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Am J Physiol Renal Physiol 284: F885-F892, 2003; doi:10.1152/ajprenal.00123.2002
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Vol. 284, Issue 5, F885-F892, May 2003

INVITED REVIEW
An update on renal peptide transporters

Hannelore Daniel and Isabel Rubio-Aliaga

Molecular Nutrition Unit, Technical University of Munich, D-85350 Freising-Weihenstephan, Germany

The brush-border membrane of renal epithelial cells contains PEPT1 and PEPT2 proteins that are rheogenic carriers for short-chain peptides. The carrier proteins display a distinct surface expression pattern along the proximal tubule, suggesting that initially di- and tripeptides, either filtered or released by surface-bound hydrolases from larger oligopeptides, are taken up by the low-affinity but high-capacity PEPT1 transporter and then by PEPT2, which possesses a higher affinity but lower transport capacity. Both carriers transport essentially all possible di- and tripeptides and numerous structurally related drugs. A unique feature of the mammalian peptide transporters is the capability of proton-dependent electrogenic cotransport of all substrates, regardless of their charge, that is achieved by variable coupling in proton movement along with the substrate down the transmembrane potential difference. This review focuses on the postcloning research efforts to understand the molecular physiology of peptide transport processes in renal tubules and summarizes available data on the underlying genes, protein structures, and transporter function as derived from studies in heterologous expression systems.

PEPT1; PEPT2; renal physiology; localization; functional analysis


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