Oligopeptide transport by epithelial cells

  title={Oligopeptide transport by epithelial cells},
  author={D. Meredith and C. Boyd},
  journal={The Journal of Membrane Biology},
This review focuses on the mechanism of peptide entry into and exit from vertebrate epithelial cells. The entry step across the apical membrane, a particularly interesting example of ion-coupled, electrogenic transport, is contrasted with the electroneutral exit step at the basolateral membrane. As in many reviews on other aspects of epithelial function, a keynote is this asymmetry between the processes occurring at the apical and basolateral membranes. However, in contrast to many epithelial… Expand
Carrier-Mediated Mechanisms for Cellular Drug Transport
Transporters are a group of polytopic membrane proteins that are involved in almost all biological functions in the cell. In brief, they mediate the entry of nutrients; facilitate uptake and releaseExpand
Transepithelial Transport of the Bioactive Tripeptide, Val-Pro-Pro, in Human Intestinal Caco-2 Cell Monolayers
PepT1-mediated transport was not involved in the transepithelial transport of intact Val-Pro-Pro, suggesting that food-derived tripeptides with angiotensin converting enzyme (ACE)-inhibitory activity were not hypotensive after being orally administered. Expand
The mammalian proton-coupled peptide cotransporter PepT1: sitting on the transporter–channel fence?
  • D. Meredith
  • Biology, Medicine
  • Philosophical Transactions of the Royal Society B: Biological Sciences
  • 2008
expression studies in Xenopus laevis on rabbit PepT1 that had undergone site-directed mutagenesis of a conserved arginine residue revealed that this residue played a role in the coupling of proton and peptide transport and prevented the movement of non-coupled ions during the transporter cycle. Expand
Peptide and peptide analog transport systems at the blood-CSF barrier.
This review addresses three main areas: choroid plexus structure, physiology, and barrier function in relation to peptide transport; polypeptide transport and secretion mechanisms into cerebrospinal fluid; and molecular physiology, expression, and functional activity of proton-coupled oligopeptide transporters in choroids. Expand
The renal type H+/peptide symporter PEPT2: structure-affinity relationships
This review compiled available affinity constants of 352 compounds, measured at different mammalian tissues and expression systems and compare the data whenever possible with those of PEPT1, its intestinal counterpart. Expand
Enhanced Daunomycin Accumulation in Human Intestinal Caco-2 Cells from Non-Ionic Food Emulsifiers Unrelated to the P-Glycoprotein Inhibitory Mechanism
The results suggest that these food emulsifiers specifically inhibited P-gp, the multi-drug transporter. Expand
Selectivity of the polyspecific cation transporter rOCT1 is changed by mutation of aspartate 475 to glutamate.
The data suggest that rOCT1 contains a large cation-binding pocket with several interaction domains that may be responsible for high-affinity binding of structurally different cations and that Asp475 is located close to one of these interaction domains. Expand
Characteristics of Lysophosphatidylcholine in Its Inhibition of Taurine Uptake by Human Intestinal Caco-2 Cells
The results suggest that the interaction of LPC with the taurine transporter in the intestinal cell membrane was the cause of the reduced taurines uptake. Expand
A modelforthekinetics ofneutral andanionic dipeptide-proton cotransport bytheapical membraneofrat kidney cortex
1. Kinetics ofinflux (mediated through peptide-proton cotransport) oftwolabelled dipeptides hasbeenstudied inapical membrane vesicles isolated fromratrenal cortex. Thesubstrates (neutral D-Phe-L-AlaExpand
Site-directed mutagenesis of Arginine282 suggests how protons and peptides are co-transported by rabbit PepT1
The mammalian proton-coupled peptide transporter PepT1 is the major route of uptake for dietary nitrogen, as well as the oral absorption of a number of drugs, including β-lactam antibiotics andExpand


Dipeptide transporters in apical and basolateral membranes of the human intestinal cell line Caco-2.
It is suggested not only that dipeptide transporters exist on both the apical and basolateral membranes of Caco-2 cells but also that the Basolateral dipePTide transporter is distinct from theApical H(+)-dipeptide cotransporter. Expand
Is intestinal peptide transport energized by a proton gradient?
Observations strongly suggest that peptides are cotransported with protons in the intestine, and it is very likely that this proton gradient is the in vivo energy source for the uphill transport of peptides. Expand
Proton-coupled transport of organic solutes in animal cell membranes and its relation to Na+ transport.
  • T. Hoshi
  • Chemistry, Medicine
  • The Japanese journal of physiology
  • 1985
In the intestinal and renal brush border membranes, transport of intact small peptides has been established to be cotransported with H+, which reveals a marked overshoot uptake when a sufficiently large proton gradient is imposed across the membrane. Expand
Dipeptide transport in brush-border membrane vesicles isolated from normal term human placenta.
These results demonstrate the presence of a dipeptide transport system in the human placenta for the first time, and many peptides inhibited the transport of glycylsarcosine whereas amino acids had no effect. Expand
Expression cloning of a mammalian proton-coupled oligopeptide transporter
The cloning and functional characterization of a H+-coupled transporter of oligopeptides and peptide-derived antibiotics from rabbit small intestine is reported, and the PepT1 primary structure is the first reported for a proton-Coupled organic solute transporter in vertebrates. Expand
Transepithelial transport of oral cephalosporins by monolayers of intestinal epithelial cell line Caco-2: specific transport systems in apical and basolateral membranes.
Findings suggest that p.o. cephalosporins accumulate in the Caco-2 cell monolayers via the H+/dipeptide cotransport system localized in the apical membranes and that a specific transport system is involved in the efflux of these antibiotics across the basolateral membranes. Expand
Dipeptide transport characteristics of the apical membrane of rat lung type II pneumocytes.
Findings strongly suggest the presence of a proton-coupled peptide transport protein in the apical surface of the type II cell, which may play a role in lung homeostasis. Expand
Dipeptide Transport Across Rat Alveolar Epithelial Cell Monolayers
The transepithelial transport and metabolism of two model peptides, glycyl-D-phenylalanine and Gly-L-Phe, across primary cultured monolayers of rat alveolar epithelial cells were studied and remained intact, as indicated by no appreciable changes in the bioelectric parameters of transe Pithelial potential difference and electrical resistance. Expand
Association of intestinal peptide transport with a protein related to the cadherin superfamily.
A monoclonal antibody that blocked uptake of cephalexin was used to identify and clone a gene that encodes an approximately 92-kilodalton membrane protein that was associated with the acquisition of peptide transport activity by transport-deficient cells. Expand
Transport of bestatin in rat renal brush-border membrane vesicles
Abstract Bestatin [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl- l -leucine] is a dipeptide, comprising l -leucine and an unusual β-ammo acid. We studied its transport mechanism in rat renalExpand