A review of process on the Heat Shock Protein 90 (Hsp90) structural specificity and functional diversity

Gunasekar Manoharan * and Balaji Nagarajan

New Jersey Bioscience Centre, 675 US Highway 1, North Brunswick, New Jersey, 08902, United States.
 
Review
International Journal of Science and Research Archive, 2023, 08(02), 227–233.
Article DOI: 10.30574/ijsra.2023.8.2.0249
Publication history: 
Received on 13 February 2023; revised on 22 March 2023; accepted on 24 March 2023
 
Abstract: 
Heat Shock Protein 90 (Hsp90) is a molecular chaperone which plays an active role in maintaining protein homeostasis. Hsp90 is known to be highly expressed in tumour cells where it regulates stability and function of several key oncogenic client proteins including Akt kinase, EGFR, CDK and PDGFR. These client proteins are mutated or overexpressed in tumours and are involved in tumour progression and metastasis due to their roles in signaling pathways, cell cycle and apoptosis. Hsp90 has two isoforms, namely Hsp90α and Hsp90β and share 85% sequence homology. Hsp90β is the constitutive isoform, however, Hsp90α is highly induced in many cancers and is responsible for tumorigenesis.
 
Keywords: 
Heat Shock Protein 90 (Hsp90); Hsp90α and Hsp90β; Hemeprotein; Oncoproteins and metastasis
 
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