Lee, Jun Hoe

Martin, Samuel A M

Mohd-Adnan, Adura

Pooley, Nicholas J.

PLoS ONE

English

PubMed

<div><p>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 <i>Aeromonas salmonicida</i> 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.</p></div

Jun-Hoe Lee (606677)

Nicholas J. Pooley (606678)

Adura Mohd-Adnan (361084)

Samuel A. M. Martin (158994)

The Francis Crick Institute

Cloning and Characterisation of Multiple Ferritin Isoforms in the Atlantic Salmon (<i>Salmo salar</i>)

The Open University

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 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

Jun-Hoe Lee

Nicholas J Pooley

Adura Mohd-Adnan

Samuel A M Martin

Directory of Open Access Journals

Cloning and characterisation of multiple ferritin isoforms in the Atlantic salmon (Salmo salar).

Nicholas J. Pooley

Samuel A. M. Martin

Crossref

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 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-1b. 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 bacteria

Jun-hoe Lee

Adura Mohd-adnan

CiteSeerX

https://figshare.com/articles/Cloning_and_Characterisation_of_Multiple_Ferritin_Isoforms_in_the_Atlantic_Salmon_Salmo_salar_/1123094

Cloning and characterisation of multiple ferritin isoforms in the Atlantic salmon (Salmo salar)

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The Francis Crick Institute

The Open University

Directory of Open Access Journals

Crossref

CiteSeerX