Betreff: HSP environ stress conditions..."cellular stress"....
Datum: Wed, 31 May 2006 11:43:46 EDT

Dear Olle:  Portions of this free but copyrighted Wikipedia site are copied in forward (some items removed to facilitate printing/saving ink).  
The portion re Hsp 70 indicating "thermal stress" might better be described as "cellular stress."  As you will note, there apparently really is one of the Hsp's that appears to be linked to actual high increases in temperature.   The Hsp 70 tho -- I believe, perhaps the most common Hsp that increases due to chronic, prolonged EMF/EMR exposures, may result not from a rise in temperature as a promoter, but rather, as a result of small increases in heat due to electron effects on cells and chronic inflammation
It seems that common usage of the term "heat shock" came about in the 1960's when a thermostat on fruit fly experiment(s) was turned-up overnight.  A tragedy of unbelievable proportions has resulted due to reliance on inappropriate use of facts based on what could almost be described as "a humorous event!!!"  Children are suffering and dying and young people such as Michael Boyum (age 23) who died from "preventable Leukemia" -- an electric clock and small fan was right behind his head -- continue not to have a voice, primarily  because of misuse of a term that has allowed government and industry to suppress, minimize and/or hide the truth!!! 
A lot of the info I have for the book indicates that "motion" induces heat......  Dehydration, as you know, plays a big part in cellular stress.  Enzyme Co-Q-10 -- necessary for cellular energy -- is reduced by toxic exposures which include nonionizing radiation.  Reductions in hormones such as Melatonin and changes in Serotonin levels, are all, I suspect not only results of stress due to EMR exposures but also are most likely an important part of the reason rises in heat shock proteins/cellular stress proteins induce protein misfolding which leads to formation of fibers and amyloid.
As you know, "protein folding research" in ongoing and is fairly recent.  However, the diseases/health problems related to protein misfolding and therefor the production of amyloid are numerous.   BSE or "mad cow disease," the TSE-like "Reactive Renal Amyloidosis identified at necropsy in one of my guinea pigs, Alzheimers, Type II Diabetes, Parkinsons, Multiple Sclerosis and much more including some of the Leukemias, all involve formation of amyloid.   Beta-amyloid also appears to be involved in glioma formation re brain tumors.
In other words, "amyloid" occurs in the form of misfolded protein fibers as result of chronic, prolonged cellular stress (a/k/a heat shock stress).  Such cellular stress is also known as "environmental stress" and the term "cellular stress due to toxic exposure," is also appropriate.   There are, of course, other toxic exposures including chemicals used in schools, workplaces and homes, sources of air pollution, mold, medications and more......."
Obviously combinations of exposures would be expected to increase amount of inflammation therefor raising the levels of environmental stress protein/cellular stress protein (heat shock protein). 
It is my "non-expert opinion" too that it is the variables in the levels of EMF/EMR environmental exposures such as distance from and amount of chronic, prolonged exposure particularly at night -- combined with one's own genetic susceptibilities/vulnerabilities -- as well as beneficial effects from healthy environmental effects from eating proper foods and getting enough exercise, etc. that determine whether a person suffers from allergic-type symptoms/sensitivity, chronic, annoying health problems, serious chronic health problems and/or dies. 
Variations in health problems appear to be considerable in regard to instances of sleeping close to electrical/telephone equipment, improper wiring/grounding, high frequencies on electrical wiring, etc. plus additional exposures such as residences being close to telecommunications' antennae, high voltage lines and there are increasing  concerns re use of wireless technology.  Daytime exposures including cell phone use further complicates such evaluations from an epidemiological standpoint.   As you know, literature does support that effects are cumulative.......
I know your work re EMF/EMR has stopped due to lack of funding.  I hope the additional information re misuse of "heat shock concept" will help you in a meaningful way when you do have opportunities to speak out.  Please don't be concerned about taking the time to respond.........   Take care  -  Joanne
Joanne C. Mueller
Guinea Pigs R Us
731 - 123rd Avenue N.W.
Minneapolis, Minnesota  55448-2127 USA
Phone:   763-755-6114
Email:  (5-31-06}
"LIGHT" is at the end of the tunnel for all to see and the lights we are holding get brighter each day in spite of an occasional flicker......THEY are frantically running in circles -- THEY are running into themselves -- THEY WON'T WIN -- It sure is great to be on the side of TRUTH!!!  Joanne C. Mueller 1-17-06
Be loyal to your country always, and to the government only when it deserves it.  -Mark Twain

Betreff: environ stress conditions
Datum: Tue, 30 May 2006 00:09:13 EDT


Heat shock protein

From Wikipedia, the free encyclopedia

Heat shock proteins (HSP) are a group of proteins whose expression is increased when the cells are exposed to elevated temperatures. This increase in expression is transcriptionally regulated. This dramatic upregulation of the heat shock proteins induced mostly by Heat Shock Factor (HSF) is a key part of the heat shock response. Production of high levels of heat shock proteins can also be triggered by exposure to different kinds of environmental stress conditions, such as infection, inflammation, exposure of the cell to toxins (ethanol, arsenic, trace metals and ultraviolet light, among many others), starvation, hypoxia (oxygen deprivation), nitrogen deficiency (in plants), or water deprivation. Consequently, the heat shock proteins are also referred to as stress proteins and their upregulation is sometimes described more generally as part of the stress response.

Scientists have not discovered exactly how heat-shock (or other environmental stressors) activates the heat-shock factor. However, some studies suggest that an increase in damaged or abnormal proteins brings HSPs into action.

Heat-shock proteins are present in all cells at all biological levels. They appear when the cell is under heat stress (or other stress). Heat-shock proteins also occur under non-stressful conditions, simply "monitoring" the cell's proteins. Some examples of their role as "monitors" are that they carry old proteins to the cell's "recycling bin" and they help newly synthesised proteins fold properly. These activities are part of a cell's own repair system, called the "cellular stress response" or the "heat-shock response." The function of heat-shock proteins is similar in virtually all living organisms, from bacteria to humans.

Heat shock proteins are molecular chaperones for protein molecules. They are usually cytoplasmic proteins and they perform functions in various intra-cellular processes. They play an important role in protein-protein interactions such as folding and assisting in the establishment of proper protein conformation (shape) and prevention of unwanted protein aggregation. By helping to stabilize partially unfolded proteins, HSPs aid in transporting proteins across membranes within the cell. Some members of the HSP family are expressed at low to moderate levels in all organisms because of their essential role in protein maintenance.

The HSPs are named according to their molecular weights, for example Hsp70 and Hsp90 each define families of chaperones. The major classes of heat shock proteins are tabulated below.



Potential applications

Heat-shock proteins are of potential interest to cancer researchers, based on research that has shown that animals may respond to cancer "vaccinations." Tumor cells were "attenuated" (or weakened) and injected in small quantities into a rodent, causing the rodent to become immune to future full-fledged tumor-cell injections. While any relevance of animal research to humans has not been established, it is possible that the same may hold true for other species.

Some physicians are conducting research on using heat shock proteins in the treatment of cancer. Some researchers speculate that HSPs may be involved in binding protein fragments from dead malignant cells and presenting them to the immune system.

Researchers are also investigating the role of HSPs in conferring stress tolerance to hybridized plants, hoping to address drought and poor soil conditions for farming.


Many years after the tumor cell attenuation research was done, Pramod Srivastava discovered that the specific part of the cell that was protecting the "immune" mice was the heat-shock proteins.

Susan Lindquist is currently a leading heat-shock protein researcher. She is investigating, among other things, "how HSPs are regulated, and how they function to protect organisms from death and from developmental anomalies induced by heat." - from her faculty page at:

Chaperones and heat shock proteins

The principal heat-shock proteins that have chaperone activity belong to five conserved classes: HSP100, HSP90, HSP70, HSP60 and the small heat-shock proteins (sHSPs).

Approximate molecular weight


Prokaryotic proteins Eukaryotic proteins Function
10 kDa GroES Hsp10
20-30 kDa GrpE The HspB group of Hsp. Ten members in mammals including Hsp27 or HspB1
40 kDa DnaJ Hsp40
60 kDa GroEL, 60kDa antigen Hsp60
70 kDa DnaK The HspA group of Hsp including Hsp71, Hsc70, Hsp72, Grp78, BiP, Hsx70 found only in primates Protein folding and unfolding, provides thermotolerance to cell on exposure to heat stress
90 kDa HtpG, C62.5 The HspC group of Hsp including Hsp90, Grp94 Maintenance of steroid receptors and transcription factors
100 kDa ClpB, ClpA, ClpX Hsp104, Hsp110 Tolerance of extreme temperature

Although the most important members of each family are tabulated here, it should be noted that some species may express additional chaperones, co-chaperones, and heat shock proteins not listed. Additionally, many of these proteins may have multiple splice variants (Hsp90╬▒ and Hsp90╬▓, for instance) or conflicts of nomenclature (Hsp72 is sometimes called Hsp70).

See also

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