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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

Fold changes in the expression of the ferritin H- and M-chain isoforms (H, M1, M2, M3) in the A. liver and B. kidney tissues of S. salar 24 hours post-infection with attenuated A. salmonicida.Bars represent standard errors mean (± SEM, n = 8) and asterisks indicate significant differences (p<0.05, t-test).
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pone-0103729-g005: Fold changes in the expression of the ferritin H- and M-chain isoforms (H, M1, M2, M3) in the A. liver and B. kidney tissues of S. salar 24 hours post-infection with attenuated A. salmonicida.Bars represent standard errors mean (± SEM, n = 8) and asterisks indicate significant differences (p<0.05, t-test).

Mentions: Total RNA was extracted from the liver and kidney tissues of S. salar at 24 hours post-infection with attenuated A. salmonicida to examine the expression changes of the ferritin isoforms. The expression of ferritin isoform M3 was excluded as several samples exhibited low peaks at Ct>35, which is generally considered unreliable due to the accumulation of background noise or non-specific fluorescence at that stage [40]. In general, distinct expression profiles were observed between the ferritin isoforms in the liver and kidney tissues in response to infection (Figure 5). In the liver, there was a significant increase of approximately 2.5-fold in the expression of the H-chain and M2. In contrast, the expression of M1 exhibited a minor decrease of 1.5-fold. The expression of the H-chain in the kidney also increased significantly by 2.5-fold, although the expression of M1 and M2 was decreased by approximately 1.5-fold.


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)

Fold changes in the expression of the ferritin H- and M-chain isoforms (H, M1, M2, M3) in the A. liver and B. kidney tissues of S. salar 24 hours post-infection with attenuated A. salmonicida.Bars represent standard errors mean (± SEM, n = 8) and asterisks indicate significant differences (p<0.05, t-test).
© Copyright Policy
Related In: Results  -  Collection

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

pone-0103729-g005: Fold changes in the expression of the ferritin H- and M-chain isoforms (H, M1, M2, M3) in the A. liver and B. kidney tissues of S. salar 24 hours post-infection with attenuated A. salmonicida.Bars represent standard errors mean (± SEM, n = 8) and asterisks indicate significant differences (p<0.05, t-test).
Mentions: Total RNA was extracted from the liver and kidney tissues of S. salar at 24 hours post-infection with attenuated A. salmonicida to examine the expression changes of the ferritin isoforms. The expression of ferritin isoform M3 was excluded as several samples exhibited low peaks at Ct>35, which is generally considered unreliable due to the accumulation of background noise or non-specific fluorescence at that stage [40]. In general, distinct expression profiles were observed between the ferritin isoforms in the liver and kidney tissues in response to infection (Figure 5). In the liver, there was a significant increase of approximately 2.5-fold in the expression of the H-chain and M2. In contrast, the expression of M1 exhibited a minor decrease of 1.5-fold. The expression of the H-chain in the kidney also increased significantly by 2.5-fold, although the expression of M1 and M2 was decreased by approximately 1.5-fold.

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