The role of HSP90 molecular chaperones in hepatocellular carcinoma.
Masoud Nouri-VaskehLeila AlizadehKhalil Haji-AsgarzadehAhad MokhtarzadehMonireh HalimiBehzad BaradaranPublished in: Journal of cellular physiology (2020)
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.
Keyphrases
- heat shock protein
- heat shock
- cell proliferation
- signaling pathway
- heat stress
- poor prognosis
- cell cycle arrest
- wild type
- induced apoptosis
- oxidative stress
- squamous cell carcinoma
- endoplasmic reticulum stress
- pi k akt
- endothelial cells
- cell death
- escherichia coli
- stem cells
- neuroendocrine tumors
- cell therapy
- staphylococcus aureus
- small molecule
- smoking cessation
- risk assessment
- squamous cell
- human health