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Receptor for plasmin on human carcinoma cells.

We have shown that cells from human tumor cell line SW 1116 have receptors for plasmin and plasminogen. These receptors are the same for the proenzyme and the enzyme, but they have a much higher affinity for plasmin (Kd = 6 X 10(-8) M) than for plasminogen (Kd = 5 X 10(-6) M). Plasminogen binding was strongly increased by preincubation of the tumor cells with urokinase and was inhibited by anti-urokinase serum. Because free plasmin is rapidly neutralized in vivo, it is likely that, under physiological conditions, plasminogen is bound by tumor cells and partially transformed into plasmin by urokinase already present at the surface of these cells. Bound plasmin retains its enzymatic activity, which demonstrates that its binding does not involve the enzyme's active site.