Abstract:
In order to understand the role of BMP in biomineralization process in mollusca, a BMP7 homolog in
Pinctada fucata named
BMP7
b was cloned in this study. The full length of
BMP7
b was 2 464 bp, including an open reading frame (ORF) of 1 194 bp which encoded 397 amino acids. The protein sequence included a signal peptide (1–26 aa), a pro-domain (25–240 aa) and a TGF-β domain (299–396 aa). No transmembrane domain was detected.
BMP7
b was expressed in all kinds of tissues and was higher expressed in gill and mantle, but lower in intestine and hepatopancreas. The
BMP7
b expression level at larva stage was much higher than that in other periods. In shell notch experiment,
BMP7
b showed increasing expression level after 24 h. These results indicate that
BMP7
b may play an important role in process of shell formation and repairment.