Impact of heat-shock protein 90 on cancer metastasis.
Impact of heat-shock protein 90 on cancer metastasis.
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DOI：
10.2217/fon.09.30
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发表时间：
2009-06
期刊：
影响因子：
--
通讯作者：
Neckers L
中科院分区：
文献类型：
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作者：
Tsutsumi S;Beebe K;Neckers L
癌症转移是复杂过程的结果，包括微环境中细胞粘附/运动的改变和新血管生成，这是支持远离原发肿瘤的组织中癌症生长所必需的。分子伴侣热休克蛋白 90 (Hsp90)，也称为“癌症伴侣”，在维持这些过程中涉及的众多信号蛋白的稳定性和活性方面发挥着至关重要的作用。小分子 Hsp90 抑制剂在体外和体内均表现出抗癌活性，目前正在进行针对几种结构不同的 Hsp90 抑制剂的多项 II 期和 III 期临床试验。在这篇综述中，我们将强调 Hsp90 在癌症转移中的重要性以及 Hsp90 抑制剂作为抗转移药物的治疗潜力。
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.