Linked Life Data

21311026

Source:http://linkedlifedata.com/resource/pubmed/id/21311026

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2011-4-28
pubmed:abstractText
Dietary protein is a major stimulant for cholecystokinin (CCK) secretion by the intestinal I cell, however, the mechanism by which protein is detected is unknown. Indirect functional evidence suggests that PepT1 may play a role in CCK-mediated changes in gastric motor function. However, it is unclear whether this oligopeptide transporter directly or indirectly activates the I cell. Using both the CCK-expressing enteroendocrine STC-1 cell and acutely isolated native I cells from CCK-enhanced green fluorescent protein (eGFP) mice, we aimed to determine whether PepT1 directly activates the enteroendocrine cell to elicit CCK secretion in response to oligopeptides. Both STC-1 cells and isolated CCK-eGFP cells expressed PepT1 transcripts. STC-1 cells were activated, as measured by ERK(1/2) phosphorylation, by both peptone and the PepT1 substrate Cefaclor; however, the PepT1 inhibitor 4-aminomethyl benzoic acid (AMBA) had no effect on STC-1 cell activity. The PepT1-transportable substrate glycyl-sarcosine dose-dependently decreased gastric motility in anesthetized rats but had no affect on activation of STC-1 cells or on CCK secretion by CCK-eGFP cells. CCK secretion was significantly increased in response to peptone but not to Cefaclor, cephalexin, or Phe-Ala in CCK-eGFP cells. Taken together, the data suggest that PepT1 does not directly mediate CCK secretion in response to PepT1 specific substrates. PepT1, instead, may have an indirect role in protein sensing in the intestine.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1522-1547
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
300
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
G895-902
pubmed:dateRevised
2011-8-1
pubmed:meshHeading
pubmed-meshheading:21311026-Animals, pubmed-meshheading:21311026-Blotting, Western, pubmed-meshheading:21311026-Caco-2 Cells, pubmed-meshheading:21311026-Cefaclor, pubmed-meshheading:21311026-Cell Line, pubmed-meshheading:21311026-Cell Separation, pubmed-meshheading:21311026-Cholecystokinin, pubmed-meshheading:21311026-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:21311026-Enteroendocrine Cells, pubmed-meshheading:21311026-Extracellular Signal-Regulated MAP Kinases, pubmed-meshheading:21311026-Gastrointestinal Motility, pubmed-meshheading:21311026-Humans, pubmed-meshheading:21311026-Immunohistochemistry, pubmed-meshheading:21311026-Mice, pubmed-meshheading:21311026-Mice, Transgenic, pubmed-meshheading:21311026-Peptones, pubmed-meshheading:21311026-Phosphorylation, pubmed-meshheading:21311026-Protein Hydrolysates, pubmed-meshheading:21311026-RNA, pubmed-meshheading:21311026-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:21311026-Symporters, pubmed-meshheading:21311026-Tranexamic Acid
pubmed:year
2011
pubmed:articleTitle
Protein hydrolysate-induced cholecystokinin secretion from enteroendocrine cells is indirectly mediated by the intestinal oligopeptide transporter PepT1.
pubmed:affiliation
Department of Anatomy, Physiology, and Cell Biology, School of Veterinary Medicine, University of California-Davis, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural