Heat shock protein 90 (Hsp90) is a molecular chaperone whose association is required for the stability and function of multiple mutated, chimeric and over-expressed signaling proteins that promote the growth and/or survival of cancer cells.

Hsp90 is a key regulator of approximately 100 'client' proteins crucial for numerous cell signaling processes. Hsp90 client proteins include mutated p53, Bcr-Abl, Raf-1, Akt, ErbB2 and hypoxia-inducible factor 1 alpha (HIF-1 alpha).

Features

 hsp90 inhibitors

References

 Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer. 2005 Oct;5(10):761-72. PMID: #16175177#

 Aoyagi S, Archer TK. Modulating molecular chaperone Hsp90 functions through reversible acetylation. Trends Cell Biol. 2005 Nov;15(11):565-7. PMID: #16199163#

 Matthews RC, Burnie JP. Human recombinant antibody to HSP90: a natural partner in combination therapy. Curr Mol Med. 2005 Jun;5(4):403-11. PMID: #15977996#

 Ruden DM, Xiao L, Garfinkel MD, Lu X. Hsp90 and environmental impacts on epigenetic states: a model for the trans-generational effects of diethylstibesterol on uterine development and cancer. Hum Mol Genet. 2005 Apr 15;14 Spec No 1:R149-55. PMID: #15809267#

 Pearl LH. Hsp90 and Cdc37 -- a chaperone cancer conspiracy. Curr Opin Genet Dev. 2005 Feb;15(1):55-61. PMID: #15661534#

 Kamal A, Boehm MF, Burrows FJ. Therapeutic and diagnostic implications of Hsp90 activation. Trends Mol Med. 2004 Jun;10(6):283-90. PMID: #15177193#

 Workman P. Altered states: selectively drugging the Hsp90 cancer chaperone. Trends Mol Med. 2004 Feb;10(2):47-51. PMID: #15106614#

 Neckers L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med. 2002;8(4 Suppl):S55-61. PMID: #11927289#