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Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3)
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| Zeitschriftentitel: | American Journal of Physiology-Renal Physiology |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | American Journal of Physiology-Renal Physiology, 287, 2004, 4, S. F628-F638 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Physiological Society
|
| Schlagwörter: |
| author_facet |
Handlogten, Mary E. Hong, Seong-Pyo Westhoff, Connie M. Weiner, I. David Handlogten, Mary E. Hong, Seong-Pyo Westhoff, Connie M. Weiner, I. David |
|---|---|
| author |
Handlogten, Mary E. Hong, Seong-Pyo Westhoff, Connie M. Weiner, I. David |
| spellingShingle |
Handlogten, Mary E. Hong, Seong-Pyo Westhoff, Connie M. Weiner, I. David American Journal of Physiology-Renal Physiology Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) Physiology |
| author_sort |
handlogten, mary e. |
| spelling |
Handlogten, Mary E. Hong, Seong-Pyo Westhoff, Connie M. Weiner, I. David 1931-857X 1522-1466 American Physiological Society Physiology http://dx.doi.org/10.1152/ajprenal.00363.2003 <jats:p>The renal collecting duct is the primary site for the ammonia secretion necessary for acid-base homeostasis. Recent studies have identified the presence of putative ammonia transporters in the collecting duct, but whether the collecting duct has transporter-mediated ammonia transport is unknown. The purpose of this study was to examine basolateral ammonia transport in the mouse collecting duct cell (mIMCD-3). To examine mIMCD-3 basolateral ammonia transport, we used cells grown to confluence on permeable support membranes and quantified basolateral uptake of the radiolabeled ammonia analog [<jats:sup>14</jats:sup>C]methylammonia ([<jats:sup>14</jats:sup>C]MA). mIMCD-3 cell basolateral MA transport exhibited both diffusive and transporter-mediated components. Transporter-mediated uptake exhibited a K<jats:sub>m</jats:sub>for MA of 4.6 ± 0.2 mM, exceeded diffusive uptake at MA concentrations below 7.0 ± 1.8 mM, and was competitively inhibited by ammonia with a K<jats:sub>i</jats:sub>of 2.1 ± 0.6 mM. Transporter-mediated uptake was not altered by inhibitors of Na<jats:sup>+</jats:sup>-K<jats:sup>+</jats:sup>-ATPase, Na<jats:sup>+</jats:sup>-K<jats:sup>+</jats:sup>-2Cl<jats:sup>−</jats:sup>cotransporter, K<jats:sup>+</jats:sup>channels or KCC proteins, by excess potassium, by extracellular sodium or potassium removal or by varying membrane potential, suggesting the presence of a novel, electroneutral ammonia-MA transport mechanism. Increasing the outwardly directed transmembrane H<jats:sup>+</jats:sup>gradient increased transport activity by increasing V<jats:sub>max</jats:sub>. Finally, mIMCD-3 cells express mRNA and protein for the putative ammonia transporter Rh B-glycoprotein (RhBG), and they exhibit basolateral RhBG immunoreactivity. We conclude that mIMCD-3 cells express a basolateral electroneutral NH<jats:sub>4</jats:sub><jats:sup>+</jats:sup>/H<jats:sup>+</jats:sup>exchange activity that may be mediated by RhBG.</jats:p> Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) American Journal of Physiology-Renal Physiology |
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10.1152/ajprenal.00363.2003 |
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1931-857X 1522-1466 |
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2004 |
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American Physiological Society |
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American Journal of Physiology-Renal Physiology |
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| title |
Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) |
| title_unstemmed |
Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) |
| title_full |
Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) |
| title_fullStr |
Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) |
| title_full_unstemmed |
Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) |
| title_short |
Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) |
| title_sort |
basolateral ammonium transport by the mouse inner medullary collecting duct cell (mimcd-3) |
| topic |
Physiology |
| url |
http://dx.doi.org/10.1152/ajprenal.00363.2003 |
| publishDate |
2004 |
| physical |
F628-F638 |
| description |
<jats:p>The renal collecting duct is the primary site for the ammonia secretion necessary for acid-base homeostasis. Recent studies have identified the presence of putative ammonia transporters in the collecting duct, but whether the collecting duct has transporter-mediated ammonia transport is unknown. The purpose of this study was to examine basolateral ammonia transport in the mouse collecting duct cell (mIMCD-3). To examine mIMCD-3 basolateral ammonia transport, we used cells grown to confluence on permeable support membranes and quantified basolateral uptake of the radiolabeled ammonia analog [<jats:sup>14</jats:sup>C]methylammonia ([<jats:sup>14</jats:sup>C]MA). mIMCD-3 cell basolateral MA transport exhibited both diffusive and transporter-mediated components. Transporter-mediated uptake exhibited a K<jats:sub>m</jats:sub>for MA of 4.6 ± 0.2 mM, exceeded diffusive uptake at MA concentrations below 7.0 ± 1.8 mM, and was competitively inhibited by ammonia with a K<jats:sub>i</jats:sub>of 2.1 ± 0.6 mM. Transporter-mediated uptake was not altered by inhibitors of Na<jats:sup>+</jats:sup>-K<jats:sup>+</jats:sup>-ATPase, Na<jats:sup>+</jats:sup>-K<jats:sup>+</jats:sup>-2Cl<jats:sup>−</jats:sup>cotransporter, K<jats:sup>+</jats:sup>channels or KCC proteins, by excess potassium, by extracellular sodium or potassium removal or by varying membrane potential, suggesting the presence of a novel, electroneutral ammonia-MA transport mechanism. Increasing the outwardly directed transmembrane H<jats:sup>+</jats:sup>gradient increased transport activity by increasing V<jats:sub>max</jats:sub>. Finally, mIMCD-3 cells express mRNA and protein for the putative ammonia transporter Rh B-glycoprotein (RhBG), and they exhibit basolateral RhBG immunoreactivity. We conclude that mIMCD-3 cells express a basolateral electroneutral NH<jats:sub>4</jats:sub><jats:sup>+</jats:sup>/H<jats:sup>+</jats:sup>exchange activity that may be mediated by RhBG.</jats:p> |
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| author | Handlogten, Mary E., Hong, Seong-Pyo, Westhoff, Connie M., Weiner, I. David |
| author_facet | Handlogten, Mary E., Hong, Seong-Pyo, Westhoff, Connie M., Weiner, I. David, Handlogten, Mary E., Hong, Seong-Pyo, Westhoff, Connie M., Weiner, I. David |
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| description | <jats:p>The renal collecting duct is the primary site for the ammonia secretion necessary for acid-base homeostasis. Recent studies have identified the presence of putative ammonia transporters in the collecting duct, but whether the collecting duct has transporter-mediated ammonia transport is unknown. The purpose of this study was to examine basolateral ammonia transport in the mouse collecting duct cell (mIMCD-3). To examine mIMCD-3 basolateral ammonia transport, we used cells grown to confluence on permeable support membranes and quantified basolateral uptake of the radiolabeled ammonia analog [<jats:sup>14</jats:sup>C]methylammonia ([<jats:sup>14</jats:sup>C]MA). mIMCD-3 cell basolateral MA transport exhibited both diffusive and transporter-mediated components. Transporter-mediated uptake exhibited a K<jats:sub>m</jats:sub>for MA of 4.6 ± 0.2 mM, exceeded diffusive uptake at MA concentrations below 7.0 ± 1.8 mM, and was competitively inhibited by ammonia with a K<jats:sub>i</jats:sub>of 2.1 ± 0.6 mM. Transporter-mediated uptake was not altered by inhibitors of Na<jats:sup>+</jats:sup>-K<jats:sup>+</jats:sup>-ATPase, Na<jats:sup>+</jats:sup>-K<jats:sup>+</jats:sup>-2Cl<jats:sup>−</jats:sup>cotransporter, K<jats:sup>+</jats:sup>channels or KCC proteins, by excess potassium, by extracellular sodium or potassium removal or by varying membrane potential, suggesting the presence of a novel, electroneutral ammonia-MA transport mechanism. Increasing the outwardly directed transmembrane H<jats:sup>+</jats:sup>gradient increased transport activity by increasing V<jats:sub>max</jats:sub>. Finally, mIMCD-3 cells express mRNA and protein for the putative ammonia transporter Rh B-glycoprotein (RhBG), and they exhibit basolateral RhBG immunoreactivity. We conclude that mIMCD-3 cells express a basolateral electroneutral NH<jats:sub>4</jats:sub><jats:sup>+</jats:sup>/H<jats:sup>+</jats:sup>exchange activity that may be mediated by RhBG.</jats:p> |
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| imprint | American Physiological Society, 2004 |
| imprint_str_mv | American Physiological Society, 2004 |
| institution | DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161 |
| issn | 1931-857X, 1522-1466 |
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| language | English |
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| physical | F628-F638 |
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| publisher | American Physiological Society |
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| series | American Journal of Physiology-Renal Physiology |
| source_id | 49 |
| spelling | Handlogten, Mary E. Hong, Seong-Pyo Westhoff, Connie M. Weiner, I. David 1931-857X 1522-1466 American Physiological Society Physiology http://dx.doi.org/10.1152/ajprenal.00363.2003 <jats:p>The renal collecting duct is the primary site for the ammonia secretion necessary for acid-base homeostasis. Recent studies have identified the presence of putative ammonia transporters in the collecting duct, but whether the collecting duct has transporter-mediated ammonia transport is unknown. The purpose of this study was to examine basolateral ammonia transport in the mouse collecting duct cell (mIMCD-3). To examine mIMCD-3 basolateral ammonia transport, we used cells grown to confluence on permeable support membranes and quantified basolateral uptake of the radiolabeled ammonia analog [<jats:sup>14</jats:sup>C]methylammonia ([<jats:sup>14</jats:sup>C]MA). mIMCD-3 cell basolateral MA transport exhibited both diffusive and transporter-mediated components. Transporter-mediated uptake exhibited a K<jats:sub>m</jats:sub>for MA of 4.6 ± 0.2 mM, exceeded diffusive uptake at MA concentrations below 7.0 ± 1.8 mM, and was competitively inhibited by ammonia with a K<jats:sub>i</jats:sub>of 2.1 ± 0.6 mM. Transporter-mediated uptake was not altered by inhibitors of Na<jats:sup>+</jats:sup>-K<jats:sup>+</jats:sup>-ATPase, Na<jats:sup>+</jats:sup>-K<jats:sup>+</jats:sup>-2Cl<jats:sup>−</jats:sup>cotransporter, K<jats:sup>+</jats:sup>channels or KCC proteins, by excess potassium, by extracellular sodium or potassium removal or by varying membrane potential, suggesting the presence of a novel, electroneutral ammonia-MA transport mechanism. Increasing the outwardly directed transmembrane H<jats:sup>+</jats:sup>gradient increased transport activity by increasing V<jats:sub>max</jats:sub>. Finally, mIMCD-3 cells express mRNA and protein for the putative ammonia transporter Rh B-glycoprotein (RhBG), and they exhibit basolateral RhBG immunoreactivity. We conclude that mIMCD-3 cells express a basolateral electroneutral NH<jats:sub>4</jats:sub><jats:sup>+</jats:sup>/H<jats:sup>+</jats:sup>exchange activity that may be mediated by RhBG.</jats:p> Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) American Journal of Physiology-Renal Physiology |
| spellingShingle | Handlogten, Mary E., Hong, Seong-Pyo, Westhoff, Connie M., Weiner, I. David, American Journal of Physiology-Renal Physiology, Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3), Physiology |
| title | Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) |
| title_full | Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) |
| title_fullStr | Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) |
| title_full_unstemmed | Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) |
| title_short | Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) |
| title_sort | basolateral ammonium transport by the mouse inner medullary collecting duct cell (mimcd-3) |
| title_unstemmed | Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3) |
| topic | Physiology |
| url | http://dx.doi.org/10.1152/ajprenal.00363.2003 |