Interaction of urokinase-type plasminogenactivator (u-PA) with its cellular receptor (u-PAR) induces phosphorylation on tyrosine of a 38 kDa protein.
We demonstrate by immunoprecipitation that u-PAR is associated with a 38 kDa protein that is phosphorylated on tyrosine after u-PA treatment of cells. As tyrosine phosphorylation is the hallmark of many signal transduction pathways that promote growth and differentiation, these data suggest that u-PA, besides its role as a regulatory protease, might act as a para- or autocrine hormone.
Research Laboratories of Schering AG, Berlin, Germany.
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I
Dumler
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T
Petri
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WD
Schleuning
D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D009363:Neoplasm Proteins / Q000378:metabolism*; D010766:Phosphorylation; D011233:Precipitin Tests; D011956:Receptors, Cell Surface / Q000302:isolation & purification / Q000378:metabolism*; D055293:Receptors, Urokinase Plasminogen Activator; D014407:Tumor Cells, Cultured; D014443:Tyrosine / Q000378:metabolism*; D014568:Urokinase-Type Plasminogen Activator / Q000378:metabolism*
D009363:Neoplasm Proteins; D011956:Receptors, Cell Surface; D055293:Receptors, Urokinase Plasminogen Activator; D014443:Tyrosine; D014568:Urokinase-Type Plasminogen Activator