ArticlePloS one2014
Cloning and characterisation of multiple ferritin isoforms in the Atlantic salmon (Salmo salar).
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Identification of Rana dybowskii Ferritin-Heavy chain gene and analysis of its role during bacterial infection.PloS one · 2025Article
- Review
- Deploying new generation sequencing for the study of flesh color depletion in Atlantic Salmon (Salmo salar).BMC genomics · 2021Article
- Chimeric Protein IPathVaccines · 2021Article
- High-throughput proteomic profiling of the fish liver following bacterial infection.BMC genomics · 2018Article
- Epidemiology of DanishFrontiers in microbiology · 2017Article
- Article
- Ferritin M of Paralichthys olivaceus possesses antimicrobial and antioxidative properties.Fish physiology and biochemistry · 2015Article
- Global gene expression patterns of grass carp following compensatory growth.BMC genomics · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
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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