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

Lee JH, Pooley NJ, Mohd-Adnan A, Martin SA - PLoS ONE (2014)

Bottom Line: 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.Tissue distribution analysis across eight different tissues showed that each of these isoforms is differentially expressed.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.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biological and Environmental Sciences, University of Aberdeen, Aberdeen, United Kingdom; School of Biosciences and Biotechnology, Faculty of Science & Technology, University of Kebangsaan, Selangor, Malaysia.

ABSTRACT
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.

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Related in: MedlinePlus

Tissue distribution of the ferritin H- and M-chain isoforms (H, M1, M2, M3) in S. salar.The relative expression of H-chain was measured as the total expression of the H1 and H2 isoforms. The relative expression of each isoform was normalised to the averaged expression of ef1α and βact. Bars represent standard errors mean (± SEM, n = 4).
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pone-0103729-g004: Tissue distribution of the ferritin H- and M-chain isoforms (H, M1, M2, M3) in S. salar.The relative expression of H-chain was measured as the total expression of the H1 and H2 isoforms. The relative expression of each isoform was normalised to the averaged expression of ef1α and βact. Bars represent standard errors mean (± SEM, n = 4).

Mentions: The expression of the ferritin isoforms was examined in in 7 tissues (trunk kidney, head kidney, liver, muscle, brain, gill and intestine) from 4 healthy juvenile S. salar individuals. The relative expression of the ferritin isoforms was normalised to the expression of ef1α and βact, and presented as relative to the lowest ferritin expression value in a particular tissue (Figure 4). The expression of the H-chain (H1 and H2) was found in all of the examined tissues and the highest expression was observed in the muscle tissue. The expression of the M-chain isoforms (M1, M2 and M3) exhibited variation among the different tissues. M1 showed the highest expression in trunk kidney, followed by almost similar expression values in gills and head kidney. In contrast, the highest expression levels of M2 were almost similar among the liver, gills and trunk kidney. On the other hand, the expression of M3 was highest in liver and brain, but was not found in detectable levels in the gills, intestine and muscle (Ct>35) (data not shown).


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

Lee JH, Pooley NJ, Mohd-Adnan A, Martin SA - PLoS ONE (2014)

Tissue distribution of the ferritin H- and M-chain isoforms (H, M1, M2, M3) in S. salar.The relative expression of H-chain was measured as the total expression of the H1 and H2 isoforms. The relative expression of each isoform was normalised to the averaged expression of ef1α and βact. Bars represent standard errors mean (± SEM, n = 4).
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4117605&req=5

pone-0103729-g004: Tissue distribution of the ferritin H- and M-chain isoforms (H, M1, M2, M3) in S. salar.The relative expression of H-chain was measured as the total expression of the H1 and H2 isoforms. The relative expression of each isoform was normalised to the averaged expression of ef1α and βact. Bars represent standard errors mean (± SEM, n = 4).
Mentions: The expression of the ferritin isoforms was examined in in 7 tissues (trunk kidney, head kidney, liver, muscle, brain, gill and intestine) from 4 healthy juvenile S. salar individuals. The relative expression of the ferritin isoforms was normalised to the expression of ef1α and βact, and presented as relative to the lowest ferritin expression value in a particular tissue (Figure 4). The expression of the H-chain (H1 and H2) was found in all of the examined tissues and the highest expression was observed in the muscle tissue. The expression of the M-chain isoforms (M1, M2 and M3) exhibited variation among the different tissues. M1 showed the highest expression in trunk kidney, followed by almost similar expression values in gills and head kidney. In contrast, the highest expression levels of M2 were almost similar among the liver, gills and trunk kidney. On the other hand, the expression of M3 was highest in liver and brain, but was not found in detectable levels in the gills, intestine and muscle (Ct>35) (data not shown).

Bottom Line: 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.Tissue distribution analysis across eight different tissues showed that each of these isoforms is differentially expressed.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.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biological and Environmental Sciences, University of Aberdeen, Aberdeen, United Kingdom; School of Biosciences and Biotechnology, Faculty of Science & Technology, University of Kebangsaan, Selangor, Malaysia.

ABSTRACT
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.

Show MeSH
Related in: MedlinePlus