Molecular characterization of myostatin-like genes expressed highly in the muscle tissue from Morotoge shrimp, Pandalopsis japonica

Myostatin is one of the transforming growth factor (TGF)-beta family members and plays inhibitory roles in the development and growth of muscle in mammals. Mammalian myostatins have been studied intensively, considering its medical and industrial potential use. Still, limited information is available about myostatin homologues in crustaceans. In the present study, we isolated for the first time cDNA that encodes for myostatin-like protein (Pj-MSTN) from Morotoge shrimp, Pandalopsis japonica. The putative mature peptide of Pj-MSTN was composed of 109 amino acids, which contains an additional amino acid residue compared with mammalian myostatins. Pj-MSTN exhibited 32% amino acid sequence identity and 52% similarity to human myostatin. Multiple sequence alignment analysis indicated that Pj-MSTN shared the conserved proteolytic cleavage site (RXXR) for its maturation and nine cysteine residues for disulphide bridges. These results suggest that Pj-MSTN has conserved the three-dimensional structure of TGF-beta family members in vertebrates. Phylogenetic analysis suggests that Pj-MSTN is a primitive form of vertebrate myostatin and GDF11. The expression of Pj-MSTN was not just identified in muscular tissues, suggesting that Pj-MSTN functions differently from mammalian myostatin. Ablation of the X-organ/sinus gland complex significantly reduced the expression of Pj-MSTN in most tissues, suggesting its potential association with moulting.