Heat Shock Proteins (HSP)

Heat shock proteins (HSP) are found in virtually all living organisms, from bacteria to humans. HSPs are a family of proteins that are produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock.

Published below studies have shown that exposure to heat induces the body to produce HSP's that perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by cell stress. Improper folding of proteins and damaged proteins have been reported to cause a large number of diseases.

Heat-shock proteins are named according to their molecular weight. For example, Hsp60, Hsp70, and Hsp90 (the most widely studied HSPs) refer to families of heat shock proteins on the order of 60, 70, and 90 kilodaltons in size, respectively.

20-30 minutes of high heat thermotherapy stimulates the biosynthesis of Heat Shock Proteins. And HSP compounds play an essential part in body resistance against diseases.

Some researchers consider that every other day short sessions could be enough to stimulate immunity and avoid adaptation to heat and thermotolerance.

You can find more information about HSP in the articles below linked from PubMed. PubMed is a searchable database of the U.S. National Library of Medicine (NLM) and the National Institutes of Health (NIH), with more than 27 million citations for biomedical literature from MEDLINE, life science journals, and online books. It is the primary source of information about the newest health technologies, medicines, and treatment researches and studies.

Heat Stress and Cardiovascular, Hormonal, and Heat Shock Proteins in Humans
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3418130/

Heat Shock Proteins as Immunomodulants
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6278532/

Extracellular cell stress (heat shock) proteins—immune responses and disease: an overview
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5717522/

Heat-shock proteins as dendritic cell-targeting vaccines – getting warmer.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3719058/

Heat shock proteins HSPB8 and DNAJC5B have HCV (Hepatitic C Virus) antiviral activity.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5705118/

The heat shock response restricts virus infection in Drosophila.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4522674/

Role of Heat Shock Proteins in Protection from and Pathogenesis of Infectious Diseases
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC88905/

Heat Shock Proteins in Cancer Immunotherapy
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6927063/

Short-Term Heat Shock Affects Host–Virus Interaction in Mice Infected with Highly Pathogenic Avian Influenza Virus H5N1
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4908103/

Heat Shock Protein 70 Modulates Influenza A Virus Polymerase Activity
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3953273/

Heat shock proteins in neurodegenerative disorders and aging
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4390795/