Identification and characterization of a hepcidin from half-smooth tongue sole Cynoglossus semilaevis
Abstract
Hepcidin, an antimicrobial peptide, has a dual function including innate immunity and iron regulation. Here, based on the sequence of an EST database, we have isolated and characterized a hepcidin gene (referred to as CsHepcidin) from half-smooth tongue sole (Cynoglossus semilaevis). Analysis of the coding regions indicated CsHepcidin gene comprised 3 exons and 2 introns. The putative CsHepcidin showed a great similarity to other hepcidin orthologues, particularly with respect to its 24 aa signal peptide, typical RX(K/R)R motif and eight conserved cysteine residues in the mature cationic peptide. Phylogenic analysis indicated that CsHepcidin was a hepcidin 1-type peptide of acanthopterygians, with highly homologous with Solea senegalensis hepcidin. In C. semilaevis ontogeny, CsHepcidin mRNA was detected at a low level in unfertilized eggs, increased on 6 d after hatching, and decreased remarkably at metamorphic stage. CsHepcidin transcripts showed a constitutive basal expression in most of the tissues, especially in liver. Challenge with formalin-inactivated Vibrio anguillarum led to significantly up-regulations of CsHepcidin gene in liver, head kidney and spleen in time-dependent manners. Biological activity analysis showed th...Continue Reading
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