Interaction of urokinase-type plasminogenactivator (u-PA) with its cellular receptor (u-PAR) induces phosphorylation on tyrosine of a 38 kDa protein

I Dumler; T Petri; W D Schleuning

doi:10.1016/0014-5793(93)81106-a

Interaction of urokinase-type plasminogenactivator (u-PA) with its cellular receptor (u-PAR) induces phosphorylation on tyrosine of a 38 kDa protein

FEBS Lett. 1993 May 3;322(1):37-40. doi: 10.1016/0014-5793(93)81106-a.

Authors

I Dumler¹, T Petri, W D Schleuning

Affiliation

¹ Research Laboratories of Schering AG, Berlin, Germany.

PMID: 8387028
DOI: 10.1016/0014-5793(93)81106-a

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

Research Support, Non-U.S. Gov't

MeSH terms

Chromatography, Affinity
Electrophoresis, Polyacrylamide Gel
Neoplasm Proteins / metabolism*
Phosphorylation
Precipitin Tests
Receptors, Cell Surface / isolation & purification
Receptors, Cell Surface / metabolism*
Receptors, Urokinase Plasminogen Activator
Tumor Cells, Cultured
Tyrosine / metabolism*
Urokinase-Type Plasminogen Activator / metabolism*

Substances

Neoplasm Proteins
Receptors, Cell Surface
Receptors, Urokinase Plasminogen Activator
Tyrosine
Urokinase-Type Plasminogen Activator