Source:http://linkedlifedata.com/resource/pubmed/id/11408272
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2001-6-15
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pubmed:abstractText |
The human intestinal cell line Caco-2 was used as a model system to study the effects of epidermal growth factor (EGF) on peptide transport. EGF decreased apical-to-basolateral fluxes of [(14)C]glycylsarcosine ([(14)C]Gly-Sar) up to 50.2 +/- 3.6% (n = 6) of control values. Kinetic analysis of the fluxes showed that maximal flux (V(max)) of transepithelial transport decreased from 3.00 +/- 0.17 nmol x cm(-2) x min(-1) in control cells to 0.50 +/- 0.07 nmol x cm(-2) x min(-1) in cells treated with 5 ng/ml EGF (n = 6, P < 0.01). The apparent Michaelis-Menten constant (K(m)) was 2.71 +/- 0.31 mM (n = 6) in control cells and 1.89 +/- 0.28 mM (n = 6, not significantly different from control) in EGF-treated cells. Similarly, apical uptake of [(14)C]Gly-Sar decreased in cells treated with EGF, with an ED(50) value of 0.36 +/- 0.06 ng/ml (n = 6) EGF and a maximal inhibition of 80 +/- 0.02% (n = 6). V(max) decreased from 2.61 +/- 0.4 to 1.06 +/- 0.1 nmol x cm(-2) x min(-1) (n = 3, P < 0.05), whereas K(m) remained constant. Basolateral Gly-Sar uptake showed no changes in V(max) or K(m) after EGF treatment (n = 3). RT-PCR showed a decrease in hPepT1 mRNA (using glucose-6-phosphate dehydrogenase mRNA as control) in cells treated with EGF. Western blotting indicated a decrease in hPepT1 protein in cell lysates. We conclude that EGF treatment decreases Gly-Sar transport in Caco-2 cells by decreasing the number of peptide transporter molecules in the apical membrane.
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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/Carbon Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/PepT1 protein,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/SLC15A1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Symporters,
http://linkedlifedata.com/resource/pubmed/chemical/glycylsarcosine
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0193-1857
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
G191-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11408272-Biological Transport,
pubmed-meshheading:11408272-Caco-2 Cells,
pubmed-meshheading:11408272-Carbon Radioisotopes,
pubmed-meshheading:11408272-Carrier Proteins,
pubmed-meshheading:11408272-Dipeptides,
pubmed-meshheading:11408272-Dose-Response Relationship, Drug,
pubmed-meshheading:11408272-Epidermal Growth Factor,
pubmed-meshheading:11408272-Gene Expression,
pubmed-meshheading:11408272-Humans,
pubmed-meshheading:11408272-Immunohistochemistry,
pubmed-meshheading:11408272-Intestinal Mucosa,
pubmed-meshheading:11408272-Microscopy, Confocal,
pubmed-meshheading:11408272-RNA, Messenger,
pubmed-meshheading:11408272-Symporters
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pubmed:year |
2001
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pubmed:articleTitle |
Epidermal growth factor inhibits glycylsarcosine transport and hPepT1 expression in a human intestinal cell line.
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pubmed:affiliation |
Department of Pharmaceutics, Royal Danish School of Pharmacy, DK-2100 Copenhagen, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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