Heat shock protein 60 (HSP60) (HSP60)

Heat shock protein 60 (HSP60), encoded by the HSPD1 gene, is a ubiquitous molecular chaperone primarily localized within the mitochondrial matrix, where it plays a critical role in protein folding and quality control [1, 5]. In many types of cancer, HSP60 is overexpressed and undergoes an unconventional translocation to the cytosol and the plasma membrane, where it serves as a tumor-associated antigen [2, 3]. On the cell surface, HSP60 can interact with the immune system and participate in pro-survival signaling pathways that facilitate tumor progression and metastasis [4]. Therapeutic approaches targeting HSP60 include small-molecule inhibitors that block its ATPase activity and monoclonal antibodies designed to recognize surface-expressed epitopes [5]. However, the ubiquitous nature of HSP60 and its essential role in normal mitochondrial function present significant challenges for drug development, requiring high specificity for the tumor-associated forms to minimize off-target toxicity and autoimmune risks [3, 4].

Other names

Chaperonin 60CPN60HSPD1Mitochondrial matrix protein P1P60 lymphocyte proteinHuCHA60Ubiquitous mitochondrial protein translocated to tumor cell surface

Inhibition of ATPase-dependent protein folding activity, disruption of mitochondrial proteostasis, and induction of apoptosis in cancer cells [4, 5].