Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Apoptosis / physiology*
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Calcimycin / analogs & derivatives
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Calcimycin / pharmacology
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Cell Line
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Cerebral Cortex / cytology
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Cysteine Endopeptidases / metabolism*
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Humans
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Ionophores / pharmacology
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Kidney / cytology
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Lac Operon
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Neurons / cytology*
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Neurons / drug effects
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Neurons / enzymology*
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Nitric Oxide / metabolism*
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Nitric Oxide / pharmacology
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Nitric Oxide Synthase / metabolism
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Nitroso Compounds / metabolism
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Transfection
Substances
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Ionophores
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Nitroso Compounds
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Nitric Oxide
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Calcimycin
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4-bromo-A-23187
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Nitric Oxide Synthase
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Cysteine Endopeptidases