Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5539943 | Developmental & Comparative Immunology | 2017 | 9 Pages |
Abstract
Ferritin is a major iron storage protein essential not only in the infectious process, but also in any circumstance generating oxidative stress. In this study, the cDNA coding sequence of ferritin-H was obtained from the sub-Antarctic Notothenioid fish Eleginops maclovinus through transcriptomic analysis of the head kidney. This sequence contained a 534 bp open reading frame that coded for a 177 amino acid protein with a molecular weight of 20,786.2Â Da and a theoretical pI of 5.56. The protein displayed a region of iron putative response elements in the 5â²UTR, two putative ferritin iron-binding region signatures, and seven characteristic amino acids with ferroxidase functions. Phylogenetic analysis related this sequence to ferritin-H sequences of other Antarctic Notothenioid fish, sharing 96.61% similarity. Constitutive gene expression analysis in different organs revealed increased ferritin-H gene expression in the gills, spleen, muscle, and liver. After infection with two bacterial strains of Piscirickettsia salmonis (LF-89 and Austral-005), ferritin-H was differentially expressed depending on bacterial strain and tissue. This study provides relevant information towards understanding the iron metabolism of a sub-Antarctic Notothenioid fish.
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Authors
D. MartÃnez, R. Oyarzún, C. Vargas-Lagos, J.P. Pontigo, M. Soto-Dávila, J. Saravia, A. Romero, J.J. Núñez, A.J. Yáñez, L. Vargas-Chacoff,