Comprehensive Physiology 2018
DOI: 10.1002/cphy.c170038
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Proton Coupled Oligopeptide Transporter 1 (PepT1) Function, Regulation, and Influence on the Intestinal Homeostasis

Abstract: As the organ with one of the largest surface areas facing the environment and responsible for nutrient uptake, the small intestine expresses numerous transport proteins in its brush-border membrane for efficient absorption and supply of dietary macro- and micronutrients. The understanding of regulation and functional interplay of these nutrient transporters is of emerging interest in nutrition and medical physiology research in respect to development of diabetes, obesity, and inflammatory bowel disease worldwi… Show more

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Cited by 51 publications
(41 citation statements)
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“…13 Peptide transporter 1 (PepT1) is an oligopeptide transporter and abundantly expressed in the apical (AP) membrane of the intestinal epithelium. 14,15 Due to high capacity and broad substrate specificity, PepT1 could efficiently identify and transport amino acid and oligopeptide (di/tripeptides), including L-valine, L-phenylalanine, and L-Val-L-Val. 16,17 It is determined that targeting PepT1 could have a high affinity for epithelium and improve intestinal permeability and oral absorption of the drug due to the amino group.…”
Section: Introductionmentioning
confidence: 99%
“…13 Peptide transporter 1 (PepT1) is an oligopeptide transporter and abundantly expressed in the apical (AP) membrane of the intestinal epithelium. 14,15 Due to high capacity and broad substrate specificity, PepT1 could efficiently identify and transport amino acid and oligopeptide (di/tripeptides), including L-valine, L-phenylalanine, and L-Val-L-Val. 16,17 It is determined that targeting PepT1 could have a high affinity for epithelium and improve intestinal permeability and oral absorption of the drug due to the amino group.…”
Section: Introductionmentioning
confidence: 99%
“…Anionic AAs are absorbed by SLC1A1 (EAAT3), which exchanges a complex of 3Na ϩ -1H ϩ -1AA Ϫ for 1K ϩ . In the small intestine, much if not most dietary protein is absorbed, not in the form of free AAs, but rather as di-and tripeptides by the proton-oligopeptide cotransporter PepT1 (SLC15A1) (46). Because these AA transporters carry different AAs and co-substrate ions (Na ϩ , H ϩ , Cl Ϫ ), the absorptive flux of each AA is expected to depend on the following: 1) the assemblage of accumulative and exchange transporters in the apical and basolateral membranes of regional epithelial cells; 2) the intrinsic affinities of apical transporters for AAs and their cosubstrate ions; 3) the regional availability of luminal substrates (AA, Na ϩ , H ϩ , Cl Ϫ ), and 4) the regulated activity of the rate-limiting transport process.…”
Section: Discussionmentioning
confidence: 99%
“…Many function as obligate AA exchangers or cotransporters driven by Na ϩ , H ϩ , or Cl Ϫ electrochemical gradients (23). In addition to AA transporters, intestinal epithelial cells are equipped with an apical H ϩ -peptide cotransporter (PepT-1, SLC15A1) that is responsible for a substantial fraction of dietary protein assimilation (46). The integrated operation of multiple transporters with overlapping substrate preferences allows for gradient coupling and efficient scavenging of diverse AAs from the intestinal lumen.…”
Section: Introductionmentioning
confidence: 99%
“…PEPT1 can also transport a vast amount of substrates, including drugs and bacterial products, and may thus be both of important pathophysiological consequence, as well as an interesting target for drug design. Although much has been learned regarding its transcriptional regulation of PEPT1 expression and the influence of hormones and intracellular kinases (Spanier & Rohm, ), less is known about the trafficking, membrane retention, the interaction with other transporters, and the ionic requirements for sustained H + /dipeptide absorption (Spanier & Rohm, ).…”
Section: Discussionmentioning
confidence: 99%