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Heat shock protein
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[[File:Wiki commons hsp.png|thumb|HSPA1A|286x286px]] '''Heat shock proteins''' (HSP) are a family of [[protein]]n that are produced by cells in response to exposure to stressful conditions, including exposure to [[Thermotherapy|heat]], [[Cryotherapy|cold]], [[UV light]], [[infection]], [[exercise]], [[starvation]]; [[fasting]] and [[hypoxia]].<ref name="Zare2011">{{Cite journal | last = Zare | first = A | date = July 2011 | title = Effect of Ramadan fasting on serum heat shock protein 70 and serum lipid profile| url = https://www.ncbi.nlm.nih.gov/pubmed/21808959|journal=Singapore Med J.|volume=52|issue =7 | pages = 491-5|via=}}</ref> Heat shock proteins are classified by their molecular weight (e.g. hsp10, hsp40, hsp60, hsp70, ect). ==Function== Heat shock proteins play the role of a chaperone for other proteins and significant part of the body's physiological stress response. HSPs are found in all cells of all organisms. These proteins also play a role in protecting from stress/apoptosis.<ref name="Li2004">{{Cite journal| url = https://www.ncbi.nlm.nih.gov/pubmed/18432918 | title = Heat-shock proteins | last = Li | first = Z | last2 = Srivastava | first2 = P | date = 2004|journal=Curr Protoc Immunol|volume=|issue=Appendix 1T | pages = |doi=10.1002/0471142735.ima01ts58|pmid =18432918|pmc=|archive-date=|url-status=|access-date=}}</ref> More specifically they also inhibit protein degradation, and as a result they inhibit [[skeletal muscle atrophy]]. <ref name="Patrick2016">{{Cite web | url = https://articles.mercola.com/sites/articles/archive/2016/05/01/health-benefits-extreme-hot-cold-temperatures.aspx?x_cid=youtube | title = The Surprising Health Benefits of Extreme Hot and Cold Temperatures | last = Patrick | first = Rhonda | date = |website=Mercola|archive-url=|archive-date=|url-status=|access-date=}}</ref> Certain HSPs appear play [[cytoprotective]] role in many human diseases, including [[ischemia]], [[inflammation]], and infection.<ref name="Gabriella1999">{{Cite journal | last = Gabriella | first = Santoro | date = June 1999 | title = Heat shock factors and the control of the stress response| url = https://www.sciencedirect.com/science/article/abs/pii/S0006295299002993#!|journal=Biochemical Pharmacology|volume=59 | pages = 55-63|via=}}</ref> ==ME/CFS== A [[Canada|Canadian]] research team first reported a decrease of heat shock proteins in [[ME/CFS]] patients after an exercise challenge.<ref name="Thambirajah2008"/> Further study was done by a [[France|French]] team interested in increased [[oxidative stress]] in ME/CFS patients. In 2009 they reported a marked reduction of HSP 27 and HSP 70 variations in ME/CFS patients post-exercise, a reduction that was not seen in heathy controls.<ref name="James2009"/> These results were confirmed in 2012, using a larger sample of 43 ME/CFS patients.<ref name="James2012"/> [[Heat shock protein family A (Hsp70) member 2|HSPA2]], a heat shock protein-encoding gene, may also have a role in ME/CFS.{{citation needed | date = 2022}} == Hormesis == Heat shock proteins, have been shown to trigger [[hormesis]] in humans, and as a result [[mitochondrial biogenesis]]. Perhaps future treatments will incorporate either HSPs or other hormesis activating compounds, as a means to foster [[mitochondrion|mitochondrial]] growth/repair. ==Notable studies== *2012, Chronic fatigue syndrome: acute infection and history of physical activity affect resting levels and response to exercise of plasma oxidant/antioxidant status and heat shock proteins<ref name="James2012">{{Cite journal | last = Jammes | first = Y. | last2 = Steinberg | first2 = J.G. | last3 = Delliaux | first3 = S. | date = Jul 2012 | title = Chronic fatigue syndrome: acute infection and history of physical activity affect resting levels and response to exercise of plasma oxidant/antioxidant status and heat shock proteins| url = https://www.ncbi.nlm.nih.gov/pubmed/22112145|journal=Journal of Internal Medicine|volume=272|issue=1 | pages = 74β84|doi=10.1111/j.1365-2796.2011.02488.x|issn=1365-2796|pmid=22112145}}</ref> - [https://www.ncbi.nlm.nih.gov/pubmed/22112145 (Abstract)] *2009, Chronic fatigue syndrome combines increased exercise-induced oxidative stress and reduced cytokine and Hsp responses<ref name="James2009">{{Cite journal | last = Jammes | first = Y. | last2 = Steinberg | first2 = J.G. | last3 = Delliaux | first3 = S. | last4 = BrΓ©geon | first4 = F. | date = Aug 2009 | title = Chronic fatigue syndrome combines increased exercise-induced oxidative stress and reduced cytokine and Hsp responses| url = https://www.ncbi.nlm.nih.gov/pubmed/19457057|journal=Journal of Internal Medicine|volume=266|issue=2 | pages = 196β206|doi=10.1111/j.1365-2796.2009.02079.x|issn=1365-2796|pmid=19457057}}</ref> - [https://www.ncbi.nlm.nih.gov/pubmed/19457057 (Full text)] *2008, Differential heat shock protein responses to strenuous standardized exercise in chronic fatigue syndrome patients and matched healthy controls<ref name="Thambirajah2008">{{Cite journal | last = Thambirajah | first = Anita A. | last2 = Sleigh | first2 = Kenna | last3 = Stiver | first3 = H. Grant | last4 = Chow | first4 = Anthony W. | date = 2008-12-01 | title = Differential heat shock protein responses to strenuous standardized exercise in chronic fatigue syndrome patients and matched healthy controls| url = https://www.ncbi.nlm.nih.gov/pubmed/19032901|journal=Clinical and Investigative Medicine. Medecine Clinique Et Experimentale|volume=31|issue=6| pages = E319β327|issn=1488-2353|pmid=19032901}}</ref> - [https://www.ncbi.nlm.nih.gov/pubmed/19032901 (Abstract)] *2006, - [ (Full text)] ==See also== *[[Cold shock protein]] *[[Heat shock protein family A (Hsp70) member 2]] (HSPA2 gene) ==Learn more== *[https://www.scientificamerican.com/article/roles-of-heat-shock-proteins/ Roles of Heat Shock Proteins] - Scientific American ==References== {{Reflist}} [[Category:Proteins]] [[Category:Stress response]]
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