Myeloperoxidase and Horseradish Peroxidase Catalyze Tyrosine Nitration in Proteins from Nitrite and Hydrogen Peroxide
作者： Jacinda B. Sampson , YaoZu Ye , Henry Rosen , Joseph S. Beckman
关键词:
摘要: Abstract Nitration of tyrosine residues in proteins occurs a wide range inflammatory diseases involving neutrophil and macrophage activation. We report that both myeloperoxidase (MPO) horseradish peroxidase (HRP) utilize nitrite (NO 2 − ) hydrogen peroxide (H O as substrates to catalyze nitration proteins. MPO was approximately 10 times more effective than HRP catalyst bovine serum albumin (BSA). BSA by did not require chloride cofactor. Physiologic levels significantly inhibit MPO. Oxidation hypochlorous acid (HOCl) is catalyzed but HRP, yet also from plus nitrite. Therefore, HOCl formation obligatory for nitration. Although can nitrate the amino simple solutions, protein observed heart homogenates, probably due presence multiple alternative targets In contrast, many rat homogenates using NO H , suggesting peroxidase-catalyzed could occur competing vivo. substitute oxidizing substrate either or tissue peroxidase. Activated neutrophils may generate nitrotyrosine several mechanisms, including peroxynitrite, nitrite, chloride-independent mechanism MPO, peroxide.
elsevier.com
sci-hub.se 参考文章(54)
A Van der Vliet, D Smith, C A O'Neill, H Kaur, V Darley-Usmar, C E Cross, B Halliwell, Interactions of peroxynitrite with human plasma and its constituents: oxidative damage and antioxidant depletion. Biochemical Journal. ,vol. 303, pp. 295- 301 ,(1994) , 10.1042/BJ3030295
E N Standfield, L D Buttery, J M Polak, T J Evans, M H Yacoub, D V Parums, D R Springall, A H Chester, Inducible nitric oxide synthase is present within human atherosclerotic lesions and promotes the formation and activity of peroxynitrite Laboratory Investigation. ,vol. 75, pp. 77- 85 ,(1996)
Jacinda B. Sampson, Henry Rosen, Joseph S. Beckman, Peroxynitrite-dependent tyrosine nitration catalyzed by superoxide dismutase, myeloperoxidase, and horseradish peroxidase Methods in Enzymology. ,vol. 269, pp. 210- 218 ,(1996) , 10.1016/S0076-6879(96)69023-5
Johannes Everse, Kathleen E. Everse, Matthew B. Grisham, Peroxidases in chemistry and biology CRC Press. ,(1990)
Leland M. Shannon, Ernest Kay, Jow Y. Lew, Peroxidase Isozymes from Horseradish Roots I. ISOLATION AND PHYSICAL PROPERTIES Journal of Biological Chemistry. ,vol. 241, pp. 2166- 2172 ,(1966) , 10.1016/S0021-9258(18)96680-9
J.W. Heinecke, W. Li, H.L. Daehnke, J.A. Goldstein, Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages. Journal of Biological Chemistry. ,vol. 268, pp. 4069- 4077 ,(1993) , 10.1016/S0021-9258(18)53581-X
John I. Gallin, Ralph Snyderman, Ira M. Goldstein, Inflammation: Basic principles and clinical correlates ,(1988)
Rene FLORIS, Sander R. PIERSMA, Guang YANG, Peter JONES, Ron WEVER, Interaction of myeloperoxidase with peroxynitrite. A comparison with lactoperoxidase, horseradish peroxidase and catalase. FEBS Journal. ,vol. 215, pp. 767- 775 ,(1993) , 10.1111/J.1432-1033.1993.TB18091.X
Joseph S. Beckman, Jun Chen, Harry Ischiropoulos, John P. Crow, [23] Oxidative chemistry of peroxynitrite Methods in Enzymology. ,vol. 233, pp. 229- 240 ,(1994) , 10.1016/S0076-6879(94)33026-3
Stanley L. Hazen, Fong Fu Hsu, Jay W. Heinecke, p-Hydroxyphenylacetaldehyde Is the Major Product of L-Tyrosine Oxidation by Activated Human Phagocytes A CHLORIDE-DEPENDENT MECHANISM FOR THE CONVERSION OF FREE AMINO ACIDS INTO REACTIVE ALDEHYDES BY MYELOPEROXIDASE Journal of Biological Chemistry. ,vol. 271, pp. 1861- 1867 ,(1996) , 10.1074/JBC.271.4.1861