Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Nitration and inactivation of tyrosine hydroxylase by peroxynitrite
Autore:
Blanchard-Fillion, B; Souza, JM; Friel, T; Jiang, GCT; Vrana, K; Sharov, V; Barron, L; Schoneich, C; Quijano, C; Alvarez, B; Radi, R; Przedborski, S; Fernando, GS; Horwitz, J; Ischiropoulos, H;
Indirizzi:
Childrens Hosp Philadelphia, Stokes Res Inst, Abramson Res Ctr, 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 Wake Forest Univ, Sch Med, Dept Physiol & Pharmacol, Winston Salem, NC 27106 USA Wake Forest Univ Winston Salem NC USA 27106 , Winston Salem, NC 27106 USA Univ Kansas, Dept Pharmaceut Chem, Lawrence, KS 66047 USA Univ Kansas Lawrence KS USA 66047 Pharmaceut Chem, Lawrence, KS 66047 USA Univ Republica, Fac Ciencas, Lab Enzimol, Montevideo 11800, Uruguay Univ Republica Montevideo Uruguay 11800 zimol, Montevideo 11800, Uruguay Univ Republica, Fac Med, Dept Bioquim, Montevideo 11800, Uruguay Univ Republica Montevideo Uruguay 11800 oquim, Montevideo 11800, Uruguay Columbia Univ, Dept Neurol, Movement Disorder Div, New York, NY 10032 USA Columbia Univ New York NY USA 10032 Disorder Div, New York, NY 10032 USA Columbia Univ, Dept Pathol, Movement Disorder Div, New York, NY 10032 USA Columbia Univ New York NY USA 10032 Disorder Div, New York, NY 10032 USA MCP Hahnemann Sch Med, Dept Physiol & Pharmacol, Philadelphia, PA USA MCP Hahnemann Sch Med Philadelphia PA USA harmacol, Philadelphia, PA USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 49, volume: 276, anno: 2001,
pagine: 46017 - 46023
SICI:
0021-9258(200112)276:49<46017:NAIOTH>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
NEURONAL NITRIC-OXIDE; SUPEROXIDE-DISMUTASE; NEURODEGENERATIVE SYNUCLEINOPATHIES; TRYPTOPHAN-HYDROXYLASE; PARKINSONS-DISEASE; OXIDATIVE STRESS; IDENTIFICATION; NEUROTOXICITY; MPTP; MICE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Ischiropoulos, H Childrens Hosp Philadelphia, Stokes Res Inst, Abramson Res Ctr, 34th St & Civ Ctr Blvd, Philadelphia, PA 19104 USA Childrens Hosp Philadelphia 34th St & Civ Ctr Blvd Philadelphia PA USA 19104
Citazione:
B. Blanchard-Fillion et al., "Nitration and inactivation of tyrosine hydroxylase by peroxynitrite", J BIOL CHEM, 276(49), 2001, pp. 46017-46023

Abstract

Tyrosine hydroxylase (TH) is modified by nitration after exposure of mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydrophenylpyridine. The temporal association of tyrosine nitration with inactivation of TH activity in vitro suggests that this covalent post-translational modification is responsible for the in vivo loss of TH function (Ara, J., Przedborski, S., Naini, A. B., Jackson-Lewis, V., Trifiletti, R. R., Horwitz, J., and Ischiropoulos, H. (1998)Proc. Natl. Acad Sci. U. S. A. 95, 7659 -7663). Recent data showed that cysteine oxidation rather than tyrosine nitration is responsible for TH inactivation after peroxynitrite exposure in vitro (Kuhn, D. M., Aretha, C. W., and Geddes, T. J. (1999) J. Neurosci. 19, 10289-10294). However, re-examination of the reaction of peroxynitrite with purified TH failed to produce cysteine oxidation but resulted in a concentration-dependent increase in tyrosine nitration and inactivation. Cysteine oxidation is only observed after partial unfolding of the protein. Tyrosine residue 423 and to lesser extenttyrosine residues 428 and 432 are modified by nitration. Mutation of Tyr(423) to Phe resulted in decreased nitration as compared with wild type protein without loss of activity. Stopped-flow experiments reveal a second orderrate constant of (3.8 +/- 0.9) X 10(3) M-1 s(-1) at pH 7.4 and 25 degreesCfor the reaction of peroxynitrite with TH. Collectively, the data indicatethat peroxynitrite reacts with the metal center of the protein and resultsprimarily in the nitration of tyrosine residue 423, which is responsible for the inactivation of TH.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/09/20 alle ore 13:42:38