Abstract
Nitric oxide and reactive nitrogen species such as nitrogen dioxide, dinitrogen trioxide and peroxynitrite react selectively with different proteins causing covalent structural modifications that alter protein function (1–3). The predominant post-translational modification mediated by nitric oxide is the S-nitrosylation of cysteine residues whereas reactive nitrogen intermediates primarily oxidize cysteine and nitrate tyrosine residues. Glyceraldehyde-3-phosphate dehydrogenase, ryanodine receptor, p21ras, hemoglobin and caspase 3 are modified by Snitrosylation of cysteine residues in vivo (4–10). The S-nitrosylation of the cysteine residues provides a selective and reversible covalent modification that regulates protein function and explains the ability of nitric oxide to regulate simultaneously different cellular pathways.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Stamler, J.S., Toone, E.J., Lip[ton, S.A. and Sucher, N.J. (1997)(S)NO signals: Translocation, regualtion and a consensus motif.Neuron 18,691–696
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
Ischiropoulos, H. (1998). Biological Tyrosine Nitration-A pathophysiological function of nitric oxide and reactive oxygen species. Arch. Biochem. Biophys. 356, 1–11.
Molina y Vedia, L., McDonald, B., Reep, B., Brune, B., Di Silvio, M., Billiar, T.R. and Lapetina, E.G. (1992) Nitric Oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation. J Biol. Chem. 267:24929–24932.
Lander, H.M., Milbank, A.J., Tauras, J.M., Hajjar, D.P., Hempstead, B.L., Schwartz, G.D., Kraemer, R.T., Mirza, U.A., Chalt, B.T., Burk, S.C., and Quilliam, L.A. (1996) Redox regulation of cell signalling. Nature 381, 380–381.
Xu, L., Eu, J.P., Msissner, G., and Stamler, J.S. (1998) Activation of the cardiac calcium Release Channel (Ryanodine Receptor) by Poly-S-Nitrosylation. Science 279, 234–237.
Lipton, S.A., Choi, Y.-B., Pan, Z.-H., Lei, S.Z., Chen, H-S.V., Sucher, N.J., Loscalzo, J., Singel, D.J. and Stamler, J.S. (1993) A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds. Nature 364:626–632.
Gow, A. and Stamler, J. (1998) Reactions between nitric oxide and haemoglobin under physiological conditions. Nature 391, 169–173.
Kim YM, Talanian RV, and Billiar TR (1997) Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms. J. Biol. Chem. 272, 31138–31148.
Mannick, J.B., Hausladen, A., Liu, L., Hess, D.T., Zeng, M., Miao, Q.X., Kane, L.S., Gow, A.J. and Stamler, J.S. (1999) Fas-induced caspase denitrosylation. Science 284, 651–654.
MacMillan-Crow, L.A., Crow, J.P., Kerby, J.D., Beckman, J.S. and Thompson, J.A. (1996) Nitration and inactivation of Mn superoxide dismutase in chronic rejection of human renal allografts. Proc. Natl. Acad. Sci. USA. 93, 11853–11858.
Zhou, M-H, Klein, T., Pasquet, J-P. and Ullrich, V. (1998) Interleukin-1β decreases prostacyclin synthase activity in rat mesanglial cells via endogenous peroxynitrite formation. Biochem. J. 336, 507–512.
Viner R1, Ferrington DA, Huhmer AFR, Bigelow DJ, and Schoneich C (1996) Accumulation of nitrotyrosine on the SERCA2a isoform of SR Ca-ATPase of rat skeletal muscle during aging: a peroxynitrite-mediated process? FEBS Lett. 379, 286–290.
Klebl, B.M., Ayoub, A.T. and Pette, D. (1998) Protein oxidation, tyrosine nitration, and inactivation of sarcoplasmic reticulum Ca2+-ATPase in low-frequency stimulated rabbit muscle. FEBS Lett. 422, 381–384.
Ara, J., Przedborski, S., Naini, A.B., Jackson-Lewis, V., Trifiletti, R.R., Horwitz, J. and Ischiropoulos, H. (1998) Inactivation of tyrosine hydroxylase following exposure to peroxynitrite and MPTP. Proc. Natl. Acad. Sci. USA. 95, 7659–7663.
Boota A, Zar H, Kim Y-M, Johnson B, Pitt B, Davies P (1996) IL-1P. stimulates superoxide and delayed peroxynitrite production by pulmonary vascular smooth muscle cells. Am. J. Physiol. 271, L932–L938.
Gole, M.D., Souza, J.M., Choi, I., Malcolm, S., Hertkom, C., Foust III, R.F., Finkel, B. Lanken, P.F. and Ischiropoulos, H. (2000) Plasma proteins modified by tyrosine nitration in acute respiratory distress syndrome. Am. J. Physiol., 278, L961–967.
Souza, J.M., Giasson, B.I., Chen, Q. Lee, V.M-Y. and Ischiropoulos, H. (2000) Dityrosine Cross-linking Promotes Formation of Stable a-synuclein Polymers: Implication of Nitrative and Oxidative Stress in the Pathogenesis of Neurodegenerative Synucleinopathies. J. Biol. Chem. 275, 18344–18349, 2000.
Furchgott. R.F. (1996) The discovery of EDRF and its importance in the identification of nitric oxide. JAMA 276, 1186–1188.
Moore, E.G. and Gibson, Q.H. (1976) Cooperativity in the dissociation of nitric oxide from hemoglobin. J Biol. Chem. 251, 2788–2794.
Craven, P.A. and DeRubertis, F.R. (1978) Restoration of the responsiveness of purified guanylate cyclase to nitrosoguanidine, nitric oxide, and related activators by heme and hemeproteins. J Biol. Chem. 253, 8433–8443.
Lancaster Jr., J.R., Langrehr, J.M., Bergonia, H.A., Murase, N., Simmons, R.L., and Hoffman, R.A. (1992) EPR detection of heme and nonheme iron-containing protein nitrosylation by nitric oxide during rejection of rat heart allograft. J. Biol. Chem. 267, 10994–10998.
Ribeiro, J.M.C., Hazzard, J.M.H., Nussenzveig, R.H., Champagne, D.E., and Walker, F.A. (1993) Reversible binding of nitric oxide by a salivary heme protein from a bloodsucking insect. Science 260, 539–541.
Gardner, P.R., Gardner, A.M., Martin, L.A., and Salzman, A.L. (1998) Nitric oxide dioxygenase: An enzymic function for flavohemoglobin. Proc. Natl. Acad. Sci. USA 95, 10378–10383.
Hausladen, A., Gow, A.J., and Stamler, J.S. (1998) Nitrosative stress: Metabolic pathway involving the flavohemoglobin. Proc. Natl. Acad. Sci. USA 95, 14100–14105.
Tsubaki, M., Hiwatashi, A., Ichikawa, Y. and Hori, H. (1987) EPR study of ferrous cytocrome P450scc-nitric oxide complexes: effects of cholesterol and its analogues. Biochemistry 26, 4527–4534.
Kennedy, M.C., Antholine, W.E., and Beinert, H. (1997) An EPR investigation of the products of the reaction of cytosolic and mitochondrial aconitase with nitric oxide. J. Biol. Chem. 272, 20340–20347.
Pearce, L.L., Gandley, R.E., Han, W., Wasserloos, K., Stitt, M., Kanai, A.J., McLaughlin, M.K., Pitt, B.R., and Levitan, E.S. (2000) Role of metallothionein in nitric oxide signaling as revealed by a green fluorescent fusion protein. Proc. Natl. Acad. Sci. 97, 477–482.
Cassina, A and Radi, R. (1996) Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport. Arch Biochem. Biophys. 328, 309–316.
Bouton, C., Raveau, M., and Drapier, J.C. (1996) Modulation of iron regulatory protein functions. J. Biol. Chem. 271, 2300–2306.
Gunthers, M.R., Hsi, L.C., Curtis, J.F., Giorse, J.K., Marnett. L.J., Eling, T.E., and Mason, R.P. (1997) Nitric oxide trapping of the tyrosyl radical of Prostaglandin H Synthase-2 leads to tyrosine iminoxyl radical and nitrotyrosine formation. J. Biol. Chem. 272, 17086–17090.
Goodwin, D.C., Gunthers, M.R., Hsi, L.C., Crews, B.C., Eling, T.E., Mason, R.P., and Marnett, L.J. (1998) Nitric oxide trapping of tyrosyl radicals generated during prostaglandin endoperoxide synthase turnover. J. Biol. Chem. 273, 8903–8909.
Guittet, O., Ducastel, B., Salem, J.S., Henry, Y., Rubin, H., Lemaire, G., and Lepoivre, M. (1998) Differential sensitivity of the tyrosyl radical of mouse ribonucleotide reductase to nitric oxide and peroxynitrite. J. Biol. Chem. 273, 22136–22144.
Gow, A., Buerk, D.G., and Ischiropoulos, H. (1997) A novel reaction mechanism for the formation of S-nitrosothiols in vivo. J. Biol. Chem. 272, 2841–2845.
Koppenol, W.H. (1998) The basic chemistry of nitrogen monoxide and peroxynitrite. Free Rad. Bio. Med. 25, 385–391.
Boese M, Mordvintcev PI, Vanin AF, Busse R, Mulsch (1995) S-Nitrosation of serum albumin by dinitrosyl-iron complex. J. Biol. Chem. 270, 29244–29249.
Inoue, K., Akaike, T., Miyamoto, Y., Okamoto, T., Sawa, T., Otagiri, M., Suzuki, S., Yoshimura, T., and Maeda, H. (1999) Nitrosothiol formation catalyzed by ceruloplasmin. J. Biol. Chem. 274, 27069–27075.
Liu, X., Miller, M.J., Johshi, M.S., Thomas, D.D. and Lancaster, Jr. J.R. (1998) Accelerated reaction of nitric oxide with oxygen within the hydrophobic interior of biological membranes. Proc. Natl. Acad. Sci. USA 95, 2175–2179.
O’Donnell VB, Eiserich, JP, Chumley, PH, Jablonsky, MJ, Krishna, NR, Kirk, M, Barnes, S, Darley-Usmar, VM, Freeman, BA (1998) Nitration of unsaturated fatty acids by nitric oxide-derived reactive nitrogen species peroxynitrite, nitric acid, nitrogen dioxide, and nitroniumion. Chem. Res. Toxicol. 12, 83–92
Wink, D.A., Cook, J.A., Kim, S.Y., Vodovotz, Y., Pacelli, R., Krishna, M.C., Russo, A., Mitchell, J.B., Jourd’heuil, D., Miles, A.M. and Grisham, M.B. (1997) Superoxide modulates the oxidation and nitrosation of thiols by nitric oxide-derived reactive intermediates. J. Biol. Chem. 272, 11147–11151.
Van der Vliet, A., Eiserich, J.P., Halliwell, B., and Cross, C.E. Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. J. Biol. Chem. 272:7617–7625, 1997.
Wu, W., Chen, Y. and Hazen, S.L. Eosinophil peroxidase nitrates protein tyrosyl residues. J. Biol. Chem. 274:25933–25944, 1999.
Van Dalen, C.J., Winterbourn, C.C., Senthilmohan, R. and Kettle, A.J. (2000) Nitrite as a substrate and inhibitor of myeloperoxidase. J. Biol. Chem. 275, 11638–11644.
Ischiropoulos, H., D. Duran, J. Nelson, A.B. Al-Mehdi. (1996) Reactions of nitric oxide and peroxynitrite with organic molecules and ferrihorseradish peroxidase: interference with the determination of hydrogen peroxide. Free Rad. Biol. Med. 20, 373–381.
Sampson, J.B., Ye, Y., Rosen, H. and Beckman, J.S. Myeloperoxidase and horseradish peroxidase catalyze tyrosine nitration in proteins from nitrite and hydrogen peroxide. Arch. Biochem. Biophys. 356, 207–213, 1998.
Schopfer F, Riobo N, Carreras MC, Alvarez B, Radi R, Boveris A, Cadenas E, Poderoso JJ. (2000) Oxidation of ubiquinol by peroxynitrite: implications for protection of mitochondria against nitrosative damage.Biochem J. 349, 35–42.
Souza, J.M., Daikhin, E., Yudkoff, M., Raman’ C.S. and Ischiropoulos, H. Factors determining the selectivity of protein tyrosine nitration. Arch. Biochem. Biophys. 371, 169–178, 1999.
Alvarez, B., Ferrer-Sueta, G., Freeman, B.A., and Radi, R. (1998) Kinetics of peroxynitrite reaction with amino acids and human serum albumin. J. Biol. Chem. 274, 842–848.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2001 Springer Science+Business Media New York
About this chapter
Cite this chapter
Souza, J.M. et al. (2001). Reactive Nitrogen Species and Proteins: Biological Significance and Clinical Relevance. In: Dansette, P.M., et al. Biological Reactive Intermediates VI. Advances in Experimental Medicine and Biology, vol 500. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0667-6_22
Download citation
DOI: https://doi.org/10.1007/978-1-4615-0667-6_22
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-5185-6
Online ISBN: 978-1-4615-0667-6
eBook Packages: Springer Book Archive