PEPT1-mediated uptake of dipeptides enhances the intestinal absorption of amino acids via transport system b 0,+

Uwe Wenzel, Barbara Meissner, Frank Döring, Hannelore Daniel

Research output: Contribution to journalArticlepeer-review

40 Scopus citations

Abstract

Free amino acids and short chain peptides are the main digestion products of dietary proteins in the small intestine. Whether there is a direct interference in transport of both groups of degradation products is not known. We used human intestinal Caco-2 cells to investigate whether the absorption of dipeptides by the peptide transporter PEPT1 alters the apical uptake of free cationic and neutral amino acids. Influx of L-[ 3H]Arg into Caco-2 cells was Na +-independent and mediated mainly by the b 0,+ system recognizing both cationic and neutral amino acids. Preincubation of cells with 10 mM of selected neutral, mono- or dicationic dipeptides increased the influx of L-Arg up to fourfold. Preloading with equivalent concentrations of the corresponding free amino acids also increased L-Arg influx but dipeptides always proved to be more efficient. The observed trans-stimulation was found to be specific for cationic amino acids since transport of L-[ 3H]Ala remained unaffected. We here demonstrate for the first time a direct interplay in amino acid and peptide transport in intestinal cells that may selectively alter the kinetics of amino acid absorption.

Original languageEnglish
Pages (from-to)251-259
Number of pages9
JournalJournal of Cellular Physiology
Volume186
Issue number2
DOIs
StatePublished - 2001

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