| pubmed-article:2677320 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2677320 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2677320 | lifeskim:mentions | umls-concept:C0010453 | lld:lifeskim |
| pubmed-article:2677320 | lifeskim:mentions | umls-concept:C0225336 | lld:lifeskim |
| pubmed-article:2677320 | lifeskim:mentions | umls-concept:C0041637 | lld:lifeskim |
| pubmed-article:2677320 | lifeskim:mentions | umls-concept:C0949771 | lld:lifeskim |
| pubmed-article:2677320 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:2677320 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:2677320 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:2677320 | pubmed:dateCreated | 1989-11-1 | lld:pubmed |
| pubmed-article:2677320 | pubmed:abstractText | 1. Nutrient transport in cultured human umbilical vein endothelial cells was characterized using a rapid dual-isotope dilution technique. Microcarrier beads with confluent endothelial cells were perfused in small columns, and uptake and efflux were assessed relative to D-mannitol (extracellular tracer) during a single transit through the column. 2. At tracer concentrations significant unidirectional uptakes were measured for L-leucine (53 +/- 2%), L-phenylalanine (73 +/- 2%), L-serine (40 +/- 4%), L-arginine (42 +/- 3%) and L-ornithine (26 +/- 3%). Uptake for L-proline, D-glucose, dopamine and serotonin was lower (6-10%), whereas uptake for the system A analogue 2-methylaminoisobutyric acid (2-MeAIB) was negligible. Uptakes rapidly decreased with time due to tracer efflux. 3. Endothelial cell transport of L-leucine was markedly inhibited during perfusion with 1 mM-BCH (beta-2-aminobicyclo-(2,2,1)-heptane-2-carboxylic acid, system L analogue), L-leucine, D-leucine, L-phenylalanine, L-methionine and L-DOPA. 2-MeAIB, L-cysteine, glycine, L-proline, hydroxy-L-proline, L-aspartate and beta-alanine were poor inhibitors, while L-serine and the cationic substrates L-lysine and L-arginine inhibited uptake by 10-35%. 4. When the kinetics of L-leucine transport were examined over a wide range of substrate concentrations (0.025-1 mM) transport was saturable. A single entry site analysis gave a half-maximal saturation constant Kt = 0.24 +/- 0.08 mM (mean +/- S.E.M., n = 5) and a Vmax = 27.8 +/- 4.6 nmol/min per column (approximately 3 x 10(6) cells). 5. Removal of sodium from the perfusate inhibited tracer uptake of L-leucine, L-serine and L-arginine by respectively 20 +/- 5% (n = 3), 77 +/- 5% (n = 3) and 35 +/- 4% (n = 3). 6. Our results provide the first evidence that cultured human endothelial cells of venous origin express a saturable transport system for large neutral amino acids resembling system L described in brain microvascular endothelium. Detection of Na+-dependent and Na+-independent L-arginine uptake is of interest in view of recent reports that this cationic amino acid may be the physiological precursor for nitric oxide released by endothelium. | lld:pubmed |
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| pubmed-article:2677320 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2677320 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2677320 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2677320 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2677320 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2677320 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:2677320 | pubmed:issn | 0022-3751 | lld:pubmed |
| pubmed-article:2677320 | pubmed:author | pubmed-author:MannG EGE | lld:pubmed |
| pubmed-article:2677320 | pubmed:author | pubmed-author:PearsonJ DJD | lld:pubmed |
| pubmed-article:2677320 | pubmed:author | pubmed-author:ToothillV JVJ | lld:pubmed |
| pubmed-article:2677320 | pubmed:author | pubmed-author:SheriffC JCJ | lld:pubmed |
| pubmed-article:2677320 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2677320 | pubmed:volume | 410 | lld:pubmed |
| pubmed-article:2677320 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2677320 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2677320 | pubmed:pagination | 325-39 | lld:pubmed |
| pubmed-article:2677320 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:2677320 | pubmed:meshHeading | pubmed-meshheading:2677320-... | lld:pubmed |
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| pubmed-article:2677320 | pubmed:meshHeading | pubmed-meshheading:2677320-... | lld:pubmed |
| pubmed-article:2677320 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2677320 | pubmed:articleTitle | Expression of amino acid transport systems in cultured human umbilical vein endothelial cells. | lld:pubmed |
| pubmed-article:2677320 | pubmed:affiliation | Department of Physiology, King's College, London. | lld:pubmed |
| pubmed-article:2677320 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2677320 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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