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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1995-2-22
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pubmed:abstractText |
The present study demonstrates that human platelets possess a specific L-arginine transport system able to provide adequate amounts of L-arginine for endogenous nitric oxide production. L-arginine uptake takes place through a saturable high affinity carrier-mediated Na(+)-independent process which is significantly inhibited by L-ornithine, L-lysine and N omega-methyl-L-arginine. The high affinity of the transport process and the pattern of inhibition are consistent with mediation of L-arginine transport via the Na(+)-independent y+ system. The data on the kinetic parameters of the transporter suggest a possible role for arginine plasma levels in the regulation of platelet nitric oxide production.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
206
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
878-84
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7832800-Arginine,
pubmed-meshheading:7832800-Biological Transport,
pubmed-meshheading:7832800-Blood Platelets,
pubmed-meshheading:7832800-Carrier Proteins,
pubmed-meshheading:7832800-Humans,
pubmed-meshheading:7832800-Kinetics,
pubmed-meshheading:7832800-Lysine,
pubmed-meshheading:7832800-Nitric Oxide,
pubmed-meshheading:7832800-Ornithine,
pubmed-meshheading:7832800-Sodium,
pubmed-meshheading:7832800-omega-N-Methylarginine
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pubmed:year |
1995
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pubmed:articleTitle |
Identification of a specific transport system for L-arginine in human platelets.
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pubmed:affiliation |
Department of Biochemical Sciences, University of Firenze, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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