rdf:type |
|
lifeskim:mentions |
umls-concept:C0003765,
umls-concept:C0014257,
umls-concept:C0017797,
umls-concept:C0033268,
umls-concept:C0132555,
umls-concept:C0332291,
umls-concept:C0392747,
umls-concept:C0470187,
umls-concept:C1280500,
umls-concept:C1704675,
umls-concept:C1710236
|
pubmed:issue |
6
|
pubmed:dateCreated |
1995-7-6
|
pubmed:abstractText |
The effect of extracellular L-arginine and L-glutamine on nitric oxide (NO) release was studied in cultured bovine aortic endothelial cells and in rabbit aortic rings. Increasing L-arginine (0.01 to 10 mM) did not alter NO release from cultured endothelial cells or modify endothelium-dependent relaxation to acetylcholine in isolated vessels. L-Glutamine (0.6 and 2 mM) inhibited NO release from cultured cells (in response to bradykinin) and from aortic rings (in response to acetylcholine or ADP). L-Arginine (0.1-10 mM) dose-dependently reversed the L-glutamine inhibition of receptor-stimulated NO release in both models. In contrast to its inhibitory response to receptor-mediated stimuli, glutamine alone slightly potentiated NO release in both models when the calcium ionophore, A23187, was added. Furthermore, cultured cells incubated with L-arginine (0.01-10 mM), in the presence or absence of glutamine, released similar amounts of NO in response to A23187. L-Glutamine did not affect intracellular L-arginine levels. Neither D-glutamine nor D-arginine affected NO release or endothelium-dependent vascular relaxation. L-Glutamine had no effect on the activity of endothelial NOS assessed by L-arginine to L-citrulline conversion. These findings show that in the absence of L-glutamine, manipulating intracellular L-arginine levels over a wide range does not affect NO release. L-Glutamine in concentrations circulating in vivo may tonically inhibit receptor-mediated NO release by interfering with signal transduction. One mechanism by which L-arginine may enhance NO release is via reversal of the inhibitory effect of L-glutamine, but apparently independently of enhancing NO synthase substrate.
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pubmed:grant |
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-1347093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-1375933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-1385480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-1401062,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-1683971,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-1689048,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-1707354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-1720542,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-1912602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-1975886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-1978327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-1999009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-2236071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-2245496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-2268354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-2440339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-2619057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-2784944,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-3093861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-3691808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-7514592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-7515853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-7526698,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-7687064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-8238295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7539455-8491002
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
AIM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0021-9738
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
95
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2565-72
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7539455-Acetylcholine,
pubmed-meshheading:7539455-Amino Acid Oxidoreductases,
pubmed-meshheading:7539455-Animals,
pubmed-meshheading:7539455-Arginine,
pubmed-meshheading:7539455-Cattle,
pubmed-meshheading:7539455-Cells, Cultured,
pubmed-meshheading:7539455-Cytoplasm,
pubmed-meshheading:7539455-Endothelium, Vascular,
pubmed-meshheading:7539455-Extracellular Space,
pubmed-meshheading:7539455-Gene Expression,
pubmed-meshheading:7539455-Glutamine,
pubmed-meshheading:7539455-Nitric Oxide,
pubmed-meshheading:7539455-Nitric Oxide Synthase,
pubmed-meshheading:7539455-RNA, Messenger,
pubmed-meshheading:7539455-Vasodilation
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pubmed:year |
1995
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pubmed:articleTitle |
Interactions between L-arginine and L-glutamine change endothelial NO production. An effect independent of NO synthase substrate availability.
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pubmed:affiliation |
Department of Medicine, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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