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Review
. 2020 Dec;235(12):9110-9120.
doi: 10.1002/jcp.29776. Epub 2020 May 26.

The role of HSP90 molecular chaperones in hepatocellular carcinoma

Masoud Nouri-Vaskeh  1   2 , Leila Alizadeh  3 , Khalil Hajiasgharzadeh  1 , Ahad Mokhtarzadeh  1 , Monireh Halimi  4 , Behzad Baradaran  1   5
Affiliations
Review

The role of HSP90 molecular chaperones in hepatocellular carcinoma

Masoud Nouri-Vaskeh et al. J Cell Physiol. 2020 Dec.

Abstract

Misfolded proteins have enhanced formation of toxic oligomers and nonfunctional protein copies lead to recruiting wild-type protein types. Heat shock protein 90 (HSP90) is a molecular chaperone generated by cells that are involved in many cellular functions through regulation of folding and/or localization of large multi-protein complexes as well as client proteins. HSP90 can regulate a number of different cellular processes including cell proliferation, motility, angiogenesis, signal transduction, and adaptation to stress. HSP90 makes the mutated oncoproteins able to avoid misfolding and degradation and permits the malignant transformation. As a result, HSP90 is an important factor in several signaling pathways associated with tumorigenicity, therapy resistance, and inhibiting apoptosis. Clinically, the upregulation of HSP90 expression in hepatocellular carcinoma (HCC) is linked with advanced stages and inappropriate survival in cases suffering from this kind of cancer. The present review comprehensively assesses HSP90 functions and its possible usefulness as a potential diagnostic biomarker and therapeutic option for HCC.

Keywords: chaperone proteins; heat shock protein 90; hepatocellular carcinoma; liver cancer.

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