Source:http://linkedlifedata.com/resource/pubmed/id/11169462
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2001-2-22
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pubmed:abstractText |
Free amino acids and short chain peptides are the main digestion products of dietary proteins in the small intestine. Whether there is a direct interference in transport of both groups of degradation products is not known. We used human intestinal Caco-2 cells to investigate whether the absorption of dipeptides by the peptide transporter PEPT1 alters the apical uptake of free cationic and neutral amino acids. Influx of L-[3H]Arg into Caco-2 cells was Na+-independent and mediated mainly by the b(0,+) system recognizing both cationic and neutral amino acids. Preincubation of cells with 10 mM of selected neutral, mono- or dicationic dipeptides increased the influx of L-Arg up to fourfold. Preloading with equivalent concentrations of the corresponding free amino acids also increased L-Arg influx but dipeptides always proved to be more efficient. The observed trans-stimulation was found to be specific for cationic amino acids since transport of L-[3H]Ala remained unaffected. We here demonstrate for the first time a direct interplay in amino acid and peptide transport in intestinal cells that may selectively alter the kinetics of amino acid absorption.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/PepT1 protein,
http://linkedlifedata.com/resource/pubmed/chemical/SLC15A1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/Symporters
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9541
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2001 Wiley-Liss, Inc.
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pubmed:issnType |
Print
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pubmed:volume |
186
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
251-9
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pubmed:dateRevised |
2004-11-18
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pubmed:meshHeading |
pubmed-meshheading:11169462-Alanine,
pubmed-meshheading:11169462-Amino Acids,
pubmed-meshheading:11169462-Arginine,
pubmed-meshheading:11169462-Biological Transport,
pubmed-meshheading:11169462-Carrier Proteins,
pubmed-meshheading:11169462-Colonic Neoplasms,
pubmed-meshheading:11169462-Dipeptides,
pubmed-meshheading:11169462-Humans,
pubmed-meshheading:11169462-Intestinal Absorption,
pubmed-meshheading:11169462-Intestinal Mucosa,
pubmed-meshheading:11169462-Intestine, Small,
pubmed-meshheading:11169462-Kinetics,
pubmed-meshheading:11169462-Sodium,
pubmed-meshheading:11169462-Symporters,
pubmed-meshheading:11169462-Tumor Cells, Cultured
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pubmed:year |
2001
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pubmed:articleTitle |
PEPT1-mediated uptake of dipeptides enhances the intestinal absorption of amino acids via transport system b(0,+).
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pubmed:affiliation |
Institute of Nutritional Sciences, Molecular Nutrition Unit, Technical University of Munich, Hochfeldweg 2, Freising-Weihenstephan, Germany.
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pubmed:publicationType |
Journal Article
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