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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4 Pt 1
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pubmed:dateCreated |
1995-6-1
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pubmed:abstractText |
This study describes the ability of passaged human intestinal Caco-2 cells to regulate transport of L-arginine via system y+. Subconfluent and confluent cells possessed system y+ activity, as determined by the sodium independence of uptake and the pattern of inhibition by amino acid analogues or N-ethylmaleimide. Initial rates of arginine uptake via system y+ decreased as the cells advanced from the undifferentiated to the differentiated state following culture passaging. Furthermore, kinetic analysis of the leucine-insensitive portion of uptake indicated that the Caco-2 system y+ transport capacity decreased with cell age, dropping from a maximal velocity (Vmax) = 1,094 pmol.mg-1.min-1 [Michaelis constant (Km) = 41 microM] in undifferentiated cells 2 days postseeding to Vmax = 320 pmol.mg-1.min-1 (Km = 37 microM) in confluent cells 9 days postseeding (from cells of the same passage). Northern analysis indicated that the levels of a single 7.9-kb mCAT-1 mRNA species were relatively constant over the course of Caco-2 differentiation and therefore were unsynchronized with the system y+ relative transport activities. It is concluded that the Caco-2 capacity to transport arginine via system y+ may be downregulated by posttransitional modifications in confluent cells compared with newly passaged undifferentiated cells. These data serve as a well-defined in vitro model for further studies regarding regulation of arginine transport in epithelial cells.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
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/Ethylmaleimide,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Virus,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/ecotropic murine leukemia virus...
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0002-9513
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
G578-85
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7733284-Amino Acids,
pubmed-meshheading:7733284-Arginine,
pubmed-meshheading:7733284-Blotting, Northern,
pubmed-meshheading:7733284-Carrier Proteins,
pubmed-meshheading:7733284-Cell Differentiation,
pubmed-meshheading:7733284-Cell Line,
pubmed-meshheading:7733284-Ethylmaleimide,
pubmed-meshheading:7733284-Humans,
pubmed-meshheading:7733284-Hydrogen-Ion Concentration,
pubmed-meshheading:7733284-Intestines,
pubmed-meshheading:7733284-Kinetics,
pubmed-meshheading:7733284-Leucine,
pubmed-meshheading:7733284-Membrane Glycoproteins,
pubmed-meshheading:7733284-Membrane Proteins,
pubmed-meshheading:7733284-Receptors, Virus,
pubmed-meshheading:7733284-Sodium
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pubmed:year |
1995
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pubmed:articleTitle |
Regulation of system y+ arginine transport capacity in differentiating human intestinal Caco-2 cells.
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pubmed:affiliation |
Department of Physiology, College of Medicine, University of Florida, Gainesville 32610-0274, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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