Cargando contenido…
Cargando contenido…
Último artículo añadido: 0 artículo/s
Cargando contenido…
» Cerrar

Millipore Applications Bibliography


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

Please note: This information is provided to you for technical reference. A reprint of the document cited is available from the publisher or from your local library and is not available from Millipore. For further assistance, please contact Millipore's Technical Services.