IMMUNOLOGICAL IDENTITY OF UROKINASE AND OVARIAN CARCINOMA PLASMINOGEN ACTIVATOR RELEASED IN TISSUE-CULTURE
IMMUNOLOGICAL IDENTITY OF UROKINASE AND OVARIAN CARCINOMA PLASMINOGEN ACTIVATOR RELEASED IN TISSUE-CULTURE
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DOI:
10.1038/261595a0
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发表时间:
1976-01-01
期刊:
影响因子:
64.8
通讯作者:
HOLMBERG, L
中科院分区:
文献类型:
--
作者:
ASTEDT, B;HOLMBERG, L
THERE is evidence that fibrinolytic enzymes are involved in the growth of tumours. It has long been known that malignant tumours in culture lyse clotted plasma substrates1–3. Davidsonet al.4found a giant-cell carcinoma of the lung to be rich in plasminogen activator and to produce it in tissue culture. Rifkinet al.5reported an abundant release of fibrinolytic enzymes by mammalian fibroblasts transformed by DNA or RNA viruses, by chemically or virally induced mammary carcinomas and by human malignant tumours in culture. Normal fibroblasts and cultures of other normal tissues released little or no fibrinolytic enzymes. Christman and Acs6found neoplastic cells, whether transformed by oncogenic viruses or by chemical agents, to release a plasminogen activator not released by normal cells. This activator was characterised as a serine protease with a molecular weight of approximately 50,000. The presence of fibrinolytic activity has been demonstrated in human ovarian tumours7as well as in ascitic fluid associated with such tumours8. We have studied a stable plasminogen-activating enzyme, released by ovarian carcinoma in tissue culture, and we report here the apparent identity of this plasminogen activator (TA) and the activator produced by foetal kidney and present in normal urine—that is, urokinase.