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Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells
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| Zeitschriftentitel: | American Journal of Physiology-Cell Physiology |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | American Journal of Physiology-Cell Physiology, 275, 1998, 6, S. C1573-C1579 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Physiological Society
|
| Schlagwörter: |
| author_facet |
Wenzel, Uwe Diehl, Daniela Herget, Martina Daniel, Hannelore Wenzel, Uwe Diehl, Daniela Herget, Martina Daniel, Hannelore |
|---|---|
| author |
Wenzel, Uwe Diehl, Daniela Herget, Martina Daniel, Hannelore |
| spellingShingle |
Wenzel, Uwe Diehl, Daniela Herget, Martina Daniel, Hannelore American Journal of Physiology-Cell Physiology Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells Cell Biology Physiology |
| author_sort |
wenzel, uwe |
| spelling |
Wenzel, Uwe Diehl, Daniela Herget, Martina Daniel, Hannelore 0363-6143 1522-1563 American Physiological Society Cell Biology Physiology http://dx.doi.org/10.1152/ajpcell.1998.275.6.c1573 <jats:p>The reabsorption of filtered di- and tripeptides as well as certain peptide mimetics from the tubular lumen into renal epithelial cells is mediated by an H<jats:sup>+</jats:sup>-coupled high-affinity transport process. Here we demonstrate for the first time H<jats:sup>+</jats:sup>-coupled uptake of dipeptides into the renal proximal tubule cell line LLC-PK<jats:sub>1</jats:sub>. Transport was assessed 1) by uptake studies using the radiolabeled dipeptided-[<jats:sup>3</jats:sup>H]Phe-l-Ala, 2) by cellular accumulation of the fluorescent dipeptided-Ala-Lys-AMCA, and 3) by measurement of intracellular pH (pH<jats:sub>i</jats:sub>) changes as a consequence of H<jats:sup>+</jats:sup>-coupled dipeptide transport. Uptake ofd-Phe-l-Ala increased linearly over 11 days postconfluency and showed all the characteristics of the kidney cortex high-affinity peptide transporter, e.g., a pH optimum for transport ofd-Phe-l-Ala of 6.0, an apparent K<jats:sub>m</jats:sub>value for influx of 25.8 ± 3.6 μM, and affinities of differently charged dipeptides or the β-lactam antibiotic cefadroxil to the binding site in the range of 20–80 μM. pH<jats:sub>i</jats:sub>measurements established the peptide transporter to induce pronounced intracellular acidification in LLC-PK<jats:sub>1</jats:sub>cells and confirm its postulated role as a cellular acid loader.</jats:p> Endogenous expression of the renal high-affinity H<sup>+</sup>-peptide cotransporter in LLC-PK<sub>1</sub>cells American Journal of Physiology-Cell Physiology |
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10.1152/ajpcell.1998.275.6.c1573 |
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Biologie |
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American Physiological Society, 1998 |
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American Physiological Society, 1998 |
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0363-6143 1522-1563 |
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wenzel1998endogenousexpressionoftherenalhighaffinityhpeptidecotransporterinllcpk1cells |
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1998 |
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American Physiological Society |
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American Journal of Physiology-Cell Physiology |
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49 |
| title |
Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells |
| title_unstemmed |
Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells |
| title_full |
Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells |
| title_fullStr |
Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells |
| title_full_unstemmed |
Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells |
| title_short |
Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells |
| title_sort |
endogenous expression of the renal high-affinity h<sup>+</sup>-peptide cotransporter in llc-pk<sub>1</sub>cells |
| topic |
Cell Biology Physiology |
| url |
http://dx.doi.org/10.1152/ajpcell.1998.275.6.c1573 |
| publishDate |
1998 |
| physical |
C1573-C1579 |
| description |
<jats:p>The reabsorption of filtered di- and tripeptides as well as certain peptide mimetics from the tubular lumen into renal epithelial cells is mediated by an H<jats:sup>+</jats:sup>-coupled high-affinity transport process. Here we demonstrate for the first time H<jats:sup>+</jats:sup>-coupled uptake of dipeptides into the renal proximal tubule cell line LLC-PK<jats:sub>1</jats:sub>. Transport was assessed 1) by uptake studies using the radiolabeled dipeptided-[<jats:sup>3</jats:sup>H]Phe-l-Ala, 2) by cellular accumulation of the fluorescent dipeptided-Ala-Lys-AMCA, and 3) by measurement of intracellular pH (pH<jats:sub>i</jats:sub>) changes as a consequence of H<jats:sup>+</jats:sup>-coupled dipeptide transport. Uptake ofd-Phe-l-Ala increased linearly over 11 days postconfluency and showed all the characteristics of the kidney cortex high-affinity peptide transporter, e.g., a pH optimum for transport ofd-Phe-l-Ala of 6.0, an apparent K<jats:sub>m</jats:sub>value for influx of 25.8 ± 3.6 μM, and affinities of differently charged dipeptides or the β-lactam antibiotic cefadroxil to the binding site in the range of 20–80 μM. pH<jats:sub>i</jats:sub>measurements established the peptide transporter to induce pronounced intracellular acidification in LLC-PK<jats:sub>1</jats:sub>cells and confirm its postulated role as a cellular acid loader.</jats:p> |
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| author | Wenzel, Uwe, Diehl, Daniela, Herget, Martina, Daniel, Hannelore |
| author_facet | Wenzel, Uwe, Diehl, Daniela, Herget, Martina, Daniel, Hannelore, Wenzel, Uwe, Diehl, Daniela, Herget, Martina, Daniel, Hannelore |
| author_sort | wenzel, uwe |
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| container_title | American Journal of Physiology-Cell Physiology |
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| description | <jats:p>The reabsorption of filtered di- and tripeptides as well as certain peptide mimetics from the tubular lumen into renal epithelial cells is mediated by an H<jats:sup>+</jats:sup>-coupled high-affinity transport process. Here we demonstrate for the first time H<jats:sup>+</jats:sup>-coupled uptake of dipeptides into the renal proximal tubule cell line LLC-PK<jats:sub>1</jats:sub>. Transport was assessed 1) by uptake studies using the radiolabeled dipeptided-[<jats:sup>3</jats:sup>H]Phe-l-Ala, 2) by cellular accumulation of the fluorescent dipeptided-Ala-Lys-AMCA, and 3) by measurement of intracellular pH (pH<jats:sub>i</jats:sub>) changes as a consequence of H<jats:sup>+</jats:sup>-coupled dipeptide transport. Uptake ofd-Phe-l-Ala increased linearly over 11 days postconfluency and showed all the characteristics of the kidney cortex high-affinity peptide transporter, e.g., a pH optimum for transport ofd-Phe-l-Ala of 6.0, an apparent K<jats:sub>m</jats:sub>value for influx of 25.8 ± 3.6 μM, and affinities of differently charged dipeptides or the β-lactam antibiotic cefadroxil to the binding site in the range of 20–80 μM. pH<jats:sub>i</jats:sub>measurements established the peptide transporter to induce pronounced intracellular acidification in LLC-PK<jats:sub>1</jats:sub>cells and confirm its postulated role as a cellular acid loader.</jats:p> |
| doi_str_mv | 10.1152/ajpcell.1998.275.6.c1573 |
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| imprint | American Physiological Society, 1998 |
| imprint_str_mv | American Physiological Society, 1998 |
| institution | DE-15, DE-Rs1, DE-Pl11, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4 |
| issn | 0363-6143, 1522-1563 |
| issn_str_mv | 0363-6143, 1522-1563 |
| language | English |
| last_indexed | 2024-03-01T15:29:27.574Z |
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| physical | C1573-C1579 |
| publishDate | 1998 |
| publishDateSort | 1998 |
| publisher | American Physiological Society |
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| recordtype | ai |
| series | American Journal of Physiology-Cell Physiology |
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| spelling | Wenzel, Uwe Diehl, Daniela Herget, Martina Daniel, Hannelore 0363-6143 1522-1563 American Physiological Society Cell Biology Physiology http://dx.doi.org/10.1152/ajpcell.1998.275.6.c1573 <jats:p>The reabsorption of filtered di- and tripeptides as well as certain peptide mimetics from the tubular lumen into renal epithelial cells is mediated by an H<jats:sup>+</jats:sup>-coupled high-affinity transport process. Here we demonstrate for the first time H<jats:sup>+</jats:sup>-coupled uptake of dipeptides into the renal proximal tubule cell line LLC-PK<jats:sub>1</jats:sub>. Transport was assessed 1) by uptake studies using the radiolabeled dipeptided-[<jats:sup>3</jats:sup>H]Phe-l-Ala, 2) by cellular accumulation of the fluorescent dipeptided-Ala-Lys-AMCA, and 3) by measurement of intracellular pH (pH<jats:sub>i</jats:sub>) changes as a consequence of H<jats:sup>+</jats:sup>-coupled dipeptide transport. Uptake ofd-Phe-l-Ala increased linearly over 11 days postconfluency and showed all the characteristics of the kidney cortex high-affinity peptide transporter, e.g., a pH optimum for transport ofd-Phe-l-Ala of 6.0, an apparent K<jats:sub>m</jats:sub>value for influx of 25.8 ± 3.6 μM, and affinities of differently charged dipeptides or the β-lactam antibiotic cefadroxil to the binding site in the range of 20–80 μM. pH<jats:sub>i</jats:sub>measurements established the peptide transporter to induce pronounced intracellular acidification in LLC-PK<jats:sub>1</jats:sub>cells and confirm its postulated role as a cellular acid loader.</jats:p> Endogenous expression of the renal high-affinity H<sup>+</sup>-peptide cotransporter in LLC-PK<sub>1</sub>cells American Journal of Physiology-Cell Physiology |
| spellingShingle | Wenzel, Uwe, Diehl, Daniela, Herget, Martina, Daniel, Hannelore, American Journal of Physiology-Cell Physiology, Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells, Cell Biology, Physiology |
| title | Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells |
| title_full | Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells |
| title_fullStr | Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells |
| title_full_unstemmed | Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells |
| title_short | Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells |
| title_sort | endogenous expression of the renal high-affinity h<sup>+</sup>-peptide cotransporter in llc-pk<sub>1</sub>cells |
| title_unstemmed | Endogenous expression of the renal high-affinity H+-peptide cotransporter in LLC-PK1cells |
| topic | Cell Biology, Physiology |
| url | http://dx.doi.org/10.1152/ajpcell.1998.275.6.c1573 |