Details

Autor(en) / Beteiligte

• Mohr, Susanne
• Hallak, Hazem
• de Boitte, Alexander
• Lapetina, Eduardo G.
• Brüne, Bernhard

Titel

Nitric Oxide-induced S-Glutathionylation and Inactivation of Glyceraldehyde-3-phosphate Dehydrogenase

Ist Teil von

• The Journal of biological chemistry, 1999-04, Vol.274 (14), p.9427-9430

Ort / Verlag

United States: American Society for Biochemistry and Molecular Biology

Erscheinungsjahr

1999

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• S -Nitrosylation of protein thiol groups by nitric oxide (NO) is a widely recognized protein modification. In this study we show that nitrosonium tetrafluoroborate (BF 4 NO), a NO + donor, modified the thiol groups of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by S -nitrosylation and caused enzyme inhibition. The resultant protein- S -nitrosothiol was found to be unstable and to decompose spontaneously, thereby restoring enzyme activity. In contrast, the NO-releasing compound S -nitrosoglutathione (GSNO) promoted S -glutathionylation of a thiol group of GAPDH both in vitro and under cellular conditions. The GSH-mixed protein disulfide formed led to a permanent enzyme inhibition, but upon dithiothreitol addition a functional active GAPDH was recovered. This S -glutathionylation is specific for GSNO because GSH itself was unable to produce protein-mixed disulfides. During cellular nitrosative stress, the production of intracellular GSNO might channel signaling responses to form protein-mixed disulfide that can regulate intracellular function.