The role of HSP90 molecular chaperones in hepatocellular carcinoma

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 local...

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Published in:Journal of cellular physiology 2020-12, Vol.235 (12), p.9110-9120
Main Authors: Nouri‐Vaskeh, Masoud, Alizadeh, Leila, Hajiasgharzadeh, Khalil, Mokhtarzadeh, Ahad, Halimi, Monireh, Baradaran, Behzad
Format: Article
Language:English
Subjects:
Angiogenesis
Apoptosis
Biomarkers
Cancer
Carcinoma, Hepatocellular - metabolism
Cell proliferation
Cell Proliferation - physiology
Cell Transformation, Neoplastic - metabolism
chaperone proteins
Chaperones
Diagnostic systems
heat shock protein 90
Heat shock proteins
Hepatocellular carcinoma
HSP90 Heat-Shock Proteins - metabolism
Hsp90 protein
Humans
Liver cancer
Liver Neoplasms - metabolism
Localization
Oligomers
Protein folding
Proteins
Signal processing
Signal Transduction
Tumorigenicity
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Summary: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. The main focus of this study is the structural, mechanistic, and therapeutic studies that have been conducted to explain how heat shock protein 90 molecular chaperone and its inhibitors act on different processes involved in hepatocellular carcinoma development and progression.
ISSN:0021-9541
1097-4652
DOI:10.1002/jcp.29776