Suppression of neuronal apoptosis by S-nitrosylation of caspases.
S-Nitrosylation (reaction of nitric oxide (NO) species with a critical cysteine sulfhydryl) can regulate the physiological activity of proteins, including enzymes, ion channels, G-proteins, and transcription factors. Caspases are a family of interleukin-1beta-converting enzyme-like proteases involved in the signaling pathway to apoptotic cell death, and each member of this enzyme family contains a critical cysteine residue in its active site. Here we show that S-nitrosylation of caspases in human embryonic kidney (HEK)-293 cells and primary cerebrocortical neurons decreases enzyme activity and is associated with protection from apoptosis.
Tenneti
L
L
Cerebrovascular and NeuroScience Research Institute, Brigham and Women's Hospital, Boston, MA 02115, USA.
D'Emilia
D M
DM
Lipton
S A
SA
D017209:Apoptosis / Q000502:physiology*; D000001:Calcimycin / Q000031:analogs & derivatives / Q000494:pharmacology; D002460:Cell Line; D002540:Cerebral Cortex / Q000166:cytology; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D006801:Humans; D007476:Ionophores / Q000494:pharmacology; D007668:Kidney / Q000166:cytology; D007763:Lac Operon; D009474:Neurons / Q000166:cytology* / Q000187:drug effects / Q000201:enzymology*; D009569:Nitric Oxide / Q000378:metabolism* / Q000494:pharmacology; D019001:Nitric Oxide Synthase / Q000378:metabolism; D009603:Nitroso Compounds / Q000378:metabolism; D014162:Transfection
D007476:Ionophores; D009603:Nitroso Compounds; D009569:Nitric Oxide; D000001:Calcimycin; C033170:4-bromo-A-23187; D019001:Nitric Oxide Synthase; D003546:Cysteine Endopeptidases