Hsp90 isoforms: Functions, expression and clinical importance

Amere Subbarao Sreedhar, Éva Kalmár, Péter Csermely*, Yu Fei Shen

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

511 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)11-15
JournalFEBS Letters
Volume562
Issue number1-3
DOIs
Publication statusPublished - 2004
Externally publishedYes

Keywords

  • Anticancer drug
  • Chaperone
  • Heat shock protein
  • Molecular evolution
  • Stress
  • Tumor therapy

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