Matsuo O, Fukao H, Matsuo C, Ueshima S
Department of Physiology, Kinki University School of Medicine, Osakasayama, Japan.
Thromb Res Suppl. 1988;8:45-55. doi: 10.1016/0049-3848(88)90153-3.
An established cell line (OC-1) was obtained from human ovarian tissue, which yielded a high concentration of plasminogen activator (PA) in the culture medium. The PA (OC-1-PA) produced by the cell line was purified and compared with urokinase (u-PA), proform of UK (scu-PA), and tissue-type PA (t-PA) purified from human melanoma cells (Bowes). OC-1-PA was purified by Zn chelate-Sepharose affinity chromatography followed by high performance liquid chromatography with a Zn chelate-5PW column and with a p-aminobenzamidine-5PW column, giving a yield of 58.3% and a purification factor of 15,439. This purified material revealed a single band of Mr 55,000 on sodium dodecylsulfate polyacrylamide gel electrophoresis in the presence or absence of reducing agents. Electrophoretic enzymography demonstrated that the Mr 55,000 protein band had a plasminogen-dependent fibrinolytic activity. Treatment with plasmin did not change the Mr even in the presence of reducing agents. These results suggest that OC-1-PA has a single-chain structure protected from protease degradation, which is completely different from UK. The activator had higher affinities for lysine and fibrin than those of u-PA or scu-PA. An immunological study demonstrated that OC-1-PA cross-reacted with anti-u-PA IgG but not with anti-t-PA IgG. All these findings indicate that OC-1-PA belongs immunologically to the u-PA type, but its structure differs from that of u-PA.
