The calpains, calcium-activated neutral proteases, play important roles in calcium-regulated intra-cellular signal transduction cascades. Here we report the isolation and initial characterization of a cDNA encoding a calpain 9, digestive tract specific calpain, from catfish taste epithelium. This calpain 9 (Ip-CAPN9a) shares 61% identity with human calpain 9. Phylogenetic analysis provides evidence that catfish calpain 9 and the related enzymes from Oncorhynchus mykiss , Danio rerio , Xenopus laevis , Mus musculus , Rattus norvegicus and Homo sapiens make up a distinct clade within the tissue-specific calpain family. Northern blot analysis reveals that Ip-CAPN9a is predominantly expressed in barbell and digestive tract, but not expressed in brain. An antibody against the N-terminal segment of Ip-CAPN9a recognizes cells within the taste buds in catfish barbells.
KeywordsGene EvolutionTasteNovel Type
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