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

C S Temple; C A Boyd

doi:10.1016/s0005-2736(98)00093-5

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

Biochim Biophys Acta. 1998 Aug 14;1373(1):277-81. doi: 10.1016/s0005-2736(98)00093-5.

Authors

C S Temple¹, C A Boyd

Affiliation

¹ Department of Human Anatomy, University of Oxford, South Parks Road, Oxford OX1 3QX, UK. catherine.temple@anat.ox.ac.uk

PMID: 9733984
DOI: 10.1016/s0005-2736(98)00093-5

Abstract

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.

MeSH terms

Angiotensin-Converting Enzyme Inhibitors / pharmacology*
Animals
Biological Transport
Captopril / pharmacology*
Carrier Proteins / metabolism*
Dipeptides / metabolism
Enalapril / pharmacology*
Kidney Cortex / drug effects*
Kidney Cortex / metabolism
Kinetics
Microvilli / drug effects
Microvilli / metabolism
Peptide Transporter 1
Rats
Symporters*

Substances

Angiotensin-Converting Enzyme Inhibitors
Carrier Proteins
Dipeptides
Peptide Transporter 1
Slc15a1 protein, rat
Symporters
Enalapril
Captopril