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The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function
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| Zeitschriftentitel: | American Journal of Physiology-Cell Physiology |
|---|---|
| Personen und Körperschaften: | , , , , , , , , |
| In: | American Journal of Physiology-Cell Physiology, 298, 2010, 5, S. C1057-C1065 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Physiological Society
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| Schlagwörter: |
| author_facet |
Singh, Anurag Kumar Riederer, Brigitte Chen, Mingmin Xiao, Fang Krabbenhöft, Anja Engelhardt, Regina Nylander, Olof Soleimani, Manoocher Seidler, Ursula Singh, Anurag Kumar Riederer, Brigitte Chen, Mingmin Xiao, Fang Krabbenhöft, Anja Engelhardt, Regina Nylander, Olof Soleimani, Manoocher Seidler, Ursula |
|---|---|
| author |
Singh, Anurag Kumar Riederer, Brigitte Chen, Mingmin Xiao, Fang Krabbenhöft, Anja Engelhardt, Regina Nylander, Olof Soleimani, Manoocher Seidler, Ursula |
| spellingShingle |
Singh, Anurag Kumar Riederer, Brigitte Chen, Mingmin Xiao, Fang Krabbenhöft, Anja Engelhardt, Regina Nylander, Olof Soleimani, Manoocher Seidler, Ursula American Journal of Physiology-Cell Physiology The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function Cell Biology Physiology |
| author_sort |
singh, anurag kumar |
| spelling |
Singh, Anurag Kumar Riederer, Brigitte Chen, Mingmin Xiao, Fang Krabbenhöft, Anja Engelhardt, Regina Nylander, Olof Soleimani, Manoocher Seidler, Ursula 0363-6143 1522-1563 American Physiological Society Cell Biology Physiology http://dx.doi.org/10.1152/ajpcell.00454.2009 <jats:p>CFTR has been recognized to function as both an anion channel and a key regulator of Slc26 anion transporters in heterologous expression systems. Whether this regulatory relationship between CFTR and Slc26 transporters is seen in native intestine, and whether this effect is coupled to CFTR transport function or other features of this protein, has not been studied. The duodena of anesthetized CFTR-, NHE3-, Slc26a6-, and Scl26a3-deficient mice and wild-type (WT) littermates were perfused, and duodenal bicarbonate (HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>) secretion (DBS) and fluid absorptive or secretory rates were measured. The selective NHE3 inhibitor S1611 or genetic ablation of NHE3 significantly reduced fluid absorptive rates and increased DBS. Slc26a6 (PAT1) or Slc26a3 (DRA) ablation reduced the S1611-induced DBS increase and reduced fluid absorptive rates, suggesting that the effect of S1611 or NHE3 ablation on HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretion may be an unmasking of Slc26a6- and Slc26a3-mediated Cl<jats:sup>−</jats:sup>/HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>exchange activity. In the absence of CFTR expression or after application of the CFTR(inh)-172, fluid absorptive rates were similar to those of WT, but S1611 induced virtually no increase in DBS, demonstrating that CFTR transport activity, and not just its presence, is required for Slc26-mediated duodenal HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretion. A functionally active CFTR is an absolute requirement for Slc26-mediated duodenal HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretion, but not for Slc26-mediated fluid absorption, in which these transporters operate in conjunction with the Na<jats:sup>+</jats:sup>/H<jats:sup>+</jats:sup>exchanger NHE3. This suggests that Slc26a6 and Slc26a3 need proton recycling via NHE3 to operate in the Cl<jats:sup>−</jats:sup>absorptive mode and Cl<jats:sup>−</jats:sup>exit via CFTR to operate in the HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretory mode.</jats:p> The switch of intestinal Slc26 exchangers from anion absorptive to HCO<sub>3</sub><sup>−</sup>secretory mode is dependent on CFTR anion channel function American Journal of Physiology-Cell Physiology |
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10.1152/ajpcell.00454.2009 |
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Biologie |
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American Physiological Society, 2010 |
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American Physiological Society |
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American Journal of Physiology-Cell Physiology |
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| title |
The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function |
| title_unstemmed |
The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function |
| title_full |
The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function |
| title_fullStr |
The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function |
| title_full_unstemmed |
The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function |
| title_short |
The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function |
| title_sort |
the switch of intestinal slc26 exchangers from anion absorptive to hco<sub>3</sub><sup>−</sup>secretory mode is dependent on cftr anion channel function |
| topic |
Cell Biology Physiology |
| url |
http://dx.doi.org/10.1152/ajpcell.00454.2009 |
| publishDate |
2010 |
| physical |
C1057-C1065 |
| description |
<jats:p>CFTR has been recognized to function as both an anion channel and a key regulator of Slc26 anion transporters in heterologous expression systems. Whether this regulatory relationship between CFTR and Slc26 transporters is seen in native intestine, and whether this effect is coupled to CFTR transport function or other features of this protein, has not been studied. The duodena of anesthetized CFTR-, NHE3-, Slc26a6-, and Scl26a3-deficient mice and wild-type (WT) littermates were perfused, and duodenal bicarbonate (HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>) secretion (DBS) and fluid absorptive or secretory rates were measured. The selective NHE3 inhibitor S1611 or genetic ablation of NHE3 significantly reduced fluid absorptive rates and increased DBS. Slc26a6 (PAT1) or Slc26a3 (DRA) ablation reduced the S1611-induced DBS increase and reduced fluid absorptive rates, suggesting that the effect of S1611 or NHE3 ablation on HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretion may be an unmasking of Slc26a6- and Slc26a3-mediated Cl<jats:sup>−</jats:sup>/HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>exchange activity. In the absence of CFTR expression or after application of the CFTR(inh)-172, fluid absorptive rates were similar to those of WT, but S1611 induced virtually no increase in DBS, demonstrating that CFTR transport activity, and not just its presence, is required for Slc26-mediated duodenal HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretion. A functionally active CFTR is an absolute requirement for Slc26-mediated duodenal HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretion, but not for Slc26-mediated fluid absorption, in which these transporters operate in conjunction with the Na<jats:sup>+</jats:sup>/H<jats:sup>+</jats:sup>exchanger NHE3. This suggests that Slc26a6 and Slc26a3 need proton recycling via NHE3 to operate in the Cl<jats:sup>−</jats:sup>absorptive mode and Cl<jats:sup>−</jats:sup>exit via CFTR to operate in the HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretory mode.</jats:p> |
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| author | Singh, Anurag Kumar, Riederer, Brigitte, Chen, Mingmin, Xiao, Fang, Krabbenhöft, Anja, Engelhardt, Regina, Nylander, Olof, Soleimani, Manoocher, Seidler, Ursula |
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| description | <jats:p>CFTR has been recognized to function as both an anion channel and a key regulator of Slc26 anion transporters in heterologous expression systems. Whether this regulatory relationship between CFTR and Slc26 transporters is seen in native intestine, and whether this effect is coupled to CFTR transport function or other features of this protein, has not been studied. The duodena of anesthetized CFTR-, NHE3-, Slc26a6-, and Scl26a3-deficient mice and wild-type (WT) littermates were perfused, and duodenal bicarbonate (HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>) secretion (DBS) and fluid absorptive or secretory rates were measured. The selective NHE3 inhibitor S1611 or genetic ablation of NHE3 significantly reduced fluid absorptive rates and increased DBS. Slc26a6 (PAT1) or Slc26a3 (DRA) ablation reduced the S1611-induced DBS increase and reduced fluid absorptive rates, suggesting that the effect of S1611 or NHE3 ablation on HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretion may be an unmasking of Slc26a6- and Slc26a3-mediated Cl<jats:sup>−</jats:sup>/HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>exchange activity. In the absence of CFTR expression or after application of the CFTR(inh)-172, fluid absorptive rates were similar to those of WT, but S1611 induced virtually no increase in DBS, demonstrating that CFTR transport activity, and not just its presence, is required for Slc26-mediated duodenal HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretion. A functionally active CFTR is an absolute requirement for Slc26-mediated duodenal HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretion, but not for Slc26-mediated fluid absorption, in which these transporters operate in conjunction with the Na<jats:sup>+</jats:sup>/H<jats:sup>+</jats:sup>exchanger NHE3. This suggests that Slc26a6 and Slc26a3 need proton recycling via NHE3 to operate in the Cl<jats:sup>−</jats:sup>absorptive mode and Cl<jats:sup>−</jats:sup>exit via CFTR to operate in the HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretory mode.</jats:p> |
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| series | American Journal of Physiology-Cell Physiology |
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| spelling | Singh, Anurag Kumar Riederer, Brigitte Chen, Mingmin Xiao, Fang Krabbenhöft, Anja Engelhardt, Regina Nylander, Olof Soleimani, Manoocher Seidler, Ursula 0363-6143 1522-1563 American Physiological Society Cell Biology Physiology http://dx.doi.org/10.1152/ajpcell.00454.2009 <jats:p>CFTR has been recognized to function as both an anion channel and a key regulator of Slc26 anion transporters in heterologous expression systems. Whether this regulatory relationship between CFTR and Slc26 transporters is seen in native intestine, and whether this effect is coupled to CFTR transport function or other features of this protein, has not been studied. The duodena of anesthetized CFTR-, NHE3-, Slc26a6-, and Scl26a3-deficient mice and wild-type (WT) littermates were perfused, and duodenal bicarbonate (HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>) secretion (DBS) and fluid absorptive or secretory rates were measured. The selective NHE3 inhibitor S1611 or genetic ablation of NHE3 significantly reduced fluid absorptive rates and increased DBS. Slc26a6 (PAT1) or Slc26a3 (DRA) ablation reduced the S1611-induced DBS increase and reduced fluid absorptive rates, suggesting that the effect of S1611 or NHE3 ablation on HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretion may be an unmasking of Slc26a6- and Slc26a3-mediated Cl<jats:sup>−</jats:sup>/HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>exchange activity. In the absence of CFTR expression or after application of the CFTR(inh)-172, fluid absorptive rates were similar to those of WT, but S1611 induced virtually no increase in DBS, demonstrating that CFTR transport activity, and not just its presence, is required for Slc26-mediated duodenal HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretion. A functionally active CFTR is an absolute requirement for Slc26-mediated duodenal HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretion, but not for Slc26-mediated fluid absorption, in which these transporters operate in conjunction with the Na<jats:sup>+</jats:sup>/H<jats:sup>+</jats:sup>exchanger NHE3. This suggests that Slc26a6 and Slc26a3 need proton recycling via NHE3 to operate in the Cl<jats:sup>−</jats:sup>absorptive mode and Cl<jats:sup>−</jats:sup>exit via CFTR to operate in the HCO<jats:sub>3</jats:sub><jats:sup>−</jats:sup>secretory mode.</jats:p> The switch of intestinal Slc26 exchangers from anion absorptive to HCO<sub>3</sub><sup>−</sup>secretory mode is dependent on CFTR anion channel function American Journal of Physiology-Cell Physiology |
| spellingShingle | Singh, Anurag Kumar, Riederer, Brigitte, Chen, Mingmin, Xiao, Fang, Krabbenhöft, Anja, Engelhardt, Regina, Nylander, Olof, Soleimani, Manoocher, Seidler, Ursula, American Journal of Physiology-Cell Physiology, The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function, Cell Biology, Physiology |
| title | The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function |
| title_full | The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function |
| title_fullStr | The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function |
| title_full_unstemmed | The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function |
| title_short | The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function |
| title_sort | the switch of intestinal slc26 exchangers from anion absorptive to hco<sub>3</sub><sup>−</sup>secretory mode is dependent on cftr anion channel function |
| title_unstemmed | The switch of intestinal Slc26 exchangers from anion absorptive to HCO3−secretory mode is dependent on CFTR anion channel function |
| topic | Cell Biology, Physiology |
| url | http://dx.doi.org/10.1152/ajpcell.00454.2009 |