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Current Pharmaceutical Design

Editor-in-Chief

ISSN (Print): 1381-6128
ISSN (Online): 1873-4286

Mini-Review Article

An Insight to Heat Shock Protein 90: A Remedy for Multiple Problems

Author(s): Megha Yadav, Ankit Kumar Singh, Adarsh Kumar, Suresh Thareja and Pradeep Kumar*

Volume 28, Issue 32, 2022

Published on: 08 September, 2022

Page: [2664 - 2676] Pages: 13

DOI: 10.2174/1381612828666220829120630

Price: $65

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Abstract

Heat shock protein 90 (Hsp90) is a chaperone protein that prevents many other proteins from aggregating by folding them in a certain way. Hsp90 consists of three structural domains: N-terminal, middle and C-terminal domains. Hsp90 has many activities in numerous proteins and signaling pathways like chimeric fusion proteins, steroid hormone receptors, tumor suppressor genes, and cell cycle regulatory proteins. The role of Hsp90 is not only in cancer but also in other diseases like COVID-19, leishmaniasis, diabetes, flavi virus, systemic sclerosis, grass carp reovirus, psoriasis, malaria, cardiac fibrosis, and alcohol-related liver diseases. This review is a compilation of the pharmacological profile of Hsp90 inhibitors, problems associated with them, and suggested remedies for the same.

Keywords: Hsp90, chaperones, cancer, proteosome, geldanamycin, radicicol.

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