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H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1
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| Zeitschriftentitel: | American Journal of Physiology-Gastrointestinal and Liver Physiology |
|---|---|
| Personen und Körperschaften: | , , , , , , |
| In: | American Journal of Physiology-Gastrointestinal and Liver Physiology, 283, 2002, 1, S. G222-G229 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Physiological Society
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| Schlagwörter: |
| author_facet |
Knütter, Ilka Rubio-Aliaga, Isabel Boll, Michael Hause, Gerd Daniel, Hannelore Neubert, Klaus Brandsch, Matthias Knütter, Ilka Rubio-Aliaga, Isabel Boll, Michael Hause, Gerd Daniel, Hannelore Neubert, Klaus Brandsch, Matthias |
|---|---|
| author |
Knütter, Ilka Rubio-Aliaga, Isabel Boll, Michael Hause, Gerd Daniel, Hannelore Neubert, Klaus Brandsch, Matthias |
| spellingShingle |
Knütter, Ilka Rubio-Aliaga, Isabel Boll, Michael Hause, Gerd Daniel, Hannelore Neubert, Klaus Brandsch, Matthias American Journal of Physiology-Gastrointestinal and Liver Physiology H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 Physiology (medical) Gastroenterology Hepatology Physiology |
| author_sort |
knütter, ilka |
| spelling |
Knütter, Ilka Rubio-Aliaga, Isabel Boll, Michael Hause, Gerd Daniel, Hannelore Neubert, Klaus Brandsch, Matthias 0193-1857 1522-1547 American Physiological Society Physiology (medical) Gastroenterology Hepatology Physiology http://dx.doi.org/10.1152/ajpgi.00534.2001 <jats:p> This study describes for the first time the presence of H<jats:sup>+</jats:sup>-peptide cotransport in cells of the bile duct. Uptake of [glycine-1-<jats:sup>14</jats:sup>C]glycylsarcosine ([<jats:sup>14</jats:sup>C]Gly-Sar) in human extrahepatic cholangiocarcinoma SK-ChA-1 cells was stimulated sevenfold by an inwardly directed H<jats:sup>+</jats:sup> gradient. Transport was mediated by a low-affinity system with a transport constant ( K <jats:sub>t</jats:sub>) value of 1.1 mM. Several dipeptides, cefadroxil, and δ-aminolevulinic acid, but not glycine and glutathione, were strong inhibitors of Gly-Sar uptake. SK-ChA-1 cells formed tight, polarized monolayers on permeable membranes. The transepithelial electrical resistance was 856 ± 29 Ω × cm<jats:sup>2</jats:sup>. The transepithelial flux of [<jats:sup>14</jats:sup>C]Gly-Sar in apical-to-basolateral direction exceeded the basolateral-to-apical flux 11-fold. Uptake was 20-fold higher from the apical side. RT-PCR analysis using primer pairs specific for the intestinal-type peptide transporter (PEPT1) or kidney-type (PEPT2) revealed that the transport system expressed in SK-ChA-1 and also in cells of the native rabbit bile duct is PEPT1. Immunohistochemistry localized PEPT1 to the apical membrane of cholangiocytes of mouse extrahepatic biliary duct. We conclude that the cells of the mammalian extrahepatic biliary tract epithelium express the intestinal-type H<jats:sup>+</jats:sup>-peptide cotransporter in their apical membrane. SK-ChA-1 cells represent a convenient model to study the physiological and clinical aspects of peptide transport in cholangiocytes. </jats:p> H<sup>+</sup>-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 American Journal of Physiology-Gastrointestinal and Liver Physiology |
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| title |
H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 |
| title_unstemmed |
H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 |
| title_full |
H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 |
| title_fullStr |
H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 |
| title_full_unstemmed |
H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 |
| title_short |
H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 |
| title_sort |
h<sup>+</sup>-peptide cotransport in the human bile duct epithelium cell line sk-cha-1 |
| topic |
Physiology (medical) Gastroenterology Hepatology Physiology |
| url |
http://dx.doi.org/10.1152/ajpgi.00534.2001 |
| publishDate |
2002 |
| physical |
G222-G229 |
| description |
<jats:p> This study describes for the first time the presence of H<jats:sup>+</jats:sup>-peptide cotransport in cells of the bile duct. Uptake of [glycine-1-<jats:sup>14</jats:sup>C]glycylsarcosine ([<jats:sup>14</jats:sup>C]Gly-Sar) in human extrahepatic cholangiocarcinoma SK-ChA-1 cells was stimulated sevenfold by an inwardly directed H<jats:sup>+</jats:sup> gradient. Transport was mediated by a low-affinity system with a transport constant ( K <jats:sub>t</jats:sub>) value of 1.1 mM. Several dipeptides, cefadroxil, and δ-aminolevulinic acid, but not glycine and glutathione, were strong inhibitors of Gly-Sar uptake. SK-ChA-1 cells formed tight, polarized monolayers on permeable membranes. The transepithelial electrical resistance was 856 ± 29 Ω × cm<jats:sup>2</jats:sup>. The transepithelial flux of [<jats:sup>14</jats:sup>C]Gly-Sar in apical-to-basolateral direction exceeded the basolateral-to-apical flux 11-fold. Uptake was 20-fold higher from the apical side. RT-PCR analysis using primer pairs specific for the intestinal-type peptide transporter (PEPT1) or kidney-type (PEPT2) revealed that the transport system expressed in SK-ChA-1 and also in cells of the native rabbit bile duct is PEPT1. Immunohistochemistry localized PEPT1 to the apical membrane of cholangiocytes of mouse extrahepatic biliary duct. We conclude that the cells of the mammalian extrahepatic biliary tract epithelium express the intestinal-type H<jats:sup>+</jats:sup>-peptide cotransporter in their apical membrane. SK-ChA-1 cells represent a convenient model to study the physiological and clinical aspects of peptide transport in cholangiocytes. </jats:p> |
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| author | Knütter, Ilka, Rubio-Aliaga, Isabel, Boll, Michael, Hause, Gerd, Daniel, Hannelore, Neubert, Klaus, Brandsch, Matthias |
| author_facet | Knütter, Ilka, Rubio-Aliaga, Isabel, Boll, Michael, Hause, Gerd, Daniel, Hannelore, Neubert, Klaus, Brandsch, Matthias, Knütter, Ilka, Rubio-Aliaga, Isabel, Boll, Michael, Hause, Gerd, Daniel, Hannelore, Neubert, Klaus, Brandsch, Matthias |
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| description | <jats:p> This study describes for the first time the presence of H<jats:sup>+</jats:sup>-peptide cotransport in cells of the bile duct. Uptake of [glycine-1-<jats:sup>14</jats:sup>C]glycylsarcosine ([<jats:sup>14</jats:sup>C]Gly-Sar) in human extrahepatic cholangiocarcinoma SK-ChA-1 cells was stimulated sevenfold by an inwardly directed H<jats:sup>+</jats:sup> gradient. Transport was mediated by a low-affinity system with a transport constant ( K <jats:sub>t</jats:sub>) value of 1.1 mM. Several dipeptides, cefadroxil, and δ-aminolevulinic acid, but not glycine and glutathione, were strong inhibitors of Gly-Sar uptake. SK-ChA-1 cells formed tight, polarized monolayers on permeable membranes. The transepithelial electrical resistance was 856 ± 29 Ω × cm<jats:sup>2</jats:sup>. The transepithelial flux of [<jats:sup>14</jats:sup>C]Gly-Sar in apical-to-basolateral direction exceeded the basolateral-to-apical flux 11-fold. Uptake was 20-fold higher from the apical side. RT-PCR analysis using primer pairs specific for the intestinal-type peptide transporter (PEPT1) or kidney-type (PEPT2) revealed that the transport system expressed in SK-ChA-1 and also in cells of the native rabbit bile duct is PEPT1. Immunohistochemistry localized PEPT1 to the apical membrane of cholangiocytes of mouse extrahepatic biliary duct. We conclude that the cells of the mammalian extrahepatic biliary tract epithelium express the intestinal-type H<jats:sup>+</jats:sup>-peptide cotransporter in their apical membrane. SK-ChA-1 cells represent a convenient model to study the physiological and clinical aspects of peptide transport in cholangiocytes. </jats:p> |
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| imprint | American Physiological Society, 2002 |
| imprint_str_mv | American Physiological Society, 2002 |
| institution | DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275 |
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| series | American Journal of Physiology-Gastrointestinal and Liver Physiology |
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| spelling | Knütter, Ilka Rubio-Aliaga, Isabel Boll, Michael Hause, Gerd Daniel, Hannelore Neubert, Klaus Brandsch, Matthias 0193-1857 1522-1547 American Physiological Society Physiology (medical) Gastroenterology Hepatology Physiology http://dx.doi.org/10.1152/ajpgi.00534.2001 <jats:p> This study describes for the first time the presence of H<jats:sup>+</jats:sup>-peptide cotransport in cells of the bile duct. Uptake of [glycine-1-<jats:sup>14</jats:sup>C]glycylsarcosine ([<jats:sup>14</jats:sup>C]Gly-Sar) in human extrahepatic cholangiocarcinoma SK-ChA-1 cells was stimulated sevenfold by an inwardly directed H<jats:sup>+</jats:sup> gradient. Transport was mediated by a low-affinity system with a transport constant ( K <jats:sub>t</jats:sub>) value of 1.1 mM. Several dipeptides, cefadroxil, and δ-aminolevulinic acid, but not glycine and glutathione, were strong inhibitors of Gly-Sar uptake. SK-ChA-1 cells formed tight, polarized monolayers on permeable membranes. The transepithelial electrical resistance was 856 ± 29 Ω × cm<jats:sup>2</jats:sup>. The transepithelial flux of [<jats:sup>14</jats:sup>C]Gly-Sar in apical-to-basolateral direction exceeded the basolateral-to-apical flux 11-fold. Uptake was 20-fold higher from the apical side. RT-PCR analysis using primer pairs specific for the intestinal-type peptide transporter (PEPT1) or kidney-type (PEPT2) revealed that the transport system expressed in SK-ChA-1 and also in cells of the native rabbit bile duct is PEPT1. Immunohistochemistry localized PEPT1 to the apical membrane of cholangiocytes of mouse extrahepatic biliary duct. We conclude that the cells of the mammalian extrahepatic biliary tract epithelium express the intestinal-type H<jats:sup>+</jats:sup>-peptide cotransporter in their apical membrane. SK-ChA-1 cells represent a convenient model to study the physiological and clinical aspects of peptide transport in cholangiocytes. </jats:p> H<sup>+</sup>-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 American Journal of Physiology-Gastrointestinal and Liver Physiology |
| spellingShingle | Knütter, Ilka, Rubio-Aliaga, Isabel, Boll, Michael, Hause, Gerd, Daniel, Hannelore, Neubert, Klaus, Brandsch, Matthias, American Journal of Physiology-Gastrointestinal and Liver Physiology, H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1, Physiology (medical), Gastroenterology, Hepatology, Physiology |
| title | H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 |
| title_full | H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 |
| title_fullStr | H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 |
| title_full_unstemmed | H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 |
| title_short | H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 |
| title_sort | h<sup>+</sup>-peptide cotransport in the human bile duct epithelium cell line sk-cha-1 |
| title_unstemmed | H+-peptide cotransport in the human bile duct epithelium cell line SK-ChA-1 |
| topic | Physiology (medical), Gastroenterology, Hepatology, Physiology |
| url | http://dx.doi.org/10.1152/ajpgi.00534.2001 |