TY - JOUR
AU - Hediger, Matthias A.
AB - 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.
TI - Expression cloning of a mammalian proton-coupled oligopeptide transporter
JF - Nature
DO - 10.1038/368563a0
DA - 1994-04-07
UR - https://www.deepdyve.com/lp/springer-journals/expression-cloning-of-a-mammalian-proton-coupled-oligopeptide-dm1GtTONMq
SP - 563
EP - 566
VL - 368
IS - 6471
DP - DeepDyve
ER -