| pubmed-article:1371384 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1371384 | lifeskim:mentions | umls-concept:C0020281 | lld:lifeskim |
| pubmed-article:1371384 | lifeskim:mentions | umls-concept:C0907533 | lld:lifeskim |
| pubmed-article:1371384 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:1371384 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:1371384 | pubmed:dateCreated | 1992-3-24 | lld:pubmed |
| pubmed-article:1371384 | pubmed:abstractText | L-Arginine-derived nitric oxide (NO) acts as an inter- and intra-cellular signal molecule in many mammalian tissues including brain, where it is formed by a flavin-containing Ca2+/calmodulin-requiring NO synthase with NADPH, tetrahydrobiopterin (H4biopterin) and molecular oxygen as cofactors. We found that purified brain NO synthase acted as a Ca2+/calmodulin-dependent NADPH:oxygen oxidoreductase, catalysing the formation of hydrogen peroxide at suboptimal concentrations of L-arginine or H4biopterin, which inhibited the hydrogen peroxide formation with half-maximal effects at 11 microM and 0.3 microM respectively. Half-maximal rates of L-citrulline formation were observed at closely similar concentrations of these compounds, indicating that the NO synthase-catalysed oxygen activation was coupled to the synthesis of L-citrulline and NO in the presence of L-arginine and H4biopterin. N omega-Nitro-L-arginine, its methyl ester and N omega-monomethyl-L-arginine inhibited the synthesis of L-citrulline from L-arginine (100 microM) with half-maximal effects at 0.74 microM, 2.8 microM and 15 microM respectively. The N omega-nitro compounds also blocked the substrate-independent generation of hydrogen peroxide, whereas N omega-monomethyl-L-arginine did not affect this reaction. According to these results, activation of brain NO synthase by Ca2+ at subphysiological levels of intracellular L-arginine or H4biopterin may result in the formation of reactive oxygen species instead of NO, and N omega-nitro-substituted L-arginine analogues represent useful tools to effectively block NO synthase-catalysed oxygen activation. | lld:pubmed |
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| pubmed-article:1371384 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1371384 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1371384 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1371384 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1371384 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:1371384 | pubmed:author | pubmed-author:BöhmeEE | lld:pubmed |
| pubmed-article:1371384 | pubmed:author | pubmed-author:JohnMM | lld:pubmed |
| pubmed-article:1371384 | pubmed:author | pubmed-author:MayerBB | lld:pubmed |
| pubmed-article:1371384 | pubmed:author | pubmed-author:KlattPP | lld:pubmed |
| pubmed-article:1371384 | pubmed:author | pubmed-author:HeinzelBB | lld:pubmed |
| pubmed-article:1371384 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1371384 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1371384 | pubmed:volume | 281 ( Pt 3) | lld:pubmed |
| pubmed-article:1371384 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1371384 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1371384 | pubmed:pagination | 627-30 | lld:pubmed |
| pubmed-article:1371384 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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| pubmed-article:1371384 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1371384 | pubmed:articleTitle | Ca2+/calmodulin-dependent formation of hydrogen peroxide by brain nitric oxide synthase. | lld:pubmed |
| pubmed-article:1371384 | pubmed:affiliation | Institut für Pharmakologie, Freie Universität Berlin, Federal Republic of Germany. | lld:pubmed |
| pubmed-article:1371384 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1371384 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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