The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Nitric Oxide-induced S-Glutathionylation and Inactivation of Glyceraldehyde-3-phosphate Dehydrogenase
Open accessAbstract
S-Nitrosylation of protein thiol groups by nitric oxide (NO) is a widely recognized protein modification. In this study we show that nitrosonium tetrafluoroborate (BF4NO), a NO+ donor, modified the thiol groups of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by S-nitrosylation and caused enzyme inhibition. The resultant protein-S-nitrosothiol was found to be unstable and to decompose spontaneously, thereby restoring enzyme activity. In contrast, the NO-releasing compound S-nitrosoglutathione (GSNO) promoted S-glutathionylation of a thiol group of GAPDH both in vitro and under cellular conditions. The GSH-mixed protein disulfide formed led to a permanent enzyme inhibition, but upon dithiothreitol addition a functional active GAPDH was recovered. This S-glutathionylation is specific for GSNO because GSH itself was unable to produce protein-mixed disulfides. During cellular nitrosative stress, the production of intracellular GSNO might channel signaling responses to form protein-mixed disulfide that can regulate intracellular function.
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Cites
Nitric oxide: physiology, pathophysiology, and pharmacology.
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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
Arnelle, D. R., & Stamler, J. S. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1231 · Cited by 604
Cited by
Glutathione and its role in cellular functions
Sies, H. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00177-x · Cited by 1,735
Radical-free biology of oxidative stress
Jones, D. P. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00283.2008 · Cited by 1,213
Nitric oxide in immunity and inflammation
Coleman, J. W. (2001) · International Immunopharmacology · doi:10.1016/s1567-5769(01)00086-8 · Cited by 945
Proteomic Identification of S -Nitrosylated Proteins in Arabidopsis
Lindermayr, C., Saalbach, G., & Durner, J. (2005) · Plant Physiology · doi:10.1104/pp.104.058719 · Cited by 734
Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species
Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00014.2008 · Cited by 542
Metadata
- Authors
- Mohr, S., Hallak, H., de Boitte, A., Lapetina, E. G., & Brüne, B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-04
- Volume
- 274
- Issue
- 14
- Pages
- 9427-9430
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2007419421
- Cited by
- 309
- References
- 3
- FWCI
- 5.00
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Mohr, S., Hallak, H., de Boitte, A., Lapetina, E. G., & Brüne, B. (1999). Nitric Oxide-induced S-Glutathionylation and Inactivation of Glyceraldehyde-3-phosphate Dehydrogenase. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.274.14.9427
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