Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
4-aminomethylbenzoic acid is a non-translocated competitive inhibitor of the epithelial peptide transporter PepT1.
Meredith D
,
Boyd CA
,
Bronk JR
,
Bailey PD
,
Morgan KM
,
Collier ID
,
Temple CS
.
???displayArticle.abstract???
1. 4-Aminomethylbenzoic acid, a molecule which mimics the special 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-exp ressing oocytes and indirectly by its failure to trans-stimulate labelle d peptide efflux through PepT1 in oocytes and in renal membrane vessicle s. 3. However 4-aminiomethylbenzoic acid does reverse trans-stimulation through expressed PepT1 of labelled peptid efflux induced by unlabelled peptide. Quantitatively this reversal is compatible with 4-aminomethyl benzoic 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.
Biber,
A high yield preparation for rat kidney brush border membranes. Different behaviour of lysosomal markers.
1981, Pubmed
Biber,
A high yield preparation for rat kidney brush border membranes. Different behaviour of lysosomal markers.
1981,
Pubmed
Daniel,
Determinants of substrate affinity for the oligopeptide/H+ symporter in the renal brush border membrane.
1992,
Pubmed
Daniel,
First insights into the operational mode of epithelial peptide transporters.
1997,
Pubmed
Deves,
The determination of kinetic parameters for carrier-mediated transport of non-labelled substrate analogues: a general method applied to the study of divalent anion transport in placental membrane vesicles.
1989,
Pubmed
Devés,
The binding and translocation steps in transport as related to substrate structure. A study of the choline carrier of erythrocytes.
1979,
Pubmed
Fei,
Expression cloning of a mammalian proton-coupled oligopeptide transporter.
1994,
Pubmed
,
Xenbase
Fei,
Molecular and structural features of the proton-coupled oligopeptide transporter superfamily.
1998,
Pubmed
Hediger,
Molecular physiology of sodium-glucose cotransporters.
1994,
Pubmed
Lister,
Dipeptide transport and hydrolysis in isolated loops of rat small intestine: effects of stereospecificity.
1995,
Pubmed
Meredith,
4-aminomethylbenzoic acid is a non-translocated competitive inhibitor of the epithelial peptide transporter PepT1.
1998,
Pubmed
,
Xenbase
Steel,
Stoichiometry and pH dependence of the rabbit proton-dependent oligopeptide transporter PepT1.
1997,
Pubmed
,
Xenbase
Temple,
Substrate-charge dependence of stoichiometry shows membrane potential is the driving force for proton-peptide cotransport in rat renal cortex.
1995,
Pubmed
Temple,
A model for the kinetics of neutral and anionic dipeptide-proton cotransport by the apical membrane of rat kidney cortex.
1996,
Pubmed
Temple,
Peptide mimics as substrates for the intestinal peptide transporter.
1998,
Pubmed
,
Xenbase
Temple,
Proton-coupled oligopeptide transport by rat renal cortical brush border membrane vesicles: a functional analysis using ACE inhibitors to determine the isoform of the transporter.
1998,
Pubmed
,
Xenbase
