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D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter
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| Zeitschriftentitel: | British Journal of Pharmacology |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | British Journal of Pharmacology, 115, 1995, 5, S. 761-766 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Thwaites, David T. Armstrong, Gillian Hirst, Barry H. Simmons, Nicholas L. Thwaites, David T. Armstrong, Gillian Hirst, Barry H. Simmons, Nicholas L. |
|---|---|
| author |
Thwaites, David T. Armstrong, Gillian Hirst, Barry H. Simmons, Nicholas L. |
| spellingShingle |
Thwaites, David T. Armstrong, Gillian Hirst, Barry H. Simmons, Nicholas L. British Journal of Pharmacology D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter Pharmacology |
| author_sort |
thwaites, david t. |
| spelling |
Thwaites, David T. Armstrong, Gillian Hirst, Barry H. Simmons, Nicholas L. 0007-1188 1476-5381 Wiley Pharmacology http://dx.doi.org/10.1111/j.1476-5381.1995.tb14998.x <jats:p><jats:list list-type="explicit-label"> <jats:list-item><jats:p>The ability of D‐cycloserine to act as a substrate for H<jats:sup>+</jats:sup>/amino acid symport has been tested in epithelial layers of Caco‐2 human intestinal cells.</jats:p></jats:list-item> <jats:list-item><jats:p>In Na<jats:sup>+</jats:sup>‐free media with the apical bathing media held at pH 6.0, D‐cycloserine (20 mM) is an effective inhibitor of net transepithelial transport (J<jats:sub>net</jats:sub>) of L‐alanine (100 μ<jats:sc>m</jats:sc>) and its accumulation (across the apical membrane) in a similar manner to amino acid substrates (L‐alanine, β‐alanine, L‐proline and glycine). In contrast L‐valine was ineffective as an inhibitor for H<jats:sup>+</jats:sup>/amino acid symport. Both inhibition of L‐alanine J<jats:sub>net</jats:sub> and its accumulation by D‐cycloserine were dose‐dependent, maximal inhibition being achieved by 5–10 mM.</jats:p></jats:list-item> <jats:list-item><jats:p>Both D‐cycloserine and known substrates for H<jats:sup>+</jats:sup>/amino acid symport stimulated an inward short circuit current (<jats:italic>I</jats:italic><jats:sub>sc</jats:sub>) when voltage‐clamped monolayers of Caco‐2 epitheha, mounted in Ussing chambers, were exposed to apical substrate in Na<jats:sup>+</jats:sup>‐free media, with apical pH held at 6.0. The D‐cycloserine dependent increase in <jats:italic>I</jats:italic><jats:sub>sc</jats:sub> was dose‐dependent with an apparent <jats:italic>K</jats:italic><jats:sub>m</jats:sub>= 15.8 + 2.0 (mean ± s.e.mean) mM, and V<jats:sub>max</jats:sub> = 373±21 nmol cm<jats:sup>−2</jats:sup> h<jats:sup>−1</jats:sup>.</jats:p></jats:list-item> <jats:list-item><jats:p>D‐Cycloserine (20 mM) induced a prompt acidification of Caco‐2 cell cytosol when superfused at the apical surface in both Na<jats:sup>+</jats:sup> and Na<jats:sup>+</jats:sup>‐free conditions. Cytosolic acidification in response to D‐cycloserine was dependent upon superfusate pH, being attenuated at pH 8 and enhanced in acidic media.</jats:p></jats:list-item> <jats:list-item><jats:p>The increment in <jats:italic>I</jats:italic><jats:sub>sc</jats:sub> with 20 mM D‐cycloserine was non‐additive with other amino acid substrates for H<jats:sup>+</jats:sup>/amino acid symport.</jats:p></jats:list-item> </jats:list></jats:p> D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H <sup>+</sup> ‐coupled amino acid transporter British Journal of Pharmacology |
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10.1111/j.1476-5381.1995.tb14998.x |
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Online Free |
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Chemie und Pharmazie |
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Wiley, 1995 |
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Wiley, 1995 |
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0007-1188 1476-5381 |
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1995 |
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Wiley |
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ai |
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ai |
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British Journal of Pharmacology |
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49 |
| title |
D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter |
| title_unstemmed |
D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter |
| title_full |
D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter |
| title_fullStr |
D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter |
| title_full_unstemmed |
D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter |
| title_short |
D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter |
| title_sort |
d‐cycloserine transport in human intestinal epithelial (caco‐2) cells: mediation by a h <sup>+</sup> ‐coupled amino acid transporter |
| topic |
Pharmacology |
| url |
http://dx.doi.org/10.1111/j.1476-5381.1995.tb14998.x |
| publishDate |
1995 |
| physical |
761-766 |
| description |
<jats:p><jats:list list-type="explicit-label">
<jats:list-item><jats:p>The ability of D‐cycloserine to act as a substrate for H<jats:sup>+</jats:sup>/amino acid symport has been tested in epithelial layers of Caco‐2 human intestinal cells.</jats:p></jats:list-item>
<jats:list-item><jats:p>In Na<jats:sup>+</jats:sup>‐free media with the apical bathing media held at pH 6.0, D‐cycloserine (20 mM) is an effective inhibitor of net transepithelial transport (J<jats:sub>net</jats:sub>) of L‐alanine (100 μ<jats:sc>m</jats:sc>) and its accumulation (across the apical membrane) in a similar manner to amino acid substrates (L‐alanine, β‐alanine, L‐proline and glycine). In contrast L‐valine was ineffective as an inhibitor for H<jats:sup>+</jats:sup>/amino acid symport. Both inhibition of L‐alanine J<jats:sub>net</jats:sub> and its accumulation by D‐cycloserine were dose‐dependent, maximal inhibition being achieved by 5–10 mM.</jats:p></jats:list-item>
<jats:list-item><jats:p>Both D‐cycloserine and known substrates for H<jats:sup>+</jats:sup>/amino acid symport stimulated an inward short circuit current (<jats:italic>I</jats:italic><jats:sub>sc</jats:sub>) when voltage‐clamped monolayers of Caco‐2 epitheha, mounted in Ussing chambers, were exposed to apical substrate in Na<jats:sup>+</jats:sup>‐free media, with apical pH held at 6.0. The D‐cycloserine dependent increase in <jats:italic>I</jats:italic><jats:sub>sc</jats:sub> was dose‐dependent with an apparent <jats:italic>K</jats:italic><jats:sub>m</jats:sub>= 15.8 + 2.0 (mean ± s.e.mean) mM, and V<jats:sub>max</jats:sub> = 373±21 nmol cm<jats:sup>−2</jats:sup> h<jats:sup>−1</jats:sup>.</jats:p></jats:list-item>
<jats:list-item><jats:p>D‐Cycloserine (20 mM) induced a prompt acidification of Caco‐2 cell cytosol when superfused at the apical surface in both Na<jats:sup>+</jats:sup> and Na<jats:sup>+</jats:sup>‐free conditions. Cytosolic acidification in response to D‐cycloserine was dependent upon superfusate pH, being attenuated at pH 8 and enhanced in acidic media.</jats:p></jats:list-item>
<jats:list-item><jats:p>The increment in <jats:italic>I</jats:italic><jats:sub>sc</jats:sub> with 20 mM D‐cycloserine was non‐additive with other amino acid substrates for H<jats:sup>+</jats:sup>/amino acid symport.</jats:p></jats:list-item>
</jats:list></jats:p> |
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| description | <jats:p><jats:list list-type="explicit-label"> <jats:list-item><jats:p>The ability of D‐cycloserine to act as a substrate for H<jats:sup>+</jats:sup>/amino acid symport has been tested in epithelial layers of Caco‐2 human intestinal cells.</jats:p></jats:list-item> <jats:list-item><jats:p>In Na<jats:sup>+</jats:sup>‐free media with the apical bathing media held at pH 6.0, D‐cycloserine (20 mM) is an effective inhibitor of net transepithelial transport (J<jats:sub>net</jats:sub>) of L‐alanine (100 μ<jats:sc>m</jats:sc>) and its accumulation (across the apical membrane) in a similar manner to amino acid substrates (L‐alanine, β‐alanine, L‐proline and glycine). In contrast L‐valine was ineffective as an inhibitor for H<jats:sup>+</jats:sup>/amino acid symport. Both inhibition of L‐alanine J<jats:sub>net</jats:sub> and its accumulation by D‐cycloserine were dose‐dependent, maximal inhibition being achieved by 5–10 mM.</jats:p></jats:list-item> <jats:list-item><jats:p>Both D‐cycloserine and known substrates for H<jats:sup>+</jats:sup>/amino acid symport stimulated an inward short circuit current (<jats:italic>I</jats:italic><jats:sub>sc</jats:sub>) when voltage‐clamped monolayers of Caco‐2 epitheha, mounted in Ussing chambers, were exposed to apical substrate in Na<jats:sup>+</jats:sup>‐free media, with apical pH held at 6.0. The D‐cycloserine dependent increase in <jats:italic>I</jats:italic><jats:sub>sc</jats:sub> was dose‐dependent with an apparent <jats:italic>K</jats:italic><jats:sub>m</jats:sub>= 15.8 + 2.0 (mean ± s.e.mean) mM, and V<jats:sub>max</jats:sub> = 373±21 nmol cm<jats:sup>−2</jats:sup> h<jats:sup>−1</jats:sup>.</jats:p></jats:list-item> <jats:list-item><jats:p>D‐Cycloserine (20 mM) induced a prompt acidification of Caco‐2 cell cytosol when superfused at the apical surface in both Na<jats:sup>+</jats:sup> and Na<jats:sup>+</jats:sup>‐free conditions. Cytosolic acidification in response to D‐cycloserine was dependent upon superfusate pH, being attenuated at pH 8 and enhanced in acidic media.</jats:p></jats:list-item> <jats:list-item><jats:p>The increment in <jats:italic>I</jats:italic><jats:sub>sc</jats:sub> with 20 mM D‐cycloserine was non‐additive with other amino acid substrates for H<jats:sup>+</jats:sup>/amino acid symport.</jats:p></jats:list-item> </jats:list></jats:p> |
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| spelling | Thwaites, David T. Armstrong, Gillian Hirst, Barry H. Simmons, Nicholas L. 0007-1188 1476-5381 Wiley Pharmacology http://dx.doi.org/10.1111/j.1476-5381.1995.tb14998.x <jats:p><jats:list list-type="explicit-label"> <jats:list-item><jats:p>The ability of D‐cycloserine to act as a substrate for H<jats:sup>+</jats:sup>/amino acid symport has been tested in epithelial layers of Caco‐2 human intestinal cells.</jats:p></jats:list-item> <jats:list-item><jats:p>In Na<jats:sup>+</jats:sup>‐free media with the apical bathing media held at pH 6.0, D‐cycloserine (20 mM) is an effective inhibitor of net transepithelial transport (J<jats:sub>net</jats:sub>) of L‐alanine (100 μ<jats:sc>m</jats:sc>) and its accumulation (across the apical membrane) in a similar manner to amino acid substrates (L‐alanine, β‐alanine, L‐proline and glycine). In contrast L‐valine was ineffective as an inhibitor for H<jats:sup>+</jats:sup>/amino acid symport. Both inhibition of L‐alanine J<jats:sub>net</jats:sub> and its accumulation by D‐cycloserine were dose‐dependent, maximal inhibition being achieved by 5–10 mM.</jats:p></jats:list-item> <jats:list-item><jats:p>Both D‐cycloserine and known substrates for H<jats:sup>+</jats:sup>/amino acid symport stimulated an inward short circuit current (<jats:italic>I</jats:italic><jats:sub>sc</jats:sub>) when voltage‐clamped monolayers of Caco‐2 epitheha, mounted in Ussing chambers, were exposed to apical substrate in Na<jats:sup>+</jats:sup>‐free media, with apical pH held at 6.0. The D‐cycloserine dependent increase in <jats:italic>I</jats:italic><jats:sub>sc</jats:sub> was dose‐dependent with an apparent <jats:italic>K</jats:italic><jats:sub>m</jats:sub>= 15.8 + 2.0 (mean ± s.e.mean) mM, and V<jats:sub>max</jats:sub> = 373±21 nmol cm<jats:sup>−2</jats:sup> h<jats:sup>−1</jats:sup>.</jats:p></jats:list-item> <jats:list-item><jats:p>D‐Cycloserine (20 mM) induced a prompt acidification of Caco‐2 cell cytosol when superfused at the apical surface in both Na<jats:sup>+</jats:sup> and Na<jats:sup>+</jats:sup>‐free conditions. Cytosolic acidification in response to D‐cycloserine was dependent upon superfusate pH, being attenuated at pH 8 and enhanced in acidic media.</jats:p></jats:list-item> <jats:list-item><jats:p>The increment in <jats:italic>I</jats:italic><jats:sub>sc</jats:sub> with 20 mM D‐cycloserine was non‐additive with other amino acid substrates for H<jats:sup>+</jats:sup>/amino acid symport.</jats:p></jats:list-item> </jats:list></jats:p> D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H <sup>+</sup> ‐coupled amino acid transporter British Journal of Pharmacology |
| spellingShingle | Thwaites, David T., Armstrong, Gillian, Hirst, Barry H., Simmons, Nicholas L., British Journal of Pharmacology, D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter, Pharmacology |
| title | D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter |
| title_full | D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter |
| title_fullStr | D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter |
| title_full_unstemmed | D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter |
| title_short | D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter |
| title_sort | d‐cycloserine transport in human intestinal epithelial (caco‐2) cells: mediation by a h <sup>+</sup> ‐coupled amino acid transporter |
| title_unstemmed | D‐Cycloserine transport in human intestinal epithelial (Caco‐2) cells: mediation by a H + ‐coupled amino acid transporter |
| topic | Pharmacology |
| url | http://dx.doi.org/10.1111/j.1476-5381.1995.tb14998.x |