Impact of heat-shock protein 90 on cancer metastasis

被引：24

作者：

Tsutsumi, Shinji ^{[1
]}

Beebe, Kristin ^{[1
]}

Neckers, Len ^{[1
]}

机构：

[1] NCI, Urol Oncol Branch, Bethesda, MD 20892 USA

来源：

FUTURE ONCOLOGY | 2009年 / 5卷 / 05期

关键词：

17AAG; 17DMAG; cell adhesion; cell motility; geldanamycin; Hsp90; metastasis; molecular chaperone; neoangiogenesis; FOCAL-ADHESION KINASE; GROWTH-FACTOR RECEPTOR; HYPOXIA-INDUCIBLE FACTOR-1-ALPHA; UROKINASE PLASMINOGEN-ACTIVATOR; HSP90 MOLECULAR CHAPERONE; INTEGRIN-LINKED KINASE; HUMAN-BREAST-CANCER; FACTOR-I RECEPTOR; CELL MOTILITY; TYROSINE KINASE;

D O I：

10.2217/FON.09.30

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

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 11 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.

引用

收藏

页码：679 / 688

页数：10

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