Glyoxalase I is a novel nitric-oxide-responsive protein.

The Biochemical journal ·Vol. 344 Pt 3 ·1999-12-15 ·Pages 837-44

Mitsumoto A, Kim KR, Oshima G, Kunimoto M, Okawa K, Iwamatsu A, Nakagawa Y

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 (H(2)O(2), paraquat and arsenite) failed to inhibit this enzyme. Our results suggest that NO oxidatively modifies Glox I and reversibly inhibits the enzyme's activity. The inactivation of Glox I by NO was more effective than 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.

MeSH Terms

Arsenites/pharmacology Cells, Cultured Dithiothreitol/pharmacology Electrophoresis, Gel, Two-Dimensional Glutathione/analogs & derivatives,pharmacology Glyceraldehyde-3-Phosphate Dehydrogenases/metabolism Humans Hydrogen Peroxide/pharmacology Lactoylglutathione Lyase/metabolism Nitric Oxide/pharmacology Nitroso Compounds/pharmacology Oxidative Stress Paraquat/pharmacology Peptide Mapping S-Nitrosoglutathione

Chemicals

Arsenites Nitroso Compounds Nitric Oxide S-Nitrosoglutathione Hydrogen Peroxide Glyceraldehyde-3-Phosphate Dehydrogenases Lactoylglutathione Lyase Glutathione arsenite Paraquat Dithiothreitol

Authors & Affiliations

7 authors, click to expand affiliations / ORCID

Mitsumoto A

School of Pharmaceutical Sciences, Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo, 108-8641 Japan.

Kim K R

Oshima G

Kunimoto M

Okawa K

Iwamatsu A

Nakagawa Y

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

Published

1999-12-15

Pages

837-44

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1220706

Subset

External Links

PubMed source PMC Full Text View journal details

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Glyoxalase I is a novel nitric-oxide-responsive protein.

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