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JNCI Journal of the National Cancer Institute 1988 80(10):762-765; doi:10.1093/jnci/80.10.762
© 1988 by Oxford University Press
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Journal of the National Cancer Institute, Vol. 80, No. 10, 762-765, July 20, 1988
© 1988 Oxford University Press

Receptor for Plasmin on Human Carcinoma Cells1

Pierre Burtin2, Marie-Claude Fondaneche2,3

2Laboratoire d'Immunochimie, ER 277 Centre National de la Recherche Scientifique, I.R.S.C., B.P. 8, 94802 Villejuif Cédex France.

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. [J Natl Cancer Inst 1988;80:762–765]


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