Teleost fish models in membrane transport research: the PEPT1(SLC15A1) H+–oligopeptide transporter as a case study

Human genes for passive, ion-coupled transporters and exchangers are included in the so-called solute carrier (SLC) gene series, to date consisting of 52 families and 398 genes. Teleost fish genes for SLC proteins have also been described in the last two decades, and catalogued in preliminary SLC-li...

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Published in:The Journal of Physiology
Main Authors: Romano, Alessandro, Barca, Amilcare, Storelli, Carlo, Verri, Tiziano
Format: Text
Language:English
Published: John Wiley & Sons Ltd 2014
Subjects:
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3948553
http://www.ncbi.nlm.nih.gov/pubmed/23981715
https://doi.org/10.1113/jphysiol.2013.259622
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spelling ftpubmed:oai:pubmedcentral.nih.gov:3948553 2023-05-15T16:42:07+02:00 Teleost fish models in membrane transport research: the PEPT1(SLC15A1) H+–oligopeptide transporter as a case study Romano, Alessandro Barca, Amilcare Storelli, Carlo Verri, Tiziano 2014-03-01 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3948553 http://www.ncbi.nlm.nih.gov/pubmed/23981715 https://doi.org/10.1113/jphysiol.2013.259622 en eng John Wiley & Sons Ltd http://www.ncbi.nlm.nih.gov/pmc/articles/PMC http://www.ncbi.nlm.nih.gov/pubmed/23981715 http://dx.doi.org/10.1113/jphysiol.2013.259622 ©2013 The Authors. The Journal of Physiology © 2013 The Physiological Society Symposium Review Text 2014 ftpubmed https://doi.org/10.1113/jphysiol.2013.259622 2015-03-08T01:01:19Z Human genes for passive, ion-coupled transporters and exchangers are included in the so-called solute carrier (SLC) gene series, to date consisting of 52 families and 398 genes. Teleost fish genes for SLC proteins have also been described in the last two decades, and catalogued in preliminary SLC-like form in 50 families and at least 338 genes after systematic GenBank database mining (December 2010–March 2011). When the kinetic properties of the expressed proteins are studied in detail, teleost fish SLC transporters always reveal extraordinary ‘molecular diversity’ with respect to the mammalian counterparts, which reflects peculiar adaptation of the protein to the physiology of the species and/or to the environment where the species lives. In the case of the H+–oligopeptide transporter PEPT1(SLC15A1), comparative analysis of diverse teleost fish orthologs has shown that the protein may exhibit very eccentric properties in terms of pH dependence (e.g. the adaptation of zebrafish PEPT1 to alkaline pH), temperature dependence (e.g. the adaptation of icefish PEPT1 to sub-zero temperatures) and/or substrate specificity (e.g. the species-specificity of PEPT1 for the uptake of l-lysine-containing peptides). The revelation of such peculiarities is providing new contributions to the discussion on PEPT1 in both basic (e.g. molecular structure–function analyses) and applied research (e.g. optimizing diets to enhance growth of commercially valuable fish). Text Icefish PubMed Central (PMC) The Journal of Physiology 592 5 881 897
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Symposium Review
spellingShingle Symposium Review
Romano, Alessandro
Barca, Amilcare
Storelli, Carlo
Verri, Tiziano
Teleost fish models in membrane transport research: the PEPT1(SLC15A1) H+–oligopeptide transporter as a case study
topic_facet Symposium Review
description Human genes for passive, ion-coupled transporters and exchangers are included in the so-called solute carrier (SLC) gene series, to date consisting of 52 families and 398 genes. Teleost fish genes for SLC proteins have also been described in the last two decades, and catalogued in preliminary SLC-like form in 50 families and at least 338 genes after systematic GenBank database mining (December 2010–March 2011). When the kinetic properties of the expressed proteins are studied in detail, teleost fish SLC transporters always reveal extraordinary ‘molecular diversity’ with respect to the mammalian counterparts, which reflects peculiar adaptation of the protein to the physiology of the species and/or to the environment where the species lives. In the case of the H+–oligopeptide transporter PEPT1(SLC15A1), comparative analysis of diverse teleost fish orthologs has shown that the protein may exhibit very eccentric properties in terms of pH dependence (e.g. the adaptation of zebrafish PEPT1 to alkaline pH), temperature dependence (e.g. the adaptation of icefish PEPT1 to sub-zero temperatures) and/or substrate specificity (e.g. the species-specificity of PEPT1 for the uptake of l-lysine-containing peptides). The revelation of such peculiarities is providing new contributions to the discussion on PEPT1 in both basic (e.g. molecular structure–function analyses) and applied research (e.g. optimizing diets to enhance growth of commercially valuable fish).
format Text
author Romano, Alessandro
Barca, Amilcare
Storelli, Carlo
Verri, Tiziano
author_facet Romano, Alessandro
Barca, Amilcare
Storelli, Carlo
Verri, Tiziano
author_sort Romano, Alessandro
title Teleost fish models in membrane transport research: the PEPT1(SLC15A1) H+–oligopeptide transporter as a case study
title_short Teleost fish models in membrane transport research: the PEPT1(SLC15A1) H+–oligopeptide transporter as a case study
title_full Teleost fish models in membrane transport research: the PEPT1(SLC15A1) H+–oligopeptide transporter as a case study
title_fullStr Teleost fish models in membrane transport research: the PEPT1(SLC15A1) H+–oligopeptide transporter as a case study
title_full_unstemmed Teleost fish models in membrane transport research: the PEPT1(SLC15A1) H+–oligopeptide transporter as a case study
title_sort teleost fish models in membrane transport research: the pept1(slc15a1) h+–oligopeptide transporter as a case study
publisher John Wiley & Sons Ltd
publishDate 2014
url http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3948553
http://www.ncbi.nlm.nih.gov/pubmed/23981715
https://doi.org/10.1113/jphysiol.2013.259622
genre Icefish
genre_facet Icefish
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC
http://www.ncbi.nlm.nih.gov/pubmed/23981715
http://dx.doi.org/10.1113/jphysiol.2013.259622
op_rights ©2013 The Authors. The Journal of Physiology © 2013 The Physiological Society
op_doi https://doi.org/10.1113/jphysiol.2013.259622
container_title The Journal of Physiology
container_volume 592
container_issue 5
container_start_page 881
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