title: Hsp90 isoforms: functions, expression and clinical importance.
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 of 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.
authors.affiliation: Department of Medical Chemistry, Semmelweis University School of Medicine, Budapest, Hungary.
authors.forename: Amere Subbarao
authors.initials: AS
authors.lastname: Sreedhar
authors.forename: Eva
authors.initials: E
authors.lastname: Kalmár
authors.forename: Péter
authors.initials: P
authors.lastname: Csermely
authors.forename: Yu-Fei
authors.initials: YF
authors.lastname: Shen
mesh_terms: D000818:Animals; D000970:Antineoplastic Agents / Q000378:metabolism; D019143:Evolution, Molecular; D018841:HSP90 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism; D009369:Neoplasms / Q000378:metabolism; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism*
chemical_list: D000970:Antineoplastic Agents; D018841:HSP90 Heat-Shock Proteins; D018832:Molecular Chaperones; D020033:Protein Isoforms