Millipore Applications Bibliography |
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S-Nitrosylation of mitochondrial caspases. | ||
| Authors: | Mannick, J B, et al. | |
| Citation: | J. Cell Biol., 154: 1111-6 (2001) | |
| Pub Med ID: | 11551979 | |
| Year: | 2001 | |
| Abstract: | Caspase-3 is a cysteine protease located in both the cytoplasm and mitochondrial intermembrane space that is a central effector of many apoptotic pathways. In resting cells, a subset of caspase-3 zymogens is S-nitrosylated at the active site cysteine, inhibiting enzyme activity. During Fas-induced apoptosis, caspases are denitrosylated, allowing the catalytic site to function. In the current studies, we sought to identify the subpopulation of caspases that is regulated by S-nitrosylation. We report that the majority of mitochondrial, but not cytoplasmic, caspase-3 zymogens contain this inhibitory modification. In addition, the majority of mitochondrial caspase-9 is S-nitrosylated. These studies suggest that S-nitrosylation plays an important role in regulating mitochondrial caspase function and that the S-nitrosylation state of a given protein depends on its subcellular localization. | |
| Application: | Apoptosis | |
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