Cloning and Characterization of the Gene Encoding the Mouse Peptide Transporter PEPT2

Rubio‐Aliaga, Isabel; Boll, Michael; Daniel, Hannelore

doi:10.1006/bbrc.2000.3546

Cited by 52 publications

(41 citation statements)

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“…This region comprises 254 bp and contains an amino acid response-like element as found in the asparagine synthetase gene (32). Rat and mouse Pept1 and the murine Pept2 promoter regions contain these amino acid response-like elements with a bp substitution in the fifth bp (25,52). Whether these cis elements play a role in controlling gene expression in the kidney in response to cellular availability of free amino acids and dipeptides needs to be determined.…”

Section: Regulation Of Expression Level and Transport Activity Of Pepmentioning

confidence: 99%

“…38). The underlying proteins, differing in transport characteristics, now designated as PEPT1 (SLC15A1) and PEPT2 (SLC15A2), have been identified, and the corresponding genes have been cloned from a variety of species (10,24,25,39,41,(52)(53)(54). The transporters have been expressed in various cellular models, and information on structure, transport function, and regulation has been gathered by flux studies and electrophysiological techniques.…”

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confidence: 99%

“…Western blot analysis of protein preparations of intestine and kidney identified PEPT1 and PEPT2 immunoreactivity as glycosylated proteins with molecular masses of ϳ75 and 100 kDa, respectively (47,52). The Pept2 gene encodes a 729-amino acid protein (10,41,52,54) with 48% amino acid identity to PEPT1 predominantly in transmembrane domains (TMD) and the lowest identity in the large extracellular loop connecting TMD 9 and 10. The genomic organization of the peptide transporter genes has also been elucidated.…”

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confidence: 99%

“…The murine Pept1 gene is estimated to be ϳ38 kb long, including a TATA-less promoter region (25), and both murine and human Pept1 genes possess 23 exons and 22 introns (25,70). The murine Pept2 gene is 34 kb long, consists of 22 exons and 21 introns (52), and also carries a TATA-less promoter. The human Pept1 and Pept2 genes have been mapped to chromosomes 13q33-34 and 3q13.3-q21, respectively (39,51).…”

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confidence: 99%

“…The human Pept1 and Pept2 genes have been mapped to chromosomes 13q33-34 and 3q13.3-q21, respectively (39,51). The murine Pept2 gene was localized in a syntenic region with human chromosome 3q13.3-q21, on central mouse chromosome 16 close to D16Mit4 and D16Mit59 (52).…”

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An update on renal peptide transporters

Daniel

Rubio‐Aliaga

2003

American Journal of Physiology-Renal Physiology

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Daniel, Hannelore, and Isabel Rubio-Aliaga. An update on renal peptide transporters. Am J Physiol Renal Physiol 284: F885-F892, 2003; 10.1152/ajprenal.00123.2002The brush-border membrane of renal epithelial cells contains PEPT1 and PEPT2 proteins that are rheogenic carriers for short-chain peptides. The carrier proteins display a distinct surface expression pattern along the proximal tubule, suggesting that initially di-and tripeptides, either filtered or released by surface-bound hydrolases from larger oligopeptides, are taken up by the low-affinity but high-capacity PEPT1 transporter and then by PEPT2, which possesses a higher affinity but lower transport capacity. Both carriers transport essentially all possible di-and tripeptides and numerous structurally related drugs. A unique feature of the mammalian peptide transporters is the capability of proton-dependent electrogenic cotransport of all substrates, regardless of their charge, that is achieved by variable coupling in proton movement along with the substrate down the transmembrane potential difference. This review focuses on the postcloning research efforts to understand the molecular physiology of peptide transport processes in renal tubules and summarizes available data on the underlying genes, protein structures, and transporter function as derived from studies in heterologous expression systems. PEPT1; PEPT2; renal physiology; localization; functional analysis RENAL TUBULAR PEPTIDE TRANSPORT activity was originally discovered after intravenous infusion of the resistant dipeptide Gly-Sar in rats that resulted in a high accumulation of the intact dipeptide in renal tissue (1, 3). Studies with renal brush-border membrane vesicles established that renal apical peptide uptake was an electrogenic, proton-dependent uphill transport process for di-and tripeptides and related drugs mediated by two kinetically different systems (for a review, see Ref. 38). The underlying proteins, differing in transport characteristics, now designated as PEPT1 (SLC15A1) and PEPT2 (SLC15A2), have been identified, and the corresponding genes have been cloned from a variety of species (10,24,25,39,41,(52)(53)(54). The transporters have been expressed in various cellular models, and information on structure, transport function, and regulation has been gathered by flux studies and electrophysiological techniques. Expression analysis of transporter mRNA and protein by in situ hybridization and immunohistochemistry has extended our knowledge of tissue distribution, particularly the renal zonation of PEPT1 and PEPT2 surface expression. THE MOLECULAR ENTITIES OF APICAL PEPTIDE TRANSPORTPEPT1 and PEPT2 are polytopic integral membrane proteins with 12 predicted membrane-spanning domains and NH 2 -and COOH-terminal ends facing the cytosol. Transporter architecture and membrane topology have not been studied systematically, and therefore structural information is still mainly based on hydropathic analysis of amino acid sequences. The mammalian PEPT1 proteins comprise 701-710 amino acids, ...

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Section: Regulation Of Expression Level and Transport Activity Of Pepmentioning

confidence: 99%