Peptide transporters

Current Opinion in Nephrology and Hypertension

Volumn 5, Issue 5, 1996, Pages 395-400

  Ganapathy, Vadivel ^a   Leibach, Frederick H ^a  

^a MEDICAL COLLEGE OF GEORGIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

RECEPTOR;

ACTIVE TRANSPORT; HUMAN; NONHUMAN; PEPTIDE TRANSPORT; PRIORITY JOURNAL; REVIEW; TRANSPORT AND BINDING PHENOMENA;

EID: 0029854276     PISSN: 10624821     EISSN: None     Source Type: Journal    
DOI: 10.1097/00041552-199609000-00003     Document Type: Review

References (33)

1. Ganapathy V, Brandsch M, Leibach FH: Intestinal transport of amino acids and peptides. In Physiology of the gastrointestinal tract. Edited by Johnson LR. New York: Raven Press; 1994:1773-1794.
2. Meredith D, Boyd CAR: Oligopeptide transport by epithelial cells. J Membr Biol 1995, 145:1-12.
3. Leibach FH, Ganapathy V: Peptide transporters in the intestine and the kidney. Annu Rev Nutr 1996, 16:99-119.
4. +/peptide cotransporter: cloning, functional expression, and chromosomal localization. J Biol Chem 1995, 270:6456-6463. This paper describes the cloning and characterization of the human intestinal peptide transporter PEPT1. The cloned PEPT1 cDNA was functionally characterized by expressing the cDNA in HeLa cells using the vaccinia virus expression system. This study also provides information on the chromosomal localization of the PEPT1 gene.
5. Fei YJ, Kanai Y, Nussberger S, Ganapathy V, Leibach FH, Romero MF, Singh SK, Boron WF, Hediger MA: Expression cloning of a mammalian protein-coupled oligopeptide transporter. Nature 1994, 386:563-566.
6. Boll M, Markovich D, Weber WM, Korte H, Daniel H, Murer H: Expression cloning of a cDNA from rabbit small intestine related to proton-coupled transport of peptides, β-lactam antibiotics and ACE inhibitors. Pflugers Arch 1994, 429:146-149.
7. +/peptide cotransporter mediating absorption of β-lactam antibiotics in the intestine and kidney. J Pharmacol Exp Ther 1995, 275:1631-1637.
8. Miyamoto K, Shiraga T, Morita K, Yamamoto H, Haga H, Taketani Y, Tamai I, Sai Y, Tsuji A, Takeda E: Sequence and tissue distribution and development changes in rat intestinal oligopeptide transporter. Biochim Biophys Acta 1996, 1305:34-38.
9. +/peptide cotransporter family from human kidney. Biochim Biophys Acta 1995, 1235:461-466. This was the first report on the cloning of the proton-peptide cotransporter from the kidney (PEPT2). This paper provided direct evidence at the molecular level for the distinctive nature of the renal transport system.
10. Boll M, Herget M, Wagener M, Weber WM, Markovich D, Biber J, Clauss W, Murer H, Daniel H: Expression cloning and functional characterization of the kidney cortex high-affinity proton-coupled peptide transporter. Proc Natl Acad Sci U S A 1996, 93:284-289. This paper reports the cloning of the rabbit homolog of PEPT2. It also provides information on the interaction between peptidomimetic drugs and PEPT2, and on the electrical properties of PEPT2-mediated transport process.
11. Saito H, Terada T, Okuda M, Sasaki S, Inui KI: Molecular cloning and tissue distribution of rat peptide transporter PEPT2. Biochim Biophys Acta 1996, 1280:173-177. This paper describes the cloning and characterization of rat PEPT2.
12. Ramamoorthy S, Liu W, Ma YY, Yang-Feng TL, Ganapathy V, Leibach FH: Proton/peptide cotransporter (PEPT2) from human kidney: functional characterization and chromosomal localization. Biochim Biophys Acta 1995, 1240:1-4. This study provides direct evidence for a functional difference between PEPT1 and PEPT2. Functional characterization of human PEPT1 and human PEPT2 in parallel under identical experimental conditions reveals that PEPT1 is a low-affinity and PEPT2 a high-affinity transporter. This study also provides evidence for the interaction of PEPT1 and PEPT2 with not only natural peptides but also peptides consisting of zwitterionic, anionic or cationic amino acids. The chromosomal location of human PEPT2 is also described.
13. Ganapathy ME, Brandsch M, Prasad PD, Ganapathy V, Leibach FH: Differential recognition of β-lactam antibiotics by intestinal and renal peptide transporters, PEPT1 and PEPT2. J Biol Chem 1995, 270:25672-25677. With cultured cell lines of intestinal and renal origin which differentially express either PEPT1 or PEPT2, and with cloned human PEPT1 and PEPT2, this study provides evidence for marked differences between the two peptide transporters in the recognition of β-lactam antibiotics as substrates.
14. +-coupled oligopeptide transporter hPEPT1. J Biol Chem 1996, 271:5430-5437. This paper gave the first description of a detailed kinetic analysis of the PEPT1-mediated transport mechanism.
15. Temple CS, Bronk JR, Bailey PD, Boyd CAR: Substrate-charge dependence of stoichiometry shows membrane potential is the driving force for proton-peptide cotransporter in rat renal cortex. Pflugers Arch 1995, 430:825-829. This study produced interesting and intriguing results with regard to proton : peptide stoichiometry for the peptide transport process in rat renal brush-border membrane vesicles. The results demonstrate that the coupling ratio for the cotransported proton and peptide substrate varies depending on the net charge of the peptide.
16. Miyamoto Y, Ganapathy V, Leibach FH: Identification of histidyl and thiol groups at the active site of rabbit renal dipeptide transporter. J Biol Chem 1986, 261:16133-16140.
17. Kramer W, Girbig F, Petzoldt E, Leipe T: Inactivation of the intestinal uptake system for β-lactam antibiotics by diethylpyrocarbonate. Biochim Biophys Acta 1988, 943:288-296.
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19. Daniel H, Adibi SA: Selective effect of zinc on uphill transport of oligopeptides into kidney brush border membrane vesicles. FASEB J 1995, 9:1112-1117. This study shows that the trace elements zinc, manganese and copper selectively activate the renal proton-peptide cotransporter. Evidence is provided for the direct interaction between these metal ions and the transporter. It is hypothesized that zinc or a closely related transition metal may be an integral part of the proton-peptide cotransporter.
20. Jia L, Bonaventura C, Bonaventura J, Stamler JS: S-Nitrosohemoglobin: a dynamic activity of blood involved in vascular control. Nature 1996, 380:221-226. It is suggested in this paper that thiol-containing dipeptides such as cysteinylglycine play an important role in nitric oxide homeostasis by their ability to form S-nitroso derivatives. Because these S-nitroso dipeptides are likely to be as good substrates as the unmodified parent dipeptides for peptide transporters, it is possible that the peptide transporters may play a role in the delivery of nitric oxide across the plasma membrane into target cells.
21. Meredith D, Boyd CAR: Dipeptide transport characteristics of the apical membrane of rat lung type II pneumocytes. Am J Physiol 1995, 269:L137-L143.
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23. +/peptide cotransporter in rat digestive tract. Biochem Biophys Res Commun 1996, 220:848-852.
24. + cotransport system in the Caco-2 human colon carcinoma cell line. Biochem J 1994, 299:253-260.
25. +-peptide cotransport in Madin-Darby canine kidney cells: expression and calmodulin-dependent regulation. Am J Physiol 1995, 268:F391-F397.
26. +/peptide cotransporter. FASEB J 1995, 9:1489-1496. This was the first report on the identification of a renal cell line which expresses PEPT2, the predominant peptide transporter in the kidney. These cells (SKPT) were originally derived from rat proximal tubule and provide an excellent model for studies of PEPT2.
27. +/peptide cotransporter in the human intestinal cell line Caco-2 by cyclic AMP. Biochem Biophys Res Commun 1996, 218:461-465.
28. Erickson RH, Gum JR, Lindstrom MM, McKean D, Kim YS: Regional expression and dietary regulation of rat small intestinal peptide and amino acid transporter mRNAs. Biochem Biophys Res Commun 1995, 216:249-257. This study provides evidence for upregulation of PEPT1 expression in the rat small intestine by a high-protein diet. Interestingly, the adaptive response is found only in distal segments of the small intestine, even though PEPT1 is expressed along the entire small intestine.
29. Perry JR, Basrai MA, Steiner HY, Naider F, Becker JM: Isolation and characterization of a Saccharomyces cerevisiae peptide transporter gene. Mol Cell Biol 1994, 14:104-115.
30. Hagting A, Kunji ERS, Leenhouts KJ, Poolman B, Konings WN: The di- and tripeptide transport protein of Lactococcus lactis: a new type of bacterial peptide transporter. J Biol Chem 1994, 269:11391-11399.
31. Tsay Y, Schroeder JI, Feldmann KA, Crawford NM: The herbicide sensitivity gene CHL1 of Arabidopsis encodes a nitrate-inducible nitrate transporter. Cell 1993, 72:705-713.
32. Steiner HY, Song W, Zhang L, Naider F, Becker JM, Stacey G: An Arabidopsis peptide transporter is a member of a new class of membrane transport proteins. Plant Cell 1994, 6:1289-1299.
33. Rentsch D, Laloi M, Rouhara I, Schmelzer E, Delrot S, Frommer WB: NTR1 encodes a high affinity oligopeptide transporter in Arabidopsis. FEBS Lett 1995, 370:264-268.