| Nitric oxide inactivates glyoxalase I in cooperation with glutathione. | |
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MedLine Citation:
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PMID: 11011147 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We previously found that glyoxalase I (Glo I) is inactivated upon exposure of 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 NO action 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. |
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Authors:
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A Mitsumoto; K R Kim; G Oshima; M Kunimoto; K Okawa; A Iwamatsu; Y Nakagawa |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Journal of biochemistry Volume: 128 ISSN: 0021-924X ISO Abbreviation: J. Biochem. Publication Date: 2000 Oct |
Date Detail:
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Created Date: 2000-12-22 Completed Date: 2000-12-22 Revised Date: 2007-12-19 |
Medline Journal Info:
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Nlm Unique ID: 0376600 Medline TA: J Biochem Country: JAPAN |
Other Details:
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Languages: eng Pagination: 647-54 Citation Subset: IM |
Affiliation:
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School of Pharmaceutical Sciences, Kitasato University, Tokyo, 108-8641, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Cell Line Cell Membrane Permeability Cysteine / analogs & derivatives, pharmacology Electrophoresis, Gel, Two-Dimensional Endothelium / cytology, drug effects, enzymology, metabolism Erythrocytes / enzymology Glutathione / analogs & derivatives, metabolism, pharmacology* Glyceraldehyde-3-Phosphate Dehydrogenases / antagonists & inhibitors, metabolism Humans Kinetics Lactoylglutathione Lyase / antagonists & inhibitors*, metabolism Nitric Oxide / metabolism, pharmacology* Nitroso Compounds / pharmacology S-Nitrosoglutathione S-Nitrosothiols* |
| Chemical | |
Reg. No./Substance:
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0/Nitroso Compounds; 0/S-Nitrosothiols; 10102-43-9/Nitric Oxide; 31702-37-1/S-(4-bromobenzyl)glutathione; 51209-75-7/S-nitrosocysteine; 52-90-4/Cysteine; 57564-91-7/S-Nitrosoglutathione; 70-18-8/Glutathione; EC 1.2.1.-/Glyceraldehyde-3-Phosphate Dehydrogenases; EC 4.4.1.5/Lactoylglutathione Lyase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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