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Interaction of urokinase‐type plasminogenactivator (u‐PA) with its cellular receptor (u‐PAR) induces phosphorylation on tyrosine of a 38 kDa protein
Author(s) -
Dumler I.,
Petri T.,
Schleuning W.-D.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81106-a
Subject(s) - tyrosine phosphorylation , phosphorylation , immunoprecipitation , autocrine signalling , tyrosine , signal transduction , protein tyrosine phosphatase , microbiology and biotechnology , chemistry , receptor tyrosine kinase , tyrosine kinase , receptor , biochemistry , biology , gene
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.