Transport of L-proline, L-proline-containing peptides and related drugs at mammalian epithelial cell membranes

Amino Acids
M Brandsch

Abstract

Membrane transport of L-proline has received considerable attention in basic and pharmaceutical research recently. Of the most recently cloned members of the solute carrier family, two are "proline transporters". The amino acid transporter PAT1, expressed in intestine, kidney, brain and other organs, mediates the uptake of proline and derivatives in a pH gradient-dependent manner. The Na(+)-dependent proline transporter SIT1, cloned in 2005, exhibits the properties of the long-sought classical IMINO system. Proline-containing peptides are of interest for several reasons. Many biologically important peptide sequences contain highly conserved proline residues. Xaa-Pro peptides are very often resistant to enzymatic hydrolysis and display, in contrast to Pro-Xaa peptides, a high affinity to the H(+)/peptide cotransporter PEPT1 which is expressed in intestinal, renal, lung and biliary duct epithelial cells. Furthermore, several orally available drugs are recognized by PEPT1 as Xaa-Pro analogues due to their sterical resemblance to small peptides.

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Citations

Apr 18, 2008·The Journal of Pharmacy and Pharmacology·Matthias BrandschEva Bosse-Doenecke
Jun 8, 2007·Journal of Peptide Science : an Official Publication of the European Peptide Society·Misako Aito-InoueYoshinori Mine
Jan 31, 2008·Biochimica Et Biophysica Acta·Linda MetznerMatthias Brandsch
Sep 25, 2017·Antioxidants & Redox Signaling·Zhenlong WuGuoyao Wu
Jan 8, 2011·ACS Medicinal Chemistry Letters·Sam Y HongHarinath Chakrapani
Nov 22, 2017·ACS Applied Materials & Interfaces·Jing YangLei Zhang
Mar 20, 2020·Journal of Medicinal Chemistry·Deepak BhattaraiKyung Bo Kim

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