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- W2000884109 abstract "The release of cytochrome c from the mitochondrial intermembrane space is a decisive event in programed cell death. Once in the cytoplasm, cytochrome c is involved in the formation of the macromolecular complex termed apoptosome, which activates procaspase-9 which in turn activates downstream procaspase-3. There are increasing evidence indicating that cyclophilin A is highly expressed in many tumors and cell lines where it exerts an anti-apoptotic function. In brain tissue, which over-expresses constitutively cyclophilin A, we found mixed dimers composed of cyclophilin A and cytochrome c. In a cell-free system we observed that pure cyclophilin A inhibited cytochrome c-dependent procaspase-3 activation. Moreover, we detected cyclophilin A–cytochrome c complexes within the cytoplasm of HCT116 cells following staurosporine-induced apoptosis. Our results strongly support that, in tumor cells, cyclophilin A is able to inhibit procaspase-3 activation by sequestering cytochrome c." @default.
- W2000884109 created "2016-06-24" @default.
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- W2000884109 date "2010-03-01" @default.
- W2000884109 modified "2023-09-27" @default.
- W2000884109 title "Cyclophilin A as negative regulator of apoptosis by sequestering cytochrome c" @default.
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- W2000884109 doi "https://doi.org/10.1016/j.bbrc.2010.01.135" @default.
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