Source:http://linkedlifedata.com/resource/pubmed/id/15623827
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
2004-12-29
|
pubmed:abstractText |
Reactive oxygen species (ROS) produced by gut mucosal cells during conditions such as inflammatory bowel disease (IBD) may impair mucosal repair and nutrient transport/absorptive function. Absorption of di- and tripeptides in the small intestine and colon is mediated by the H(+)-dependent transporter PepT1, but effects of oxidative stress on di- and tripeptide transport are unknown. We assessed whether exposure to hydrogen peroxide (H(2)O(2)) influences dipeptide transport in human colonic epithelial (Caco-2) cells. Uptake of [(14)C]glycylsarcosine (Gly-Sar) was used to evaluate PepT1-mediated dipeptide transport. Exposure to 1-5 mmol/L H(2)O(2) for 24 h caused a dose-dependent decrease in Gly-Sar transport, which was associated with decreased PepT1 transport velocity (V(max)). Treatment with alanylglutamine (Ala-Gln) or growth hormone (GH) did not alter Caco-2 Gly-Sar transport in the absence of H(2)O(2). However, both Ala-Gln and GH prevented the decrease in dipeptide transport observed with 1 mmol/L H(2)O(2) treatment. Ala-Gln, but not GH, maintained cellular glutathione and prevented the decrease in PepT1 protein expression. Thus, these agents should be further investigated as potential therapies to improve absorption of small peptides in disorders associated with oxidative injury to the gut mucosa.
|
pubmed:grant |
http://linkedlifedata.com/resource/pubmed/grant/F32 DK65345,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK55850,
http://linkedlifedata.com/resource/pubmed/grant/R01 ES009047,
http://linkedlifedata.com/resource/pubmed/grant/R01 ES011195,
http://linkedlifedata.com/resource/pubmed/grant/R24 DK064399
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Human Growth Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/PepT1 protein,
http://linkedlifedata.com/resource/pubmed/chemical/Symporters,
http://linkedlifedata.com/resource/pubmed/chemical/alanylglutamine
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0022-3166
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
135
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
19-26
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:15623827-Biological Transport,
pubmed-meshheading:15623827-Cell Line, Tumor,
pubmed-meshheading:15623827-Colonic Neoplasms,
pubmed-meshheading:15623827-Dipeptides,
pubmed-meshheading:15623827-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:15623827-Human Growth Hormone,
pubmed-meshheading:15623827-Humans,
pubmed-meshheading:15623827-Intestinal Mucosa,
pubmed-meshheading:15623827-Oxidative Stress,
pubmed-meshheading:15623827-Symporters
|
pubmed:year |
2005
|
pubmed:articleTitle |
Alanylglutamine dipeptide and growth hormone maintain PepT1-mediated transport in oxidatively stressed Caco-2 cells.
|
pubmed:affiliation |
Department of Nutrition Science, University of Bonn, Germany.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|