An update on renal peptide transporters.

作者: Hannelore Daniel , Isabel Rubio-Aliaga

DOI: 10.1152/AJPRENAL.00123.2002

关键词: Cell biologyProtein structureOligopeptideTransporterTripeptideCotransporterBiochemistryPeptide transportHeterologous expressionChemistryPeptide

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.

参考文章(76)
Hideyuki Motohashi, Toshiya Katsura, Hideyuki Saito, Ken‐ichi Inui, Effects of tacrolimus and cyclosporin a on peptide transporter PEPT1 in caco-2 cells Pharmaceutical Research. ,vol. 18, pp. 713- 717 ,(2001) , 10.1023/A:1011006015593
Rong Liang, You-Jun Fei, Puttur D. Prasad, Sammanda Ramamoorthy, Hong Han, Teresa L. Yang-Feng, Matthias A. Hediger, Vadivel Ganapathy, Frederick H. Leibach, Human Intestinal H+/Peptide Cotransporter Journal of Biological Chemistry. ,vol. 270, pp. 6456- 6463 ,(1995) , 10.1074/JBC.270.12.6456
Siamak A. Adibi, Clearance of dipeptides from plasma: role of kidney and intestine. Ciba Foundation Symposium 50 - Peptide Transport and Hydrolysis. pp. 265- 286 ,(1977) , 10.1002/9780470720318.CH15
Glenn C. Turner, Fangyong Du, Alexander Varshavsky, Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway Nature. ,vol. 405, pp. 579- 583 ,(2000) , 10.1038/35014629
H Daniel, E.L. Morse, S.A. Adibi, Determinants of substrate affinity for the oligopeptide/H+ symporter in the renal brush border membrane. Journal of Biological Chemistry. ,vol. 267, pp. 9565- 9573 ,(1992) , 10.1016/S0021-9258(19)50128-4
David A. Groneberg, Monika Nickolaus, Jochen Springer, Frank Döring, Hannelore Daniel, Axel Fischer, Localization of the Peptide Transporter PEPT2 in the Lung The American Journal of Pathology. ,vol. 158, pp. 707- 714 ,(2001) , 10.1016/S0002-9440(10)64013-8
H Y Steiner, F Naider, J M Becker, J R Perry, M A Basrai, Isolation and characterization of a Saccharomyces cerevisiae peptide transport gene. Molecular and Cellular Biology. ,vol. 14, pp. 104- 115 ,(1994) , 10.1128/MCB.14.1.104
H. Minami, H. Daniel, E. L. Morse, S. A. Adibi, Oligopeptides: mechanism of renal clearance depends on molecular structure. American Journal of Physiology-renal Physiology. ,vol. 263, ,(1992) , 10.1152/AJPRENAL.1992.263.1.F109
Wei Liu, Rong Liang, Sammanda Ramamoorthy, You-Jun Fei, Malliga E. Ganapathy, Matthias A. Hediger, Vadivel Ganapathy, Frederick H. Leibach, Molecular cloning of PEPT 2, a new member of the H+/peptide cotransporter family, from human kidney Biochimica et Biophysica Acta. ,vol. 1235, pp. 461- 466 ,(1995) , 10.1016/0005-2736(95)80036-F