The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation.
Open accessAbstract
Using conditions that produced chronic inflammation in rat liver, we were able to find a correlation between induction of nitric oxide production and inhibition of glyceraldehyde-3-phosphate dehydrogenase (GAPDH; EC 1.2.1.12). This enzyme is a tetramer composed of identical M(r) 37,000 subunits. The tetramer contains 16 thiol groups, four of which are essential for enzymatic activity. Our information indicates that four thiol groups are S-nitrosylated by exposure to authentic nitric oxide (NO) gas. Furthermore, NO decreased GAPDH activity while increasing its auto-ADP-ribosylation. Reduced nicotinamide adenine dinucleotide and dithiothreitol are required for the S-nitrosylation of GAPDH caused by the NO-generating compound sodium nitroprusside. Our results suggests that a new and important action of nitric oxide on cells is the S-nitrosylation and inactivation of GAPDH. S-Nitrosylation of GAPDH may be a key covalent modification of multiple regulatory consequences in chronic liver inflammation.
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Cites
Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
Palmer, R. M. J., Ferrige, A. G., & Moncada, S. (1987) · Nature · doi:10.1038/327524a0 · Cited by 10,704
Billiar, T. R., Curran, R. D., Harbrecht, B. G., Stuehr, D. J., Demetris, A. J., & Simmons, R. L. (1990) · Journal of Leukocyte Biology · doi:10.1002/jlb.48.6.565 · Cited by 335
Cited by
Biochemistry of nitric oxide and its redox-activated forms
Stamler, J. S., Singel, D. J., & Loscalzo, J. (1992) · Science · doi:10.1126/science.1281928 · Cited by 2,744
Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production
Powers, S. K., & Jackson, M. J. (2008) · Physiological Reviews · doi:10.1152/physrev.00031.2007 · Cited by 2,459
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Veal, E. A., Day, A. M., & Morgan, B. A. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.016 · Cited by 1,604
Nitric Oxide Activation of Poly(ADP-Ribose) Synthetase in Neurotoxicity
Zhang, J., Dawson, V. L., Dawson, T. M., & Snyder, S. H. (1994) · Science · doi:10.1126/science.8080500 · Cited by 1,118
The diverse functions of GAPDH: Views from different subcellular compartments
Tristan, C., Shahani, N., Sedlak, T. W., & Sawa, A. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2010.08.003 · Cited by 663
Metadata
- Authors
- Molina y Vedia, L., McDonald, B., Reep, B., Brüne, B., Di Silvio, M., Billiar, T. R., & Lapetina, E. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-12
- Volume
- 267
- Issue
- 35
- Pages
- 24929-24932
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1523151859
- Cited by
- 389
- References
- 2
- FWCI
- 9.67
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Molina y Vedia, L., McDonald, B., Reep, B., Brüne, B., Di Silvio, M., Billiar, T. R., & Lapetina, E. G. (1992). Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)73985-4
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