The 60 kDa heat shock chaperonin protein 60 (Hsp60 or Cpn60) is highly conserved in
evolution and present in nearly all organisms. Eukaryotic paralogues are nuclear encoded but act in certain
intra- and extracellular compartments including venous blood. HSP60s function as ATP-dependent
molecular chaperones and collaborate with further chaperones to perform their duties. While intracellular
HSP60s are crucially involved in proteostasis as well as pro-apoptotic and pro-survival pathways,
membrane-bound and extracellular HSP60s are thought to function as danger signals to the immune
system and act as powerful immune mediators. HSP60s are released into the peripheral blood from healthy
subjects and under a variety of pathological conditions, including cardiovascular diseases and cancer.
Hsp60 levels successively rise or decline during tumorigenesis in diverse organs. Hsp60 over-expression
in cancer cells stimulates cell proliferation, blocks senescence as well as stress-induced apoptosis, and
facilitates oncogenic transformation. This chaperone might thus have future applicability as biomarker for
diagnosis and assessing prognosis or response to therapeutic intervention. Hsp60 chaperonopathies
represent the basis for targeting Hsp60 for the development of novel agents affecting its activity. This
review summarizes recent knowledge and new perspectives on the Hsp60 chaperone machinery and its
role in disease and therapy.
Keywords: Hsp60, chaperonin, structure, regulation, disease relevance, inhibitors, function, therapeutic implications.
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