The teleost fish PepT1-type peptide transporters and their relationships with neutral and charged substrates
In teleosts, two PepT1-type (Slc15a1) transporters, i.e., PepT1a and PepT1b, are expressed at the intestinal level. They translocate charged di/tripeptides with different efficiency, which depends on the position of the charged amino acid in the peptide and the external pH. The relation between the...
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ftpubmed:oai:pubmedcentral.nih.gov:10475540 2023-10-09T21:49:54+02:00 The teleost fish PepT1-type peptide transporters and their relationships with neutral and charged substrates Vacca, Francesca Gomes, Ana S. De Gennaro, Marco Rønnestad, Ivar Bossi, Elena Verri, Tiziano 2023-08-21 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10475540/ http://www.ncbi.nlm.nih.gov/pubmed/37670771 https://doi.org/10.3389/fphys.2023.1186475 en eng Frontiers Media S.A. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10475540/ http://www.ncbi.nlm.nih.gov/pubmed/37670771 http://dx.doi.org/10.3389/fphys.2023.1186475 Copyright © 2023 Vacca, Gomes, De Gennaro, Rønnestad, Bossi and Verri. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. Front Physiol Physiology Text 2023 ftpubmed https://doi.org/10.3389/fphys.2023.1186475 2023-09-10T00:50:18Z In teleosts, two PepT1-type (Slc15a1) transporters, i.e., PepT1a and PepT1b, are expressed at the intestinal level. They translocate charged di/tripeptides with different efficiency, which depends on the position of the charged amino acid in the peptide and the external pH. The relation between the position of the charged amino acid and the capability of transporting the dipeptide was investigated in the zebrafish and Atlantic salmon PepT1-type transporters. Using selected charged (at physiological pH) dipeptides: i.e., the negatively charged Asp-Gly and Gly-Asp, and the positively charged Lys-Gly and Gly-Lys and Lys-Met and Met-Lys, transport currents and kinetic parameters were collected. The neutral dipeptide Gly-Gln was used as a reference substrate. Atlantic salmon PepT1a and PepT1b transport currents were similar in the presence of Asp-Gly and Gly-Asp, while zebrafish PepT1a elicited currents strongly dependent on the position of Asp in the dipeptide and zebrafish PepT1b elicited small transport currents. For Lys- and Met-containing dipeptides smaller currents compared to Gly-Gln were observed in PepT1a-type transporters. In general, for zebrafish PepT1a the currents elicited by all tested substrates slightly increased with membrane potential and pH. For Atlantic salmon PepT1a, the transport current increased with negative potential but only in the presence of Met-containing dipeptides and in a pH-dependent way. Conversely, large currents were shown for PepT1b for all tested substrates but Gly-Lys in Atlantic salmon. This shows that in Atlantic salmon PepT1b for Lys-containing substrates the position of the charged dipeptides carrying the Lys residue defines the current amplitudes, with larger currents observed for Lys in the N-terminal position. Our results add information on the ability of PepT1 to transport charged amino acids and show species-specificity in the kinetic behavior of PepT1-type proteins. They also suggest the importance of the proximity of the substrate binding site of residues such as ... Text Atlantic salmon PubMed Central (PMC) Frontiers in Physiology 14 |
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Physiology Vacca, Francesca Gomes, Ana S. De Gennaro, Marco Rønnestad, Ivar Bossi, Elena Verri, Tiziano The teleost fish PepT1-type peptide transporters and their relationships with neutral and charged substrates |
topic_facet |
Physiology |
description |
In teleosts, two PepT1-type (Slc15a1) transporters, i.e., PepT1a and PepT1b, are expressed at the intestinal level. They translocate charged di/tripeptides with different efficiency, which depends on the position of the charged amino acid in the peptide and the external pH. The relation between the position of the charged amino acid and the capability of transporting the dipeptide was investigated in the zebrafish and Atlantic salmon PepT1-type transporters. Using selected charged (at physiological pH) dipeptides: i.e., the negatively charged Asp-Gly and Gly-Asp, and the positively charged Lys-Gly and Gly-Lys and Lys-Met and Met-Lys, transport currents and kinetic parameters were collected. The neutral dipeptide Gly-Gln was used as a reference substrate. Atlantic salmon PepT1a and PepT1b transport currents were similar in the presence of Asp-Gly and Gly-Asp, while zebrafish PepT1a elicited currents strongly dependent on the position of Asp in the dipeptide and zebrafish PepT1b elicited small transport currents. For Lys- and Met-containing dipeptides smaller currents compared to Gly-Gln were observed in PepT1a-type transporters. In general, for zebrafish PepT1a the currents elicited by all tested substrates slightly increased with membrane potential and pH. For Atlantic salmon PepT1a, the transport current increased with negative potential but only in the presence of Met-containing dipeptides and in a pH-dependent way. Conversely, large currents were shown for PepT1b for all tested substrates but Gly-Lys in Atlantic salmon. This shows that in Atlantic salmon PepT1b for Lys-containing substrates the position of the charged dipeptides carrying the Lys residue defines the current amplitudes, with larger currents observed for Lys in the N-terminal position. Our results add information on the ability of PepT1 to transport charged amino acids and show species-specificity in the kinetic behavior of PepT1-type proteins. They also suggest the importance of the proximity of the substrate binding site of residues such as ... |
format |
Text |
author |
Vacca, Francesca Gomes, Ana S. De Gennaro, Marco Rønnestad, Ivar Bossi, Elena Verri, Tiziano |
author_facet |
Vacca, Francesca Gomes, Ana S. De Gennaro, Marco Rønnestad, Ivar Bossi, Elena Verri, Tiziano |
author_sort |
Vacca, Francesca |
title |
The teleost fish PepT1-type peptide transporters and their relationships with neutral and charged substrates |
title_short |
The teleost fish PepT1-type peptide transporters and their relationships with neutral and charged substrates |
title_full |
The teleost fish PepT1-type peptide transporters and their relationships with neutral and charged substrates |
title_fullStr |
The teleost fish PepT1-type peptide transporters and their relationships with neutral and charged substrates |
title_full_unstemmed |
The teleost fish PepT1-type peptide transporters and their relationships with neutral and charged substrates |
title_sort |
teleost fish pept1-type peptide transporters and their relationships with neutral and charged substrates |
publisher |
Frontiers Media S.A. |
publishDate |
2023 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10475540/ http://www.ncbi.nlm.nih.gov/pubmed/37670771 https://doi.org/10.3389/fphys.2023.1186475 |
genre |
Atlantic salmon |
genre_facet |
Atlantic salmon |
op_source |
Front Physiol |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10475540/ http://www.ncbi.nlm.nih.gov/pubmed/37670771 http://dx.doi.org/10.3389/fphys.2023.1186475 |
op_rights |
Copyright © 2023 Vacca, Gomes, De Gennaro, Rønnestad, Bossi and Verri. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
op_doi |
https://doi.org/10.3389/fphys.2023.1186475 |
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Frontiers in Physiology |
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1779312944132128768 |