Journal
NATURE CELL BIOLOGY
Volume 2, Issue 3, Pages 156-162Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/35004029
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Funding
- NATIONAL CANCER INSTITUTE [T32CA009345, P01CA069381] Funding Source: NIH RePORTER
- NCI NIH HHS [CA69381, CA09345] Funding Source: Medline
- PHS HHS [A140646] Funding Source: Medline
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Release of cytochrome c from mitochondria triggers activation of caspase proteases and death of a cell by apoptosis, However, the mechanism and kinetics of cytochrome c release remain unknown. Here we study this event by using green fluorescent protein (GFP)-tagged cytochrome c, and find that the release of cytochrome-c-GFP always precedes exposure of phosphatidylserine and the loss of plasma-membrane integrity-characteristics of apoptotic cells. Once initiated, the release of cytochrome-c-GFP continues until all of the protein is released from all mitochondria in individual cells, within about 5 minutes, regardless of the type or strength of stimulus or the time elapsed since the stimulus was applied, Temperatures ranging from 24 degrees C to 37 degrees C do not change the duration of release, and nor does the addition of caspase inhibitors. Further, we find that the electron-transport chain can maintain the mitochondrial transmembrane potential even after cytochrome c has been released.
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