期刊
CELL
卷 131, 期 2, 页码 257-270出版社
CELL PRESS
DOI: 10.1016/j.cell.2007.08.028
关键词
-
资金
- NCI NIH HHS [CA90917, CA78810] Funding Source: Medline
- NHLBI NIH HHS [HL54131] Funding Source: Medline
Molecular chaperones, especially members of the heat shock protein 90 ( Hsp90) family, are thought to promote tumor cell survival, but this function is not well understood. Here, we show that mitochondria of tumor cells, but not most normal tissues, contain Hsp90 and its related molecule, TRAP-1. These chaperones interact with Cyclophilin D, an immunophilin that induces mitochondrial cell death, and antagonize its function via protein folding/refolding mechanisms. Disabling this pathway using novel Hsp90 ATPase antagonists directed to mitochondria causes sudden collapse of mitochondrial function and selective tumor cell death. Therefore, Hsp90 directed chaperones are regulators of mitochondrial integrity, and their organelle-specific antagonists may provide a previously undescribed class of potent anticancer agents.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据