Heat shock proteins (HSPs) are ubiquitous and evolutionary conserved proteins induced by cell stress. HSP60, in particular, is
a typical mitochondrial molecular chaperone that is known to assist nascent polypeptides to reach a native conformation. HSP60 is also
known to interact with HSP10. In the last decade, HSP60 has been detected in the cytosol, the cell surface, the extracellular space, and
biological fluids. HSP60 elicits potent proinflammatory response in cells of the innate immune system and serves as a danger signal of
stressed or damaged cells. As cytosolic HSP60 levels gradually increase or decrease during carcinogenesis in various organs, HSP60 can
be used as a biomarker for the diagnosis and prognosis of preneoplastic and neoplastic lesions. In this review, we summarize recent discoveries
on the important roles of HSP60 in various diseases ranging from autoimmune diseases to tumors. Furthermore, small molecules
targeting HSP60, which were the target of intensive investigations in the last few years, are also summarized. The possibility of utilizing
HSP60 as a new drug target for the treatment of certain diseases is examined.
Keywords: HSP60, molecular chaperone, apoptosis, proinflammatory response, biomarker, carcinogenesis, inhibitor, cell stress, diagnosis, prognosis.
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