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Titolo:
Factors determining the selectivity of protein tyrosine nitration
Autore:
Souza, JM; Daikhin, E; Yudkoff, M; Raman, CS; Ischiropoulos, H;
Indirizzi:
Childrens Hosp Philadelphia, Stokes Res Inst, Abramson Res Ctr 416D, Philadelphia, PA 19104 USA Childrens Hosp Philadelphia Philadelphia PA USA 19104 lphia, PA 19104 USA Childrens Hosp Philadelphia, Dept Pediat, Div Neonatol, Philadelphia, PA 19104 USA Childrens Hosp Philadelphia Philadelphia PA USA 19104 lphia, PA 19104 USA Childrens Hosp Philadelphia, Dept Child Dev & Rehabil Med, Philadelphia, PA 19104 USA Childrens Hosp Philadelphia Philadelphia PA USA 19104 lphia, PA 19104 USA Childrens Hosp Philadelphia, Dept Biochem & Biophys, Philadelphia, PA 19104 USA Childrens Hosp Philadelphia Philadelphia PA USA 19104 lphia, PA 19104 USA Univ Penn, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104Univ Penn, Philadelphia, PA 19104 USA Univ Calif Irvine, Dept Mol Biol, Irvine, CA 92717 USA Univ Calif Irvine Irvine CA USA 92717 Dept Mol Biol, Irvine, CA 92717 USA Univ Republ, Fac Med, Dept Bioquim, Montevideo 11800, Uruguay Univ RepublMontevideo Uruguay 11800 Bioquim, Montevideo 11800, Uruguay
Titolo Testata:
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
fascicolo: 2, volume: 371, anno: 1999,
pagine: 169 - 178
SICI:
0003-9861(19991115)371:2<169:FDTSOP>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
MANGANESE-SUPEROXIDE-DISMUTASE; NITRIC-OXIDE; HORSERADISH-PEROXIDASE; PEROXYNITRITE; INACTIVATION; MYELOPEROXIDASE; OXIDATION; NITROTYROSINE; MECHANISM; ACID;
Keywords:
3-nitrotyrosine; nitric oxide; superoxide; peroxynitrite;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Ischiropoulos, H Childrens Hosp Philadelphia, Stokes Res Inst, Abramson Res Ctr 416D, 34th St & Civ Ctr Blvd, Philadelphia, PA 19104 USA Childrens Hosp Philadelphia 34th St & Civ Ctr Blvd Philadelphia PA USA 19104
Citazione:
J.M. Souza et al., "Factors determining the selectivity of protein tyrosine nitration", ARCH BIOCH, 371(2), 1999, pp. 169-178

Abstract

Tyrosine nitration is a covalent posttranslational protein modification derived from the reaction of proteins with nitrating agents. Protein nitration appears to be a selective process since not all tyrosine residues in proteins or all proteins are nitrated in vivo. To investigate factors that may determine the biological selectivity of protein tyrosine nitration, we developed an in vitro model consisting of three proteins with similar size but different three-dimensional structure and tyrosine content. Exposure of ribonuclease A to putative in vivo nitrating agents revealed preferential nitration of tyrosine residue Y-115. Tyrosine residue Y-23 and to a lesser extent residue Y-20 were preferentially ;nitrated in lysozyme, whereas tyrosineY-102 was the only residue modified by nitration in phospholipase A(2). Tyrosine Y-115 was the residue modified by nitration after exposure of ribonuclease A to different nitrating agents: chemically synthesized peroxynitrite, nitric oxide, and superoxide generated by SIN-1 or myeloperoxidase (MPO)/H2O2 plus nitrite (NO2-) in the presence of bicarbonate/CO2. The nature ofthe nitrating agent determined in part the protein that would be predominantly modified by nitration in a mixture of all three proteins. RibonucleaseA was preferentially nitrated upon exposure to MPO/H2O2/NO2-, whereas phospholipase A(2) was the primary target for nitration upon exposure to peroxynitrite. The data also suggest that the exposure of the aromatic ring to the surface of the protein, the location of the tyrosine on a loop structure,and its association with a neighboring negative charge are some of the factors determining the selectivity of tyrosine nitration In proteins. (C) 1999 Academic Press.

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Documento generato il 22/09/20 alle ore 13:59:21