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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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 |
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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 |
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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 |
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The Journal of Physiology |
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592 |
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5 |
container_start_page |
881 |
op_container_end_page |
897 |
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1766032565198651392 |