ArticleProceedings of the National Academy of Sciences of the United States of America1993
Stimulation by nitric oxide of an NAD linkage to glyceraldehyde-3-phosphate dehydrogenase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 237 citations in OpenAlex.
- Modification of Glyceraldehyde-3-Phosphate Dehydrogenase with Nitric Oxide: Role in Signal Transduction and Development of Apoptosis.Biomolecules · 2021Review
- Starving honey bee (Apis mellifera) larvae signal pheromonally to worker bees.Scientific reports · 2016Article
- Effective elimination of cancer stem cells by a novel drug combination strategy.Stem cells (Dayton, Ohio) · 2013Article
- Selective vulnerability of synaptic signaling and metabolism to nitrosative stress.Antioxidants & redox signaling · 2012Review
- Differential mechanisms of inhibition of glyceraldehyde-3-phosphate dehydrogenase by S-nitrosothiols and NO in cellular and cell-free conditions.American journal of physiology. Heart and circulatory physiology · 2010Article
- Long-lasting inhibition of presynaptic metabolism and neurotransmitter release by protein S-nitrosylation.Free radical biology & medicine · 2010Article
- Neuroprotective effects of pyruvate following NMDA-mediated excitotoxic insults in hippocampal slices.Neuroscience letters · 2010Article
- Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegeneration.Journal of Alzheimer's disease : JAD · 2010Review
- Cardioprotection by metabolic shut-down and gradual wake-up.Journal of molecular and cellular cardiology · 2009Review
- Ethanol metabolism and effects: nitric oxide and its interaction.Current clinical pharmacology · 2007Review
- Reversible post-translational modification of proteins by nitrated fatty acids in vivo.The Journal of biological chemistry · 2006Article
- Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells.The Journal of clinical investigation · 2003Article
- Inactivation of platelet-derived growth factor-BB following modification by ADP-ribosyltransferase.British journal of pharmacology · 2001Article
- Regulation of glutamate dehydrogenase by reversible ADP-ribosylation in mitochondria.The EMBO journal · 2001Article
- Specific phosphorylated forms of glyceraldehyde 3-phosphate dehydrogenase associate with human parainfluenza virus type 3 and inhibit viral transcription in vitro.Journal of virology · 2000Article
- Effects of site-directed mutagenesis of Escherichia coli heat-labile enterotoxin on ADP-ribosyltransferase activity and interaction with ADP-ribosylation factors.Infection and immunity · 1999Article
- Nitric oxide and its congeners in mitochondria: implications for apoptosis.Environmental health perspectives · 1998Review
- The synthesis of ATP by glycolytic enzymes in the postsynaptic density and the effect of endogenously generated nitric oxide.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Glyceraldehyde-3-phosphate dehydrogenase: nuclear translocation participates in neuronal and nonneuronal cell death.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Purification of a dichlorophenol-indophenol oxidoreductase from rat and bovine synaptic membranes: tight complex association of a glyceraldehyde-3-phosphate dehydrogenase isoform, TOAD64, enolase-gamma and aldolase C.The Biochemical journal · 1997Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nitric oxide-stimulated modification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by [adenylate-32P]NAD has been interpreted in recent reports as ADP-ribosylation. Incubations of GAPDH with the NO-releasing agent sodium nitroprusside (SNP) and NAD resulted, however, in essentially equal incorporation of radiolabel from the adenine, phosphate, and nicotinamide moieties to the extent of approximately 0.02 mol of NAD.mol of GAPDH-1. Modification of GAPDH by free adenosine 5'-diphosphoribose (ADP-ribose) was only 10% of that by NAD. Exposure of GAPDH modified by NAD in the presence of SNP to HgCl2, which acts at thiol linkages, released two products. Both contained nicotinamide and adenylate but did not cochromatograph with NAD. GAPDH activity was inhibited by SNP in a dose-dependent manner in the presence of NAD. When inhibition was 80%, with 1 mM SNP and 1 mM dithiothreitol, covalent modification with NAD was < 2%. This result is consistent with the conclusion that inhibition of GAPDH activity by SNP in the presence of NAD is due primarily to active-site nitrosylation, as reported by other workers, and is not due to the minor modification with NAD. These results demonstrate that NO-stimulated modification of GAPDH with NAD is not ADP-ribosylation as previously reported but rather is covalent binding of NAD through a NO-dependent thiol intermediate, possibly providing an example of an unexpected, altered reactivity of a nitrosylated protein.
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