Expression cloning of a mammalian proton-coupled oligopeptide transporter

You Jun Fei, Yoshikatsu Kanai, Stephan Nussberger, Vadivel Ganapathy, Frederick H. Leibach, Michael F. Romero, Satish K. Singh, Walter F. Boron, Matthias A. Hediger

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Abstract

IN mammals, active transport of organic solutes across plasma membranes was thought to be primarily driven by the Na+ gradient1-3. Here we report the cloning and functional characterization of a H +-coupled transporter of oligopeptides and peptide-derived antibiotics from rabbit small intestine. This new protein, named PepT1, displays an unusually broad substrate specificity. PepT1-mediated uptake is electrogenic, independent of extracellular Na+, K+ and Cl-, and of membrane potential. PepT1 messenger RNA was found in intestine, kidney and liver and in small amounts in brain. In the intestine, the PepTl pathway constitutes a major mechanism for absorption of the products of protein digestion. To our knowledge, the PepT1 primary structure is the first reported for a proton-coupled organic solute transporter in vertebrates and represents an interesting evolutionary link between prokaryotic H +-coupled and vertebrate Na+-coupled transporters of organic solutes.

Original languageEnglish (US)
Pages (from-to)563-566
Number of pages4
JournalNature
Volume368
Issue number6471
DOIs
StatePublished - Jan 1 1994

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Fei, Y. J., Kanai, Y., Nussberger, S., Ganapathy, V., Leibach, F. H., Romero, M. F., Singh, S. K., Boron, W. F., & Hediger, M. A. (1994). Expression cloning of a mammalian proton-coupled oligopeptide transporter. Nature, 368(6471), 563-566. https://doi.org/10.1038/368563a0