Cloning and Characterisation of Multiple Ferritin Isoforms in the Atlantic Salmon (Salmo salar)
Ferritin is a highly-conserved iron-storage protein that has also been identified as an acute phase protein within the innate immune system. The iron-storage function is mediated through complementary roles played by heavy (H)-chain subunit as well as the light (L) in mammals or middle (M)-chain in...
Published in: | PLoS ONE |
---|---|
Main Authors: | , , , |
Format: | Text |
Language: | English |
Published: |
Public Library of Science
2014
|
Subjects: | |
Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4117605 http://www.ncbi.nlm.nih.gov/pubmed/25078784 https://doi.org/10.1371/journal.pone.0103729 |
id |
ftpubmed:oai:pubmedcentral.nih.gov:4117605 |
---|---|
record_format |
openpolar |
spelling |
ftpubmed:oai:pubmedcentral.nih.gov:4117605 2023-05-15T15:30:51+02:00 Cloning and Characterisation of Multiple Ferritin Isoforms in the Atlantic Salmon (Salmo salar) Lee, Jun-Hoe Pooley, Nicholas J. Mohd-Adnan, Adura Martin, Samuel A. M. 2014-07-31 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4117605 http://www.ncbi.nlm.nih.gov/pubmed/25078784 https://doi.org/10.1371/journal.pone.0103729 en eng Public Library of Science http://www.ncbi.nlm.nih.gov/pmc/articles/PMC http://www.ncbi.nlm.nih.gov/pubmed/25078784 http://dx.doi.org/10.1371/journal.pone.0103729 This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. CC-BY Research Article Text 2014 ftpubmed https://doi.org/10.1371/journal.pone.0103729 2014-08-10T00:54:58Z Ferritin is a highly-conserved iron-storage protein that has also been identified as an acute phase protein within the innate immune system. The iron-storage function is mediated through complementary roles played by heavy (H)-chain subunit as well as the light (L) in mammals or middle (M)-chain in teleosts, respectively. In this study, we report the identification of five ferritin subunits (H1, H2, M1, M2, M3) in the Atlantic salmon that were supported by the presence of iron-regulatory regions, gene structure, conserved domains and phylogenetic analysis. Tissue distribution analysis across eight different tissues showed that each of these isoforms is differentially expressed. We also examined the expression of the ferritin isoforms in the liver and kidney of juvenile Atlantic salmon that was challenged with Aeromonas salmonicida as well as in muscle cell culture stimulated with interleukin-1β. We found that each isoform displayed unique expression profiles, and in certain conditions the expressions between the isoforms were completely diametrical to each other. Our study is the first report of multiple ferritin isoforms from both the H- and M-chains in a vertebrate species, as well as ferritin isoforms that showed decreased expression in response to infection. Taken together, the results of our study suggest the possibility of functional differences between the H- and M-chain isoforms in terms of tissue localisation, transcriptional response to bacterial exposure and stimulation by specific immune factors. Text Atlantic salmon Salmo salar PubMed Central (PMC) PLoS ONE 9 7 e103729 |
institution |
Open Polar |
collection |
PubMed Central (PMC) |
op_collection_id |
ftpubmed |
language |
English |
topic |
Research Article |
spellingShingle |
Research Article Lee, Jun-Hoe Pooley, Nicholas J. Mohd-Adnan, Adura Martin, Samuel A. M. Cloning and Characterisation of Multiple Ferritin Isoforms in the Atlantic Salmon (Salmo salar) |
topic_facet |
Research Article |
description |
Ferritin is a highly-conserved iron-storage protein that has also been identified as an acute phase protein within the innate immune system. The iron-storage function is mediated through complementary roles played by heavy (H)-chain subunit as well as the light (L) in mammals or middle (M)-chain in teleosts, respectively. In this study, we report the identification of five ferritin subunits (H1, H2, M1, M2, M3) in the Atlantic salmon that were supported by the presence of iron-regulatory regions, gene structure, conserved domains and phylogenetic analysis. Tissue distribution analysis across eight different tissues showed that each of these isoforms is differentially expressed. We also examined the expression of the ferritin isoforms in the liver and kidney of juvenile Atlantic salmon that was challenged with Aeromonas salmonicida as well as in muscle cell culture stimulated with interleukin-1β. We found that each isoform displayed unique expression profiles, and in certain conditions the expressions between the isoforms were completely diametrical to each other. Our study is the first report of multiple ferritin isoforms from both the H- and M-chains in a vertebrate species, as well as ferritin isoforms that showed decreased expression in response to infection. Taken together, the results of our study suggest the possibility of functional differences between the H- and M-chain isoforms in terms of tissue localisation, transcriptional response to bacterial exposure and stimulation by specific immune factors. |
format |
Text |
author |
Lee, Jun-Hoe Pooley, Nicholas J. Mohd-Adnan, Adura Martin, Samuel A. M. |
author_facet |
Lee, Jun-Hoe Pooley, Nicholas J. Mohd-Adnan, Adura Martin, Samuel A. M. |
author_sort |
Lee, Jun-Hoe |
title |
Cloning and Characterisation of Multiple Ferritin Isoforms in the Atlantic Salmon (Salmo salar) |
title_short |
Cloning and Characterisation of Multiple Ferritin Isoforms in the Atlantic Salmon (Salmo salar) |
title_full |
Cloning and Characterisation of Multiple Ferritin Isoforms in the Atlantic Salmon (Salmo salar) |
title_fullStr |
Cloning and Characterisation of Multiple Ferritin Isoforms in the Atlantic Salmon (Salmo salar) |
title_full_unstemmed |
Cloning and Characterisation of Multiple Ferritin Isoforms in the Atlantic Salmon (Salmo salar) |
title_sort |
cloning and characterisation of multiple ferritin isoforms in the atlantic salmon (salmo salar) |
publisher |
Public Library of Science |
publishDate |
2014 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4117605 http://www.ncbi.nlm.nih.gov/pubmed/25078784 https://doi.org/10.1371/journal.pone.0103729 |
genre |
Atlantic salmon Salmo salar |
genre_facet |
Atlantic salmon Salmo salar |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC http://www.ncbi.nlm.nih.gov/pubmed/25078784 http://dx.doi.org/10.1371/journal.pone.0103729 |
op_rights |
This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.1371/journal.pone.0103729 |
container_title |
PLoS ONE |
container_volume |
9 |
container_issue |
7 |
container_start_page |
e103729 |
_version_ |
1766361326746075136 |