Cell membrane receptors for urokinase plasminogen activator are increased in malignant ovarian tumours.
The binding of 125I-labelled urokinase plasminogen activator (uPA) to cell membranes of ovarian tumours was characterised. Binding was fast, specific to HMW-uPA, and saturated at low concentration [1.5 (range 1.2-1.6) nmol/l]. Scatchard analysis suggested a single class of binding sites with Kd 1.1 (0.9-1.3) nmol/l. These data indicate the presence of a specific cell membrane receptor for uPA in ovarian tumours, whose characteristics are similar to those reported for uPA receptors in other tissues. Endogenously occupied receptors were uncovered by exposing the membranes to acid conditions (pH 2) before assay, thereby allowing quantitation of the total amount of receptor. uPA receptors were assayed in 10 malignant and 6 benign epithelial ovarian tumours. The total number of receptors was higher in the malignant tumours. This was secondary to increases of both free and occupied receptors. We conclude that this reflects the biological function of cell surface bound plasminogen activation in tumour growth and spread.
Casslén
B
B
Department of Obstetrics and Gynecology, University Hospital, University of Lund, Sweden.
Gustavsson
B
B
Astedt
B
B
D000230:Adenocarcinoma / Q000378:metabolism; D001665:Binding Sites; D001667:Binding, Competitive; D005260:Female; D006801:Humans; D008970:Molecular Weight; D010051:Ovarian Neoplasms / Q000201:enzymology*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D055293:Receptors, Urokinase Plasminogen Activator; D014568:Urokinase-Type Plasminogen Activator / Q000378:metabolism*
C524898:PLAUR protein, human; D011956:Receptors, Cell Surface; D055293:Receptors, Urokinase Plasminogen Activator; D014568:Urokinase-Type Plasminogen Activator