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Division of Neurosurgery, St. Michael's Hospital, Toronto M5B 1W8, and Department of Surgery, University of Toronto, Toronto, Canada [W. S. T.], and Division of Neurosurgery [W. M. K.] and Department of Pathology [A. M-H., L. M. F.], University of Colorado Medical Center, Denver, Colorado 80220
Cell cultures were prepared from nine human brain tumors. Fibrin plate assays showed plasminogen-dependent fibrinolytic activity in lysates and in material released by these neoplastic cells but not in those from normal adult human white matter.
Antibodies against human urokinase caused catalytic inhibition of the urokinase and of the plasminogen activator from WI-38 cells, simian virus 40-transformed WI-38 cells, human prostatic cells, and human ovarian carcinoma cells. However, the anti-urokinase immunoglobulin G did not inhibit the plasminogen activator activity of any of the human brain tumor preparations. These studies indicate that the plasminogen activator produced by human brain tumor cells is antigenically different from the plasminogen activator of other human normal and neoplastic cells.
1 This work was supported by NIH Grants CA-15823, CA-15109, and CA-13419 and American Cancer Society Grant BC-189.
2 Supported by an Irving Heward Cameron Scholarship from the University of Toronto. To whom requests for reprints should be addressed.
3 Recipient of a USPHS Research Career Development Award.
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