Hsp90 isoforms: Functions, expression and clinical importance

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

Research output: Contribution to journalShort surveypeer-review

436 Citations (Scopus)


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
Issue number1-3
Publication statusPublished - 2004
Externally publishedYes


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


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