Identification and characterization of the Atlantic salmon peptide transporter 1a
Peptide transporter 1 (PepT1) mediates the uptake of dietary di-/tripeptides in vertebrates. However, in teleost fish gut, more than one PepT1-type transporter might operate, because of teleost-specific whole gen(om)e duplication event(s) that occurred during evolution. Here, we describe a novel tel...
Published in: | American Journal of Physiology-Cell Physiology |
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Online Access: | http://hdl.handle.net/11383/2086905 https://doi.org/10.1152/ajpcell.00360.2019 https://www.physiology.org/doi/pdf/10.1152/ajpcell.00360.2019 |
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ftuninsubriairis:oai:irinsubria.uninsubria.it:11383/2086905 2024-09-09T19:30:01+00:00 Identification and characterization of the Atlantic salmon peptide transporter 1a Gomes A. S. Vacca F. Cinquetti R. Murashita K. Barca A. Bossi E. Ronnestad I. Verri T. Gomes, A. S. Vacca, F. Cinquetti, R. Murashita, K. Barca, A. Bossi, E. Ronnestad, I. Verri, T. 2020 ELETTRONICO http://hdl.handle.net/11383/2086905 https://doi.org/10.1152/ajpcell.00360.2019 https://www.physiology.org/doi/pdf/10.1152/ajpcell.00360.2019 eng eng info:eu-repo/semantics/altIdentifier/pmid/31664857 info:eu-repo/semantics/altIdentifier/wos/WOS:000507356500016 volume:318 issue:1 firstpage:C191 lastpage:C204 numberofpages:14 journal:AMERICAN JOURNAL OF PHYSIOLOGY. CELL PHYSIOLOGY http://hdl.handle.net/11383/2086905 doi:10.1152/ajpcell.00360.2019 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85077664265 https://www.physiology.org/doi/pdf/10.1152/ajpcell.00360.2019 info:eu-repo/semantics/closedAccess Di-/tripeptide transport(ers) Digestive physiology Peptide absorption Whole genome duplication Xenopus laevis oocyte info:eu-repo/semantics/article 2020 ftuninsubriairis https://doi.org/10.1152/ajpcell.00360.2019 2024-07-22T23:37:26Z Peptide transporter 1 (PepT1) mediates the uptake of dietary di-/tripeptides in vertebrates. However, in teleost fish gut, more than one PepT1-type transporter might operate, because of teleost-specific whole gen(om)e duplication event(s) that occurred during evolution. Here, we describe a novel teleost di-/tripeptide transporter, i.e., the Atlantic salmon (Salmo salar) peptide transporter 1a [PepT1a; or solute carrier family 15 member 1a (Slc15a1a)], which is a paralog (77% similarity and 64% identity at the amino acid level) of the well-described Atlantic salmon peptide transporter 1b [PepT1b, alias PepT1; or solute carrier family 15 member 1b (Slc15a1b)]. Comparative analysis and evolutionary relationships of gene/protein sequences were conducted after ad hoc database mining. Tissue mRNA expression analysis was performed by quantitative real-time PCR, whereas transport function analysis was accomplished by heterologous expression in Xenopus laevis oocytes and two-electrode voltage-clamp measurements. Atlantic salmon pept1a is highly expressed in the proximal intestine (pyloric ceca ≈ anterior midgut > midgut > > posterior midgut), in the same gut regions as pept1b but notably ∼5-fold less abundant. Like PepT1b, Atlantic salmon PepT1a is a low-affinity/high-capacity system. Functional analysis showed electrogenic, Na+-independent/pH-dependent transport and apparent substrate affinity (K0.5) values for Gly-Gln of 1.593 mmol/L at pH 7.6 and 0.076 mmol/L at pH 6.5. In summary, we show that a piscine PepT1a-type transporter is functional. Defining the role of Atlantic salmon PepT1a in the gut will help to understand the evolutionary and functional relationships among peptide transporters. Its functional characterization will contribute to elucidate the relevance of peptide transporters in Atlantic salmon nutritional physiology. Article in Journal/Newspaper Atlantic salmon Salmo salar IRInSubria - Institutional Repository Insubria (Università degli Studi dell’Insubria) American Journal of Physiology-Cell Physiology 318 1 C191 C204 |
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Open Polar |
collection |
IRInSubria - Institutional Repository Insubria (Università degli Studi dell’Insubria) |
op_collection_id |
ftuninsubriairis |
language |
English |
topic |
Di-/tripeptide transport(ers) Digestive physiology Peptide absorption Whole genome duplication Xenopus laevis oocyte |
spellingShingle |
Di-/tripeptide transport(ers) Digestive physiology Peptide absorption Whole genome duplication Xenopus laevis oocyte Gomes A. S. Vacca F. Cinquetti R. Murashita K. Barca A. Bossi E. Ronnestad I. Verri T. Identification and characterization of the Atlantic salmon peptide transporter 1a |
topic_facet |
Di-/tripeptide transport(ers) Digestive physiology Peptide absorption Whole genome duplication Xenopus laevis oocyte |
description |
Peptide transporter 1 (PepT1) mediates the uptake of dietary di-/tripeptides in vertebrates. However, in teleost fish gut, more than one PepT1-type transporter might operate, because of teleost-specific whole gen(om)e duplication event(s) that occurred during evolution. Here, we describe a novel teleost di-/tripeptide transporter, i.e., the Atlantic salmon (Salmo salar) peptide transporter 1a [PepT1a; or solute carrier family 15 member 1a (Slc15a1a)], which is a paralog (77% similarity and 64% identity at the amino acid level) of the well-described Atlantic salmon peptide transporter 1b [PepT1b, alias PepT1; or solute carrier family 15 member 1b (Slc15a1b)]. Comparative analysis and evolutionary relationships of gene/protein sequences were conducted after ad hoc database mining. Tissue mRNA expression analysis was performed by quantitative real-time PCR, whereas transport function analysis was accomplished by heterologous expression in Xenopus laevis oocytes and two-electrode voltage-clamp measurements. Atlantic salmon pept1a is highly expressed in the proximal intestine (pyloric ceca ≈ anterior midgut > midgut > > posterior midgut), in the same gut regions as pept1b but notably ∼5-fold less abundant. Like PepT1b, Atlantic salmon PepT1a is a low-affinity/high-capacity system. Functional analysis showed electrogenic, Na+-independent/pH-dependent transport and apparent substrate affinity (K0.5) values for Gly-Gln of 1.593 mmol/L at pH 7.6 and 0.076 mmol/L at pH 6.5. In summary, we show that a piscine PepT1a-type transporter is functional. Defining the role of Atlantic salmon PepT1a in the gut will help to understand the evolutionary and functional relationships among peptide transporters. Its functional characterization will contribute to elucidate the relevance of peptide transporters in Atlantic salmon nutritional physiology. |
author2 |
Gomes, A. S. Vacca, F. Cinquetti, R. Murashita, K. Barca, A. Bossi, E. Ronnestad, I. Verri, T. |
format |
Article in Journal/Newspaper |
author |
Gomes A. S. Vacca F. Cinquetti R. Murashita K. Barca A. Bossi E. Ronnestad I. Verri T. |
author_facet |
Gomes A. S. Vacca F. Cinquetti R. Murashita K. Barca A. Bossi E. Ronnestad I. Verri T. |
author_sort |
Gomes A. S. |
title |
Identification and characterization of the Atlantic salmon peptide transporter 1a |
title_short |
Identification and characterization of the Atlantic salmon peptide transporter 1a |
title_full |
Identification and characterization of the Atlantic salmon peptide transporter 1a |
title_fullStr |
Identification and characterization of the Atlantic salmon peptide transporter 1a |
title_full_unstemmed |
Identification and characterization of the Atlantic salmon peptide transporter 1a |
title_sort |
identification and characterization of the atlantic salmon peptide transporter 1a |
publishDate |
2020 |
url |
http://hdl.handle.net/11383/2086905 https://doi.org/10.1152/ajpcell.00360.2019 https://www.physiology.org/doi/pdf/10.1152/ajpcell.00360.2019 |
genre |
Atlantic salmon Salmo salar |
genre_facet |
Atlantic salmon Salmo salar |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/31664857 info:eu-repo/semantics/altIdentifier/wos/WOS:000507356500016 volume:318 issue:1 firstpage:C191 lastpage:C204 numberofpages:14 journal:AMERICAN JOURNAL OF PHYSIOLOGY. CELL PHYSIOLOGY http://hdl.handle.net/11383/2086905 doi:10.1152/ajpcell.00360.2019 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85077664265 https://www.physiology.org/doi/pdf/10.1152/ajpcell.00360.2019 |
op_rights |
info:eu-repo/semantics/closedAccess |
op_doi |
https://doi.org/10.1152/ajpcell.00360.2019 |
container_title |
American Journal of Physiology-Cell Physiology |
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318 |
container_issue |
1 |
container_start_page |
C191 |
op_container_end_page |
C204 |
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1809899053089030144 |