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4‐Aminomethylbenzoic acid is a non‐translocated competitive inhibitor of the epithelial peptide transporter PepT1
Author(s) -
Meredith D.,
Boyd C. A. R.,
Bronk J. R.,
Bailey P. D.,
Morgan K. M.,
Collier I. D.,
Temple C. S.
Publication year - 1998
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1111/j.1469-7793.1998.629bd.x
Subject(s) - peptide , xenopus , oligopeptide , transporter , efflux , dipeptide , brush border , vesicle , amino acid , biochemistry , biology , chemistry , microbiology and biotechnology , membrane , gene
1 4‐Aminomethylbenzoic acid, a molecule which mimics the spatial configuration of a dipeptide, competitively inhibits peptide influx in both Xenopus laevis oocytes expressing rabbit PepT1 and through PepT1 in rat renal brush border membrane vesicles. 2 This molecule is not translocated through PepT1 as measured both by direct HPLC analysis in PepT1‐expressing oocytes and indirectly by its failure to trans‐stimulate labelled peptide efflux through PepT1 in oocytes and in renal membrane vesicles. 3 However 4‐aminomethylbenzoic acid does reverse trans‐stimulation through expressed PepT1 of labelled peptide efflux induced by unlabelled peptide. Quantitatively this reversal is compatible with 4‐aminomethylbenzoic acid competitively binding to the external surface of PepT1. 4 4‐Aminomethylbenzoic acid (the first molecule discovered to be a non‐translocated competitive inhibitor of proton‐coupled oligopeptide transport) and its derivatives may thus be particularly useful as experimental tools.