Format

Send to

Choose Destination
Invest New Drugs. 1999;17(4):361-73.

Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity.

Author information

1
Department of Cell and Cancer Biology, Medicine Branch, National Cancer Institute, Rockville, MD, USA.

Abstract

Heat shock protein 90 is one of the most abundant cellular proteins. Although its functions are still being characterized, it appears to serve as a chaperone for a growing list of cell signaling proteins, including many tyrosine and serine/threonine kinases, involved in proliferation and/or survival. The benzoquinone ansamycin geldanamycin has been shown to bind to Hsp90 and to specifically inhibit this chaperone's function, resulting in client protein destabilization. Its ability to simultaneously stimulate depletion of multiple oncogenic proteins suggests that geldanamycin, or other molecules capable of targeting Hsp90 in cancer cells, may be of clinical benefit.

PMID:
10759403
DOI:
10.1023/a:1006382320697
[Indexed for MEDLINE]

Supplemental Content

Loading ...
Support Center