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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1998-7-2
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pubmed:abstractText |
The dibasic amino acid, L-arginine, is a substrate for both nitric oxide synthase (NOS) and arginase and therefore, plays an important role in cell signaling and cell growth. We examined the effects of various NOS inhibitors on L-arginine transport into rat renal brush border membrane (BBM) vesicles. L-Arginine uptake was stimulated in the presence of an inwardly directed Na+ gradient and an imposed inside negative potential in BBM but not basolateral membrane vesicles. In BBM vesicles, the L-arginine analogs, N-iminoethyl-L-orinithine and Nw-monomethyl-L-arginine (L-NMMA) were potent inhibitors of L-arginine uptake (IC50 of 0.48 and 0.82 mM, respectively), while Nw-nitro-L-arginine was less active (IC50 = 10 mM) and Nw-nitro-L-arginine methyl ester (L-NAME) was inactive. The inhibition of L-arginine transport by L-NMMA was competitive in nature. L-NIO, L-NMMA as well as L-arginine and L-lysine but not Nw-nitro-L-arginine methyl ester, trans-stimulated L-arginine uptake when preloaded into BBM vesicles. The L-arginine analogs had no effect on the transport of the neutral amino acid, L-leucine, in the same preparations. The data suggest that in addition to inhibiting NOS, the L-arginine analogs, N-iminoethyl-L-orinithine, L-NMMA and to a lesser extent L-NA, also inhibit L-arginine transport across the BBM of proximal tubules.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-3565
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
285
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1019-22
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:9618403-Animals,
pubmed-meshheading:9618403-Arginine,
pubmed-meshheading:9618403-Binding, Competitive,
pubmed-meshheading:9618403-Dose-Response Relationship, Drug,
pubmed-meshheading:9618403-Drug Interactions,
pubmed-meshheading:9618403-Enzyme Inhibitors,
pubmed-meshheading:9618403-Kidney Tubules, Proximal,
pubmed-meshheading:9618403-Male,
pubmed-meshheading:9618403-Microvilli,
pubmed-meshheading:9618403-NG-Nitroarginine Methyl Ester,
pubmed-meshheading:9618403-Rats,
pubmed-meshheading:9618403-Rats, Sprague-Dawley,
pubmed-meshheading:9618403-omega-N-Methylarginine
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pubmed:year |
1998
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pubmed:articleTitle |
Interaction of L-arginine analogs with L-arginine uptake in rat renal brush border membrane vesicles.
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pubmed:affiliation |
Department of Renal Pharmacology, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania, USA.
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pubmed:publicationType |
Journal Article
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