Molecular cloning and tissue distribution of hyaluronan binding protein 2 (HABP2) in red sea bream Pagrus major.

Previously we have isolated a novel gelatinolytic serine proteinase, named G1, from the muscle and the plasma of red sea bream. In order to clarify the structure and function of G1, we cloned the full-length cDNA of G1 from the hepatopancreas of red sea bream. G1 cDNA encoded 633 amino acids with a secretory signal sequence at N-terminus, three epidermal growth factor-like domains, a kringle domain, and a trypsin-like serine protease domain. The active site residues of a serine proteinase were conserved in the serine protease domain of G1. The tissue distributions of the mRNA and gelatinolytic activity of G1 were investigated using RT-PCR and gelatin zymography, respectively. Its activity was detected in various tissues while the mRNA of it was strongly expressed in the hepatopancreas. These results suggest that G1 is synthesized in hepatopancreas and carried to the muscle, kidney, heart and ovary via the bloodstream in the red sea bream. The enzyme has a similar domain structure and tissue distribution to those of human hyaluronan binding protein 2 (HABP2) engaged in the extracellular matrix (ECM) turnover. Thus, it is suggested that G1 is identified as HABP2 and is possibly involved in ECM proteolysis of red sea bream.