Suppression of neuronal apoptosis by S-nitrosylation of caspases

• Published in: Neuroscience letters 1997-11, Vol.236 (3), p.139-142
• Main Authors: Tenneti, Lalitha, D'Emilia, Danielle M, Lipton, Stuart A
• Format: Article
• Language: English
• Subjects: Ageing, cell death; Apoptosis; Apoptosis - physiology; Biological and medical sciences; Calcimycin - analogs & derivatives; Calcimycin - pharmacology; Caspases; Cell Line; Cell physiology; Cerebral Cortex - cytology; Cysteine Endopeptidases - metabolism; Fundamental and applied biological sciences. Psychology; Humans; Ionophores - pharmacology; Kidney - cytology; Lac Operon; Molecular and cellular biology; Neurons - cytology; Neurons - drug effects; Neurons - enzymology; Nitric Oxide - metabolism; Nitric Oxide - pharmacology; Nitric Oxide Synthase - metabolism; Nitroso Compounds - metabolism; S-Nitrosylation; Transfection
• ISSN: 0304-3940; 1872-7972
• DOI: 10.1016/S0304-3940(97)00780-5

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-1 β-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.