author_facet Börner, Volker
Fei, You‐Jun
Hartrodt, Bianka
Ganapathy, Vadivel
Leibach, Frederick H.
Neubert, Klaus
Brandsch, Matthias
Börner, Volker
Fei, You‐Jun
Hartrodt, Bianka
Ganapathy, Vadivel
Leibach, Frederick H.
Neubert, Klaus
Brandsch, Matthias
author Börner, Volker
Fei, You‐Jun
Hartrodt, Bianka
Ganapathy, Vadivel
Leibach, Frederick H.
Neubert, Klaus
Brandsch, Matthias
spellingShingle Börner, Volker
Fei, You‐Jun
Hartrodt, Bianka
Ganapathy, Vadivel
Leibach, Frederick H.
Neubert, Klaus
Brandsch, Matthias
European Journal of Biochemistry
Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
Biochemistry
author_sort börner, volker
spelling Börner, Volker Fei, You‐Jun Hartrodt, Bianka Ganapathy, Vadivel Leibach, Frederick H. Neubert, Klaus Brandsch, Matthias 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1046/j.1432-1327.1998.2550698.x <jats:p>Transport of amino acid aryl amides by the intestinal H<jats:sup>+</jats:sup>/peptide symporter (PEPT1) was studied in Caco‐2 cells and in <jats:italic>Xenopus laevis</jats:italic> oocytes expressing human PEPT1. Several amino acid amides were able to inhibit the uptake of [<jats:sup>14</jats:sup>C]glycylsarcosine in Caco‐2 cells. Ala‐4‐nitroanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.08 mM), Phe‐4‐nitroanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.09 mM) and Ala‐4‐phenylanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.03 mM) were accepted as substrates with equal or higher affinity than natural Ala‐Xaa dipeptides. Ala‐anilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 2.9 mM), Ala‐7‐amido‐4‐methylcoumarin (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.2 mM), Ala‐4‐chloroanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.3 mM) and Ala‐4‐methylanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.3 mM) were also recognized by PEPT1 as substrates. In contrast, alanine, Ala‐amide, Phe‐amide, Ala‐methyl ester, Ala‐4‐nitrobenzyl ester and Ala‐methylamide were not recognized (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> &gt; 20 mM). In <jats:italic>X. laevis</jats:italic> oocytes, transport of Ala‐4‐nitroanilide, Ala‐7‐amido‐4‐methylcoumarin, Ala‐4‐methylanilide and Ala‐anilide was associated with transfer of positive charge and the currents were saturable with respect to substrate concentration (<jats:italic>K</jats:italic><jats:sub>0.5</jats:sub> values : 0.1, 0.2, 0.8 and 3.1 mM, respectively). The currents induced by Ala‐4‐methylanilide were saturable with respect to the substrate concentration and influenced by the membrane potential. The affinity of the transporter for Ala‐4‐methylanilide was also found to be influenced by the membrane potential. We conclude that the intestinal H<jats:sup>+</jats:sup>/peptide cotransport system PEPT1 accepts amino acid aryl amides as substrates.</jats:p> Transport of amino acid aryl amides by the intestinal H<sup>+</sup>/peptide cotransport system, PEPT1 European Journal of Biochemistry
doi_str_mv 10.1046/j.1432-1327.1998.2550698.x
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imprint_str_mv Wiley, 1998
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match_str borner1998transportofaminoacidarylamidesbytheintestinalhpeptidecotransportsystempept1
publishDateSort 1998
publisher Wiley
recordtype ai
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series European Journal of Biochemistry
source_id 49
title Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
title_unstemmed Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
title_full Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
title_fullStr Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
title_full_unstemmed Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
title_short Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
title_sort transport of amino acid aryl amides by the intestinal h<sup>+</sup>/peptide cotransport system, pept1
topic Biochemistry
url http://dx.doi.org/10.1046/j.1432-1327.1998.2550698.x
publishDate 1998
physical 698-702
description <jats:p>Transport of amino acid aryl amides by the intestinal H<jats:sup>+</jats:sup>/peptide symporter (PEPT1) was studied in Caco‐2 cells and in <jats:italic>Xenopus laevis</jats:italic> oocytes expressing human PEPT1. Several amino acid amides were able to inhibit the uptake of [<jats:sup>14</jats:sup>C]glycylsarcosine in Caco‐2 cells. Ala‐4‐nitroanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.08 mM), Phe‐4‐nitroanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.09 mM) and Ala‐4‐phenylanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.03 mM) were accepted as substrates with equal or higher affinity than natural Ala‐Xaa dipeptides. Ala‐anilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 2.9 mM), Ala‐7‐amido‐4‐methylcoumarin (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.2 mM), Ala‐4‐chloroanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.3 mM) and Ala‐4‐methylanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.3 mM) were also recognized by PEPT1 as substrates. In contrast, alanine, Ala‐amide, Phe‐amide, Ala‐methyl ester, Ala‐4‐nitrobenzyl ester and Ala‐methylamide were not recognized (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> &gt; 20 mM). In <jats:italic>X. laevis</jats:italic> oocytes, transport of Ala‐4‐nitroanilide, Ala‐7‐amido‐4‐methylcoumarin, Ala‐4‐methylanilide and Ala‐anilide was associated with transfer of positive charge and the currents were saturable with respect to substrate concentration (<jats:italic>K</jats:italic><jats:sub>0.5</jats:sub> values : 0.1, 0.2, 0.8 and 3.1 mM, respectively). The currents induced by Ala‐4‐methylanilide were saturable with respect to the substrate concentration and influenced by the membrane potential. The affinity of the transporter for Ala‐4‐methylanilide was also found to be influenced by the membrane potential. We conclude that the intestinal H<jats:sup>+</jats:sup>/peptide cotransport system PEPT1 accepts amino acid aryl amides as substrates.</jats:p>
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author Börner, Volker, Fei, You‐Jun, Hartrodt, Bianka, Ganapathy, Vadivel, Leibach, Frederick H., Neubert, Klaus, Brandsch, Matthias
author_facet Börner, Volker, Fei, You‐Jun, Hartrodt, Bianka, Ganapathy, Vadivel, Leibach, Frederick H., Neubert, Klaus, Brandsch, Matthias, Börner, Volker, Fei, You‐Jun, Hartrodt, Bianka, Ganapathy, Vadivel, Leibach, Frederick H., Neubert, Klaus, Brandsch, Matthias
author_sort börner, volker
container_issue 3
container_start_page 698
container_title European Journal of Biochemistry
container_volume 255
description <jats:p>Transport of amino acid aryl amides by the intestinal H<jats:sup>+</jats:sup>/peptide symporter (PEPT1) was studied in Caco‐2 cells and in <jats:italic>Xenopus laevis</jats:italic> oocytes expressing human PEPT1. Several amino acid amides were able to inhibit the uptake of [<jats:sup>14</jats:sup>C]glycylsarcosine in Caco‐2 cells. Ala‐4‐nitroanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.08 mM), Phe‐4‐nitroanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.09 mM) and Ala‐4‐phenylanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.03 mM) were accepted as substrates with equal or higher affinity than natural Ala‐Xaa dipeptides. Ala‐anilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 2.9 mM), Ala‐7‐amido‐4‐methylcoumarin (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.2 mM), Ala‐4‐chloroanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.3 mM) and Ala‐4‐methylanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.3 mM) were also recognized by PEPT1 as substrates. In contrast, alanine, Ala‐amide, Phe‐amide, Ala‐methyl ester, Ala‐4‐nitrobenzyl ester and Ala‐methylamide were not recognized (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> &gt; 20 mM). In <jats:italic>X. laevis</jats:italic> oocytes, transport of Ala‐4‐nitroanilide, Ala‐7‐amido‐4‐methylcoumarin, Ala‐4‐methylanilide and Ala‐anilide was associated with transfer of positive charge and the currents were saturable with respect to substrate concentration (<jats:italic>K</jats:italic><jats:sub>0.5</jats:sub> values : 0.1, 0.2, 0.8 and 3.1 mM, respectively). The currents induced by Ala‐4‐methylanilide were saturable with respect to the substrate concentration and influenced by the membrane potential. The affinity of the transporter for Ala‐4‐methylanilide was also found to be influenced by the membrane potential. We conclude that the intestinal H<jats:sup>+</jats:sup>/peptide cotransport system PEPT1 accepts amino acid aryl amides as substrates.</jats:p>
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imprint Wiley, 1998
imprint_str_mv Wiley, 1998
institution DE-D275, 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
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match_str borner1998transportofaminoacidarylamidesbytheintestinalhpeptidecotransportsystempept1
mega_collection Wiley (CrossRef)
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publishDate 1998
publishDateSort 1998
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record_format ai
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series European Journal of Biochemistry
source_id 49
spelling Börner, Volker Fei, You‐Jun Hartrodt, Bianka Ganapathy, Vadivel Leibach, Frederick H. Neubert, Klaus Brandsch, Matthias 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1046/j.1432-1327.1998.2550698.x <jats:p>Transport of amino acid aryl amides by the intestinal H<jats:sup>+</jats:sup>/peptide symporter (PEPT1) was studied in Caco‐2 cells and in <jats:italic>Xenopus laevis</jats:italic> oocytes expressing human PEPT1. Several amino acid amides were able to inhibit the uptake of [<jats:sup>14</jats:sup>C]glycylsarcosine in Caco‐2 cells. Ala‐4‐nitroanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.08 mM), Phe‐4‐nitroanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.09 mM) and Ala‐4‐phenylanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.03 mM) were accepted as substrates with equal or higher affinity than natural Ala‐Xaa dipeptides. Ala‐anilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 2.9 mM), Ala‐7‐amido‐4‐methylcoumarin (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.2 mM), Ala‐4‐chloroanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.3 mM) and Ala‐4‐methylanilide (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 0.3 mM) were also recognized by PEPT1 as substrates. In contrast, alanine, Ala‐amide, Phe‐amide, Ala‐methyl ester, Ala‐4‐nitrobenzyl ester and Ala‐methylamide were not recognized (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> &gt; 20 mM). In <jats:italic>X. laevis</jats:italic> oocytes, transport of Ala‐4‐nitroanilide, Ala‐7‐amido‐4‐methylcoumarin, Ala‐4‐methylanilide and Ala‐anilide was associated with transfer of positive charge and the currents were saturable with respect to substrate concentration (<jats:italic>K</jats:italic><jats:sub>0.5</jats:sub> values : 0.1, 0.2, 0.8 and 3.1 mM, respectively). The currents induced by Ala‐4‐methylanilide were saturable with respect to the substrate concentration and influenced by the membrane potential. The affinity of the transporter for Ala‐4‐methylanilide was also found to be influenced by the membrane potential. We conclude that the intestinal H<jats:sup>+</jats:sup>/peptide cotransport system PEPT1 accepts amino acid aryl amides as substrates.</jats:p> Transport of amino acid aryl amides by the intestinal H<sup>+</sup>/peptide cotransport system, PEPT1 European Journal of Biochemistry
spellingShingle Börner, Volker, Fei, You‐Jun, Hartrodt, Bianka, Ganapathy, Vadivel, Leibach, Frederick H., Neubert, Klaus, Brandsch, Matthias, European Journal of Biochemistry, Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1, Biochemistry
title Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
title_full Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
title_fullStr Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
title_full_unstemmed Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
title_short Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
title_sort transport of amino acid aryl amides by the intestinal h<sup>+</sup>/peptide cotransport system, pept1
title_unstemmed Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
topic Biochemistry
url http://dx.doi.org/10.1046/j.1432-1327.1998.2550698.x