作者: Hannelore Daniel , Isabel Rubio-Aliaga
DOI: 10.1152/AJPRENAL.00123.2002
关键词: Cell biology 、 Protein structure 、 Oligopeptide 、 Transporter 、 Tripeptide 、 Cotransporter 、 Biochemistry 、 Peptide transport 、 Heterologous expression 、 Chemistry 、 Peptide
摘要: The brush-border membrane of renal epithelial cells contains PEPT1 and PEPT2 proteins that are rheogenic carriers for short-chain peptides. carrier display a distinct surface expression pattern along the proximal tubule, suggesting initially di- tripeptides, either filtered or released by surface-bound hydrolases from larger oligopeptides, taken up low-affinity but high-capacity transporter then PEPT2, which possesses higher affinity lower transport capacity. Both essentially all possible tripeptides numerous structurally related drugs. A unique feature mammalian peptide transporters is capability proton-dependent electrogenic cotransport substrates, regardless their charge, achieved variable coupling in proton movement with substrate down transmembrane potential difference. This review focuses on postcloning research efforts to understand molecular physiology processes tubules summarizes available data underlying genes, protein structures, function as derived studies heterologous systems.