ABSTRACT
AIM: To investigate the physiological function of the novel serine protease SNC19 protein and its possible role in cancer invasion and metastasis. METHODS: Monoclonal antibodies directly against SNC19 extracellular domain was prepared. The protein and SNC19 mRNA expression were determined in different kinds of cell lines respectively by Western blot and Northern blot analysis. Cellular migration and adhesion abilities were assayed by monoclonal antibody blocking method. RESULTS: Western blot analysis showed there were two bands of SNC19 protein in BCAP37, COLO205, SW480 cells at about 120 kD and 60 kD while only one band in SW620 cells at 60 kD; Northern blots showed a approximate 3.4-kilobase fragment appearing in most epithelial-derived cell lines with this only form and high levels but no detection was obtained in OV, TCA8113, KB and SGC7901 cells. In antibody blocking experiments, the migration of SW480 cells was significantly inhibited compared with the control and the abilities of (SW480/SW480), SW480/NIH3T3 adhesion increased at the beginning of the experiments, but the difference reduced (along) with the time passed.CONCLUSION: SNC19 protein is closely related with cellular homogeneous and heterogeneous adhesion as well as cellular motility. As a novel serine protease, it may participate both in physiological and pathological processes, such as cell migration, tissue remodeling and cancer invasion and metastasis.