Abstract
Nitric oxide (NO) is a diatomic free-radical product of mammalian cells that has diverse and important physiological functions, including the regulation of renal, cardiovascular, pulmonary, gastrointestinal, neuronal, inflammatory, and immune systems. At the cellular level, NO is a pivotal modulator of proliferation, differentiation, migration, and programmed cell death. These actions of NO are engendered by covalent chemical addition of NO (or NO-derived species) to protein targets.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Stamler, J. S., Lamas, S., and Fang, F. C. (2001) Nitrosylation: the prototypic redox-based signaling mechanism. Cell 106, 675–683.
Greenacre, S. A. and Ischiropoulos, H. (2001) Tyrosine nitration: localisation, quantification, consequences for protein function and signal transduction. Free Radic. Res. 34, 541–581.
Denninger, J. W. and Marletta, M. A. (1999) Guanylate cyclase and the NO/cGMP signaling pathway. Biochem. Biophys. Acta 1411, 334–350.
Hess, D. T., Matsumoto, A., Nudelman, R., and Stamler, J. S. (2001) S-nitrosylation: spectrum and specificity. Nat. Cell Biol. 3, E46–E49.
Lane, P., Hao, G., and Gross, S. S. (2001) S-Nitrosylation is emerging as a specific and fundamental posttranslational protein modification: head-to-head comparison with O-phosphorylation. Science’s STKE http://www.stke.org/cgi/content/full/OCsigtrans;2001/86/re1.
Kashiba-Iwatsuki, M., Kitoh, K., Kasahara, E., Yu, H., Nisikawa, M., Matsuo, M., and Inoue, M. (1997) Ascorbic acid and reducing agents regulate the fates and functions of S-nitrosothiols. J. Biochem. Tokyo 122, 1208–1214.
Dicks, A. P. and Williams, D. L. (1996) Generation of nitric oxide from S-nitrosothiols using protein-bound Cu2+ sources. Chem. Biol. 3, 655–659.
Stubauer, G., Giuffre, A., and Sarti, P. (1999) Mechanism of S-nitrosothiol formation and degradation mediated by copper ions. J. Biol. Chem. 274, 28,128–28,133.
Simon, D. I., Mullins, M. E., Jia, L., Gaston, B., Singel, D. J., and Stamler, J. S. (1996) Polynitrosylated proteins: characterization, bioactivity, and functional consequences. Proc. Natl. Acad. Sci. USA 93, 4736–4741.
Jaffrey, S. R., Erdjument-Bromage, H., Ferris, C. D., Tempst, P., and Snyder, S. H. (2001) Protein S-nitrosylation: a physiological signal for neuronal nitric oxide. Nat. Cell Biol. 3, 193–197.
Radi, R., Peluffo, G., Alvarez, M. N., Naviliat, M., and Cayota, A. (2001) Unraveling peroxynitrite formation in biological systems. Free Radic. Biol. Med. 30, 463–488.
Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., and Freeman, B. A. (1990) Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc. Natl. Acad. Sci. USA 87, 1620–1624.
Berlett, B. S., Levine, R. L., and Stadtman, E. R. (1998) Carbon dioxide stimulates peroxynitrite-mediated nitration of tyrosine residues and inhibits oxidation of methionine residues of glutamine synthetase: both modifications mimic effects of adenylylation. Proc. Natl. Acad. Sci. USA 95, 2784–2789.
Eiserich, J. P., Cross, C. E., Jones, A. D., Halliwell, B., and van der Vliet, A. (1996) Formation of nitrating and chlorinating species by reaction of nitrite with hypochlorous acid. A novel mechanism for nitric oxide-mediated protein modification. J. Biol. Chem. 271, 19,199–19,208.
Aulak, K. S., Miyagi, M., Yan, L., West, K. A., Massillon, D., Crabb, J. W., and Stuehr, D. J. (2001) Proteomic method identifies proteins nitrated in vivo during inflammatory challenge. Proc. Natl. Acad. Sci. USA 98, 12,056–12,061.
Maruyama, W., Hashizume, Y., Matsubara, K., and Naoi, M. (1996) Identification of 3-nitro-L-tyrosine, a product of nitric oxide and superoxide, as an indicator of oxidative stress in the human brain. J. Chromatogr. B Biomed. Appl. 676, 153–158.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2003 Humana Press Inc., Totowa, NJ
About this protocol
Cite this protocol
Crabtree, M., Hao, G., Gross, S.S. (2003). Detection of Cysteine S-Nitrosylation and Tyrosine 3-Nitration in Kidney Proteins. In: Goligorsky, M.S. (eds) Renal Disease. Methods in Molecular Medicine™, vol 86. Humana Press. https://doi.org/10.1385/1-59259-392-5:373
Download citation
DOI: https://doi.org/10.1385/1-59259-392-5:373
Publisher Name: Humana Press
Print ISBN: 978-1-58829-134-9
Online ISBN: 978-1-59259-392-7
eBook Packages: Springer Protocols