RGD Reference Report - Cloning and characterization of a rat H+/peptide cotransporter mediating absorption of beta-lactam antibiotics in the intestine and kidney. - Rat Genome Database

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Cloning and characterization of a rat H+/peptide cotransporter mediating absorption of beta-lactam antibiotics in the intestine and kidney.

Authors: Saito, H  Okuda, M  Terada, T  Sasaki, S  Inui, K 
Citation: Saito H, etal., J Pharmacol Exp Ther 1995 Dec;275(3):1631-7.
RGD ID: 729908
Pubmed: PMID:8531138   (View Abstract at PubMed)

A complementary DNA (cDNA) encoding the rat H+/peptide cotransporter (PepT1) was isolated, and the transport characteristics of orally active beta-lactam antibiotics were assessed by measuring uptake into Xenopus oocytes expressing the rat PepT1. The rat PepT1 cDNA encoded a 710-amino acid protein with 77% identity to the rabbit PepT1. The message for rat PepT1 was approximately 2.9 kilobases and was found predominantly in the small intestine, whereas reverse transcription-polymerase chain reaction amplification revealed that the message was expressed both in the small intestine and in the kidney cortex. The 75-kDa protein was identified by translation of in vitro synthesized transcript of rat PepT1 cDNA by use of rabbit reticulocyte lysates and by Western blot analysis with a specific antibody against the rat PepT1. When expressed in Xenopus oocytes, rat PepT1 stimulated the uptake of ceftibuten (anion) and cephradine (zwitterion) in the presence of an inward H+ gradient, and the expressed uptake was inhibited by excess dipeptides. Kinetic analysis revealed that ceftibuten has 14-fold higher affinity for the rat PepT1 than cephradine. These findings suggest that the rat PepT1 mediates H(+)-coupled uphill transport of the oral beta-lactam antibiotics across the brush-border membranes of intestinal and renal proximal tubular cells.

Objects referenced in this article
Gene Slc15a1 solute carrier family 15 member 1 Rattus norvegicus

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