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Titolo:
Glyoxalase I is a novel nitric-oxide-responsive protein
Autore:
Mitsumoto, A; Kim, KR; Oshima, G; Kunimoto, M; Okawa, K; Iwamatsu, A; Nakagawa, Y;
Indirizzi:
Kitasato Univ, Sch Pharmaceut Sci, Minato Ku, Tokyo 1088641, Japan Kitasato Univ Tokyo Japan 1088641 t Sci, Minato Ku, Tokyo 1088641, Japan Natl Inst Environm Studies, Tsukuba, Ibaraki 3050053, Japan Natl Inst Environm Studies Tsukuba Ibaraki Japan 3050053 i 3050053, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Kanazawa Ku, Yokohama, Kanagawa 2360004, Japan Kirin Brewery Co Ltd Yokohama Kanagawa Japan 2360004 agawa 2360004, Japan
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 344, anno: 1999,
parte:, 3
pagine: 837 - 844
SICI:
0264-6021(199912)344:<837:GIIANN>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLYACRYLAMIDE-GEL ELECTROPHORESIS; S-NITROSYLATION; DERIVATIVES; SYNTHASE; CELLS; INACTIVATION; INHIBITION; BINDING; INVITRO; DIESTER;
Keywords:
endothelial cell; nitrosative stress; oxidation; posttranslational modification; two-dimensional PAGE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Nakagawa, Y Kitasato Univ, Sch Pharmaceut Sci, Minato Ku, 5-9-1 Shirokane,Tokyo 1088641, Japan Kitasato Univ 5-9-1 Shirokane Tokyo Japan 1088641 8641, Japan
Citazione:
A. Mitsumoto et al., "Glyoxalase I is a novel nitric-oxide-responsive protein", BIOCHEM J, 344, 1999, pp. 837-844

Abstract

To clarify the molecular mechanisms of nitric oxide (NO) signalling, we examined the NO-responsive proteins in cultured human endothelial cells by two-dimensional (2D) PAGE. Levels of two proteins [NO-responsive proteins (NORPs)] with different pi values responded to NO donors. One NORP (pI 5.2) appeared in response to NO, whereas another (pI 5.0) disappeared. These proteins were identified as a native form and a modified form of human glyoxalase I (Glox I; EC 4.4.1.5) by peptide mapping, microsequencing and correlation between the activity and the isoelectric shift. Glox I lost activity in response to NO, and all NO donors tested inhibited its activity in a dose-dependent manner. Activity and normal electrophoretic mobility were restored by dithiothreitol and by the removal of sources of NO from the culture medium. Glox I was selectively inactivated by NO; compounds that induce oxidative stress (H2O2, paraquat and arsenite) failed to inhibit this enzyme. Our results suggest that NO oxidatively modifies Glox I and reversibly inhibitsthe enzyme's activity. The inactivation of Glox I by NO was more effectivethan that of glyceraldehyde-3-phosphate dehydrogenase (G3PDH), another NO-sensitive enzyme. Thus Glox I seems to be a novel NO-responsive protein that is more sensitive to NO than G3PDH.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 11:06:21