Cyclophilin A as negative regulator of apoptosis by sequestering cytochrome c.

Abstract : The release of cytochrome c from the mitochondrial intermembrane space is a decisive event in programmed 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.
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Biochemical and Biophysical Research Communications, Elsevier, 2010, 393 (2), pp.325-30. 〈10.1016/j.bbrc.2010.01.135〉
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Claude Bonfils, Nicole Bec, Christian Larroque, Maguy Del Rio, Céline Gongora, et al.. Cyclophilin A as negative regulator of apoptosis by sequestering cytochrome c.. Biochemical and Biophysical Research Communications, Elsevier, 2010, 393 (2), pp.325-30. 〈10.1016/j.bbrc.2010.01.135〉. 〈inserm-00457539〉

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