Abstract
Clusterin is a broadly distributed glycoprotein constitutively expressed by various tissues and cell types and has been shown to be associated with several physiological and pathological functions. In order to study the molecular evolution of clusterin, here we report the cloning and characterization of two clusterin genes in rainbow trout (Oncorhynchus mykiss). The deduced amino acid sequences of clusterin-1 and a partial clusterin-2 clone are 89% identical to each other, showing 45, 42 and 38% identity with chicken, frog and human orthologs, respectively. Most of the putative N-glycosylation sites, as well as all 10 cysteine residues which are involved in disulfide bond formation in the mature trout clusterin-1 protein, are fully conserved when aligned with its orthologs from various species. Although trout clusterin genes exhibit the same exon–intron organization, in line with that of human clusterin, they show a totally different mRNA expression profile among various trout tissues. Phylogenetic analysis indicates an early segregation of the clusterin ancestral gene within the taxon of fish leading to the formation of a separate subgroup.
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