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

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Neckers L, Schulte TW, Mimnaugh E

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

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

PubMed ID

10759403 [ View in PubMed

]

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.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Rifabutin	Heat shock protein HSP 90-alpha	Protein	Humans	No	Other/unknown	Details