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.
We demonstrate that the angiotensin-converting enzyme inhibitors enalapril and captopril inhibit the transport of D-Phe-L-Gln into PepT1-expressing Xenopus oocytes and into rat renal cortical brush border membrane vesicles (BBMV). The kinetics of inhibition are competitive. Enalapril and captopril are not substrates for PepT2 (Boll et al., Proc. Natl. Acad. Sci. 93 (1996) 284-289). Therefore we conclude that in rat renal cortical BBMV this neutral dipeptide is transported via PepT1.
Temple
C S
CS
Department of Human Anatomy, University of Oxford, South Parks Road, Oxford OX1 3QX, UK. catherine.temple@anat.ox.ac.uk
Boyd
C A
CA
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000494:pharmacology*; D000818:Animals; D001692:Biological Transport; D002216:Captopril / Q000494:pharmacology*; D002352:Carrier Proteins / Q000378:metabolism*; D004151:Dipeptides / Q000378:metabolism; D004656:Enalapril / Q000494:pharmacology*; D007672:Kidney Cortex / Q000187:drug effects* / Q000378:metabolism; D007700:Kinetics; D008871:Microvilli / Q000187:drug effects / Q000378:metabolism; D000074011:Peptide Transporter 1; D051381:Rats; D027981:Symporters
D000806:Angiotensin-Converting Enzyme Inhibitors; D002352:Carrier Proteins; D004151:Dipeptides; D000074011:Peptide Transporter 1; C489940:Slc15a1 protein, rat; D027981:Symporters; D004656:Enalapril; D002216:Captopril