Impact of heat-shock protein 90 on cancer metastasis.
Cancer metastasis is the result of complex processes, including alteration of cell adhesion/motility in the microenvironment and neoangiogenesis, that are necessary to support cancer growth in tissues distant from the primary tumor. The molecular chaperone heat-shock protein 90 (Hsp90), also termed the 'cancer chaperone', plays a crucial role in maintaining the stability and activity of numerous signaling proteins involved in these processes. Small-molecule Hsp90 inhibitors display anticancer activity both in vitro and in vivo, and multiple Phase II and Phase III clinical trials of several structurally distinct Hsp90 inhibitors are currently underway. In this review, we will highlight the importance of Hsp90 in cancer metastasis and the therapeutic potential of Hsp90 inhibitors as antimetastasis drugs.
Tsutsumi
Shinji
S
Urologic Oncology Branch, National Cancer Institute, NIH, Bethesda, MD 20892-1107, USA.
Beebe
Kristin
K
Neckers
Len
L
D000970:Antineoplastic Agents / Q000494:pharmacology; D002986:Clinical Trials as Topic; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism* / Q000494:pharmacology; D006801:Humans; D009362:Neoplasm Metastasis / Q000473:pathology*; D009369:Neoplasms / Q000188:drug therapy / Q000378:metabolism* / Q000473:pathology*
D000970:Antineoplastic Agents; D018841:HSP90 Heat-Shock Proteins