Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Chromatography, Affinity
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Electrophoresis, Polyacrylamide Gel
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Neoplasm Proteins / metabolism*
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Phosphorylation
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Precipitin Tests
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Receptors, Cell Surface / isolation & purification
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Receptors, Cell Surface / metabolism*
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Receptors, Urokinase Plasminogen Activator
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Tumor Cells, Cultured
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Tyrosine / metabolism*
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Urokinase-Type Plasminogen Activator / metabolism*
Substances
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Neoplasm Proteins
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Receptors, Cell Surface
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Receptors, Urokinase Plasminogen Activator
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Tyrosine
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Urokinase-Type Plasminogen Activator