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Titolo:
Nitric oxide inactivates glyoxalase I in cooperation with glutathione
Autore:
Mitsumoto, A; Kim, KR; Oshima, G; Kunimoto, M; Okawa, K; Iwamatsu, A; Nakagawa, Y;
Indirizzi:
Kitasato Univ, Sch Pharmaceut Sci, Tokyo 1088641, Japan Kitasato Univ Tokyo Japan 1088641 h Pharmaceut Sci, Tokyo 1088641, Japan Natl Inst Environm Studies, Tsukuba, Ibaraki, Japan Natl Inst Environm Studies Tsukuba Ibaraki Japan Tsukuba, Ibaraki, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Yokohama, Kanagawa, Japan Kirin Brewery Co Ltd Yokohama Kanagawa Japan , Yokohama, Kanagawa, Japan
Titolo Testata:
JOURNAL OF BIOCHEMISTRY
fascicolo: 4, volume: 128, anno: 2000,
pagine: 647 - 654
SICI:
0021-924X(200010)128:4<647:NOIGII>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
S-NITROSOGLUTATHIONE; MEDIATED DECOMPOSITION; LIQUID-CHROMATOGRAPHY; REACTION-MECHANISM; NITROSOTHIOLS; INHIBITION; CELLS; NITROSYLATION; NITROSOHEMOGLOBIN; IDENTIFICATION;
Keywords:
endothelial cells; glutathione; glyoxalase I; nitrosative stress; S-nitrosoglutathione;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Nakagawa, Y Kitasato Univ, Sch Pharmaceut Sci, Tokyo 1088641, Japan Kitasato Univ Tokyo Japan 1088641 Sci, Tokyo 1088641, Japan
Citazione:
A. Mitsumoto et al., "Nitric oxide inactivates glyoxalase I in cooperation with glutathione", J BIOCHEM, 128(4), 2000, pp. 647-654

Abstract

We previously found that glyoxalase I (Glo I) is inactivated upon exposureof human endothelial cells to extracellular nitric oxide (NO), and this event correlates with an increase in its pi on two-dimensional gels. In this study, we demonstrate that NO can modulate Glo I activity in cooperation with cellular glutathione (GSH), Severe depletion of intracellular GSH prevents the inactivation of Glo I in response to NO, although such depletion enhances the inactivation of glyceraldehyde-3-phosphate dehydrogenase (G3PDH),a well-known enzyme susceptible to NO-induced oxidation, S-Nitrosoglutathione (GSNO), an adduct of GSH and NO, lowers the activity of purified human Glo I, while S-nitrosocysteine (CysNO) inactivates the enzyme only in the presence of GSH. This indicates that a dysfunction in Glo I would require the formation of GSNO in situ, Competitive inhibitors of Glo I, S-(4-bromobenzyl)glutathione and its membrane-permeating form, completely abolish the NOaction in vitro and inside cells, respectively. Taken together, these results reveal that Glo I can interact directly with GSNO, and that the interaction converts Glo I into an inactive form, Moreover, the data suggest that the substrate recognition site of Glo I might be involved in the interaction with GSNO.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/21 alle ore 04:42:23