Linked Life Data

11305591

Source:http://linkedlifedata.com/resource/pubmed/id/11305591

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2001-4-17
pubmed:abstractText
This study aimed to examine molecular mechanisms responsible for the metabolic fate of S-nitrosoglutathione (GSNO) in endothelial cells. After addition of 1 mM GSNO in culture medium, concentration of S-nitrosothiols (RSNO) significantly decreased with concomitant accumulation of nitrite (NO2-) only in the presence of human endothelial cells (ECV304), while no change in RSNO decomposition and NO2- accumulation was observed in case of S-nitrosocysteine. Bathocuproine disulfonic acid (BCS), a chelator for Cu(I), prevented the cell-mediated decomposition of RSNO and accumulation of NO2-. Chelator for Cu(III), Fe(II), or Fe(III); inhibitors of gamma-glutamyltranspeptidase; or a superoxide quenching enzyme had no effect on the cell-mediated degradation of RSNO and accumulation of NO2-. These results indicate that cellular Cu(I) would play a major role in the conversion of GSNO into NO2-. We recently demonstrated that human glyoxalase I (Glo I) interacts with GSNO in vitro and within cells. When Glo I interacts with GSNO, Glo I is inactivated and is chemically modified with pI alteration on 2D gels. So, we examined effect of Cu(I) chelation on the Glo I response. As a result, chelation of cellular Cu(I) by BCS enhanced the inactivation and chemical modification of Glo I by GSNO. The Glo I response could be detected when the cells were exposed to GSNO at 10 microM, corresponding to the concentration of RSNO under physiological conditions, with pretreatment of BCS. Metal chelators for copper and iron ions had no effect on the sensitivity of Glo I to an nitric oxide (NO) radical donor. These results indicate that chelation of cellular Cu(I) potentiates the sensitivity of GIo I to GSNO. The observation in the present study implicates that intracellular levels of GSNO might be elevated, accompanying with stabilization of extracellular RSNO.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Chelating Agents, http://linkedlifedata.com/resource/pubmed/chemical/Copper, http://linkedlifedata.com/resource/pubmed/chemical/Free Radicals, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione, http://linkedlifedata.com/resource/pubmed/chemical/Lactoylglutathione Lyase, http://linkedlifedata.com/resource/pubmed/chemical/Mercaptoethanol, http://linkedlifedata.com/resource/pubmed/chemical/Nitrites, http://linkedlifedata.com/resource/pubmed/chemical/Nitroso Compounds, http://linkedlifedata.com/resource/pubmed/chemical/S-Nitrosoglutathione, http://linkedlifedata.com/resource/pubmed/chemical/S-Nitrosothiols, http://linkedlifedata.com/resource/pubmed/chemical/S-nitrosomercaptoethanol, http://linkedlifedata.com/resource/pubmed/chemical/Sulfonic Acids
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0918-6158
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
336-41
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Chelation of cellular Cu(I) raised the degree of glyoxalase I inactivation in human endothelial cells upon exposure to S-nitrosoglutathione through stabilization of S-nitrosothiols.
pubmed:affiliation
School of Pharmaceutical Sciences, Kitasato University, Tokyo, Japan.
pubmed:publicationType
Journal Article