Identification, expression, and responses to bacterial challenge of the cathepsin C gene from the razor clam...

Cathepsin C (dipeptidyl-peptidaseI, DPPI) is a lysosomal cysteine proteinase that belongs to the papain superfamily, and it is involved in protein degradation and proenzyme activation. However, very little is known about the function of cathepsin C in bivalves. In the present study, we identified the cathepsin C gene in the razor clam Sinonovacula constricta (Sc-CTSC). The full-length Sc-CTSC cDNA contained a complete open reading frame (ORF) of 1371 nt encoding 456 amino acids, a 98 bp 5' UTR, and a 1043 bp 3' UTR. The ORF of Sc-CTSC consisted of a putative signal peptide of 22 aa, a propeptide of 229 aa, and a mature peptide of 205 aa containing the active site triad of Cys, His, and Asn. The Sc-CTSC transcript was expressed in a wide range of tissues but exhibited the greatest level of expression in the digestive gland. During the early developmental stages, the transcript was detected widely. Upon injection with Vibrio anguillarum, the Sc-CTSC transcript was significantly up-regulated in digestive gland, mantle, and gill tissues. The results provided important information for further exploring the roles of cathepsin C in the innate immune responses.