Hsp90 isoforms

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Hsp90 isoforms

Functions, expression and clinical importance

Review (2004)

Author(s)

Amere Subbarao Sreedhar (Semmelweis University, Ctr. for Cell. and Molecular Biology)

Éva Kalmár (Semmelweis University)

Péter Csermely (Semmelweis University)

Yu Fei Shen (Chinese Academy of Sciences)

Stress Anticancer drug Chaperone Heat shock protein Molecular evolution Tumor therapy

DOI related publication

https://doi.org/10.1016/S0014-5793(04)00229-7 Final published version

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https://resolver.tudelft.nl/uuid:6d8ac561-3779-4326-9fd3-d9c46fdda11e

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Publication Year

2004

Language

English

Issue number

1-3

Volume number

562

Pages (from-to)

11-15

Downloads counter

162

Abstract

The 90 kDa heat shock protein, Hsp90, is a main functional component of an important cytoplasmic chaperone complex, and it is involved in various cellular processes, such as cell proliferation, differentiation and apoptosis. Identification of Hsp90 as a molecular target of various anticancer drugs highlighted its importance from the clinical point of view. Here we summarize the current knowledge on various Hsp90 isoforms regarding their genomic location, molecular evolution, functional differences, differential induction after various environmental stresses and in pathological conditions as well as the growing importance of discriminating between Hsp90 isoforms in clinical practice.