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Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1
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Zeitschriftentitel: | European Journal of Biochemistry |
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Personen und Körperschaften: | , , , , , , |
In: | European Journal of Biochemistry, 255, 1998, 3, S. 698-702 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Wiley
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Schlagwörter: |
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 |
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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> > 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 |
facet_avail |
Online Free |
finc_class_facet |
Chemie und Pharmazie |
format |
ElectronicArticle |
fullrecord |
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ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA0Ni9qLjE0MzItMTMyNy4xOTk4LjI1NTA2OTgueA |
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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 |
imprint |
Wiley, 1998 |
imprint_str_mv |
Wiley, 1998 |
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0014-2956 1432-1033 |
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0014-2956 1432-1033 |
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English |
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Wiley (CrossRef) |
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borner1998transportofaminoacidarylamidesbytheintestinalhpeptidecotransportsystempept1 |
publishDateSort |
1998 |
publisher |
Wiley |
recordtype |
ai |
record_format |
ai |
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> > 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 |
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container_title | European Journal of Biochemistry |
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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> > 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> |
doi_str_mv | 10.1046/j.1432-1327.1998.2550698.x |
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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) |
physical | 698-702 |
publishDate | 1998 |
publishDateSort | 1998 |
publisher | Wiley |
record_format | ai |
recordtype | ai |
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> > 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 |