Premium
The role of HSP90 molecular chaperones in hepatocellular carcinoma
Author(s) -
NouriVaskeh Masoud,
Alizadeh Leila,
Hajiasgharzadeh Khalil,
Mokhtarzadeh Ahad,
Halimi Monireh,
Baradaran Behzad
Publication year - 2020
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.29776
Subject(s) - hsp90 , heat shock protein , hepatocellular carcinoma , signal transduction , cancer research , chaperone (clinical) , motility , downregulation and upregulation , biology , protein folding , microbiology and biotechnology , biomarker , biochemistry , medicine , pathology , gene
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.