Hsp90 isoforms

Functions, expression and clinical importance

Review (2004)
Author(s)

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

Eva Kalmár (Semmelweis University)

Péter Csermely (Semmelweis University)

Yu Fei Shen (Chinese Academy of Sciences)

Affiliation
External organisation
DOI related publication
https://doi.org/10.1016/S0014-5793(04)00229-7
More Info
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Publication Year
2004
Language
English
Affiliation
External organisation
Issue number
1-3
Volume number
562
Pages (from-to)
11-15

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.

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