and grow muscle, the body must activate the mTOR mechanism. In reaction, the muscle is signaled to build protein. If your insulin receptors are insensitive, like with type 2 diabetes, muscle wasting is inevitable. HSP keeps those insulin receptors sensitive and assists in regulating protein metabolism by inhibiting protein degradation.
Specifically, insulin works by increasing protein synthesis by stimulating the uptake of amino acids into skeletal muscle and decreasing protein degradation by inhibiting proteasome, a protein complex that is responsible for cellular protein degradation.14
Hyper thermic conditioning is also known to help improve insulin sensitivity, which may be yet another route by which it ultimately boosts muscle growth and performance.
One animal study even found that 30 minutes of hyper thermic treatment, three times a week for 12 weeks, resulted in a 31% percent decrease in insulin levels and a significant reduction in blood sugar levels. This has implications not only for your muscles, of course, but also for the many other chronic diseases that are driven by insulin resistance, like type 2 diabetes and metabolic syndrome.
11 Ibid. 12 Ibid. 13 M. V. Blagosklonny, “TOR-centric view on insulin resistance and diabetic complications: perspective for endocrinologists and gerontologists,” Cell Death and Disease, 2013, : e964 14 Ibid.
Infrared Bio Thermo-therapy
Infrared bio-thermals can encourage the synthesis of heat shock proteins by using infrared heat to create an environment for the body that allows HSPs to achieve a thermo-therapy treatment at a mild, deep, long lasting bio-heat. The physiological experience is enhanced by introducing the healing qualities of gemstones, allowing the synergistic effects to channel the far infrared rays to transfer directly into the body and ultimately the cell. Uniquely qualified infrared frequency has a lower originating temperature so that there is still ample enough bio thermal created to stimulate the development of these beneficial HSP proteins without causing cell damage.
To stimulate the creation of heat shock proteins and use the available infrared frequency influence, the human body receives negative ion therapy plus deeppenetrating warmth and temperature elevation. Utilization of infrared frequencies to induce higher temperatures will direct the production of HSPs to a particular area of muscle or organ repair. Palpation will demonstrate relatively cool sensation; while you will feel a pleasant sensation of warmth throughout your body the far infrared rays can safely penetrate deeply into your body. You may also find yourself sweating as your body temperature climbs. This is a perfectly normal part of the bio resonance heat therapy.
What are the long-term research needs of HSP and Infrared?
The role of heat shock proteins in treatments for immune deficiencies and cancer is ongoing. The use of heat shock proteins in treating existing conditions and predicting response to anticancer treatments is becoming more and more widespread, and is even being used in anticancer vaccines. The ongoing study of heat shock proteins continues to yield great contributions to basic and clinical cancer research.
Conclusion
Infrared frequency serves as a fundamental natural stress inducer. The heat shock proteins triggered by Infrared play an integral part in initiating and directing the body’s natural immune response. While the induction of HSPs can be initiated by various natural stress inducers, it can also be induced by non-natural stress influences. In both cases, the promotion of HSP leads to a natural immunological response and cascading benefits for cellular health and overall health of the human body.
Sources:
Babak, Javid, MacAry, Paul, and Lehner, Paul. Structure and Function: Heat Shock Proteins ad Adaptive Immunity. J Immunol 2007; 179:2035-2040
Balch, W. E., Morimoto, R. I., Dillin, A. & Kelly, J. W. Adapting proteostasis for disease intervention. Science 319, 916-919 (2008
Blagosklonny,.V. “TOR-centric view on insulin resistance and diabetic complications: perspective for endocrinologists and gerontologists,” Cell Death and Disease, 2013, : e964
Brignull, H. R., Morley, J. F. & Morimoto, R. I. The stress of misfolded proteins: C. elegans models for neurodegenerative disease and aging. Adv Exp Med Biol. 594:1- 13 594, 167-189 (2007).
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Huey, Kimberly A. “Regulation of HSP25 expression and phosphorylation in functionally overloaded rat plantaris and soleus muscles,” J. App. Phys., 2006, 100(2): 451-456
Kapoor, Charu. “Heat Shock Protein (HSP) and Cancer: an Overview,” Am. J. Med.Dent. Sci., 2013, 1(1): 31-34
Sherman, M. Y. & Goldberg, A. L. Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases. Neuron 29, 15-32 (2001).
Valentina Tremaroli, Backhed, Fredrik. Functional Interactions Bentween the Gut Microbiota and host Metabolism. Nature 489, 242–249 (13 September 2012):
Winklhofer, K. F., Tatzelt, J. & Haass, C. The two faces of protein misfolding: gainand loss-of-function in neurodegenerative diseases. Embo J 27, 336-349 (2008).
Professor Besner was appointed full professorship status by ANPAN Business School in 2013 in infrared and in applied studies of infrared science in 2014. Formally educated at Boston University, Mr. Besner was granted a Bachelor of Science Degree from that institution for his studies in psychology, biology, and Business Administration. He subsequently engaged in graduate study and research at Case Western University’s Graduate School of Biology/Anatomy in Cleveland, Ohio. He has lectured extensively on infrared and the application of infrared sciences on behalf of Therasage.