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An update on renal peptide transporters
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| Zeitschriftentitel: | American Journal of Physiology-Renal Physiology |
|---|---|
| Personen und Körperschaften: | , |
| In: | American Journal of Physiology-Renal Physiology, 284, 2003, 5, S. F885-F892 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Physiological Society
|
| Schlagwörter: |
| author_facet |
Daniel, Hannelore Rubio-Aliaga, Isabel Daniel, Hannelore Rubio-Aliaga, Isabel |
|---|---|
| author |
Daniel, Hannelore Rubio-Aliaga, Isabel |
| spellingShingle |
Daniel, Hannelore Rubio-Aliaga, Isabel American Journal of Physiology-Renal Physiology An update on renal peptide transporters Physiology |
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daniel, hannelore |
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Daniel, Hannelore Rubio-Aliaga, Isabel 1931-857X 1522-1466 American Physiological Society Physiology http://dx.doi.org/10.1152/ajprenal.00123.2002 <jats:p>The 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.</jats:p> An update on renal peptide transporters American Journal of Physiology-Renal Physiology |
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American Physiological Society, 2003 |
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American Journal of Physiology-Renal Physiology |
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| title |
An update on renal peptide transporters |
| title_unstemmed |
An update on renal peptide transporters |
| title_full |
An update on renal peptide transporters |
| title_fullStr |
An update on renal peptide transporters |
| title_full_unstemmed |
An update on renal peptide transporters |
| title_short |
An update on renal peptide transporters |
| title_sort |
an update on renal peptide transporters |
| topic |
Physiology |
| url |
http://dx.doi.org/10.1152/ajprenal.00123.2002 |
| publishDate |
2003 |
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F885-F892 |
| description |
<jats:p>The 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.</jats:p> |
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| author | Daniel, Hannelore, Rubio-Aliaga, Isabel |
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| description | <jats:p>The 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.</jats:p> |
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| series | American Journal of Physiology-Renal Physiology |
| source_id | 49 |
| spelling | Daniel, Hannelore Rubio-Aliaga, Isabel 1931-857X 1522-1466 American Physiological Society Physiology http://dx.doi.org/10.1152/ajprenal.00123.2002 <jats:p>The 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.</jats:p> An update on renal peptide transporters American Journal of Physiology-Renal Physiology |
| spellingShingle | Daniel, Hannelore, Rubio-Aliaga, Isabel, American Journal of Physiology-Renal Physiology, An update on renal peptide transporters, Physiology |
| title | An update on renal peptide transporters |
| title_full | An update on renal peptide transporters |
| title_fullStr | An update on renal peptide transporters |
| title_full_unstemmed | An update on renal peptide transporters |
| title_short | An update on renal peptide transporters |
| title_sort | an update on renal peptide transporters |
| title_unstemmed | An update on renal peptide transporters |
| topic | Physiology |
| url | http://dx.doi.org/10.1152/ajprenal.00123.2002 |