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Examines the activation of the native Glu-plasminogen by tissue-type plasminogen activator (t-PA) in the presence of prostromelysin-1. Enhancement of the catalytic efficiency of two chain t-PA; Use of bispecific interaction analysis; Affinity of plasminogen.

Investigates the functional property of a recombinant chimeric protein with combined thrombin inhibitory and plasminogen-activating potential. Specific activity of the chimera; Fibrinolytically active concentration in a plasma medium required for thrombin inhibition.

The synthesis of plasminogen activators and inhibitors in endothelial cells is highly regulated by hormones, drugs and growth factors. The present study evaluates the effector of retinoic on the synthesis of tissue-type plasminogen activator (t-PA) and of plasminogen activator inhibitor-1 (PAI-1) by cultured human umbilical vein endothelial cells (HUVEC). Retinoic acid produced a time- and concentration-dependent increase in the secretion of t-PA-related antigen but not of PAI-1 related antigen into the culture medium. A maximal sevenfold increase of t-PA antigen after 24 h was observed with 10 μM and a half-maximal increase with 0.1 μM retinoic acid. Retinoic acid induced a time-dependent increase of the t-PA mRNA, with a maximum at 8 h and returning to normal at 24 h. The protein kinase inhibitor H7 decreased the t-PA antigen induced by both retinoic acid and phorbol 12-myristate 13-acetate. These results suggest that treatment of HUVEC with retinoic acid increases t-PA synthesis in the absence of altered PAI-1 synthesis, which may enhance the fibrinolytic potential of the endothelium. [ABSTRACT FROM AUTHOR]