| Literature DB >> 31713482 |
Qiang Shan1, Fengtao Ma1, Jingya Wei1, Hongyang Li1, Hui Ma2, Peng Sun1.
Abstract
Heat shock proteins (HSPs) are molecular chaperones involved in a variety of life activities. HSPs function in the refolding of misfolded proteins, thereby contributing to the maintenance of cellular homeostasis. Heat shock factor (HSF) is activated in response to environmental stresses and binds to heat shock elements (HSEs), promoting HSP translation and thus the production of high levels of HSPs to prevent damage to the organism. Here, we summarize the role of molecular chaperones as anti-heat stress molecules and their involvement in immune responses and the modulation of apoptosis. In addition, we review the potential application of HSPs to cancer therapy, general medicine, and the treatment of heart disease. Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.Entities:
Keywords: Heat shock proteins; antioxidation; heat shock factor; immunity; molecular chaperone; tumor
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Year: 2020 PMID： 31713482 DOI： 10.2174/1389203720666191111113726
Source DB: PubMed Journal: Curr Protein Pept Sci ISSN： 1389-2037 Impact factor: 3.272