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Phosphorylation of a 72-kDa protein in PDGF-stimulated cells which forms complex with c-Crk, c-Fyn and Eps15

Author

Summary, in English

Ligand-induced activation of the beta-receptor for platelet-derived growth factor (PDGF) induces tyrosine phosphorylation of a number of downstream signaling proteins. In the present study, we used two-dimensional gel electrophoresis to characterize the spectrum of proteins phosphorylated in response to PDGF stimulation in porcine aortic endothelial cells expressing PDGF beta-receptors. Several previously known substrates for the PDGF beta-receptor were identified as well as a novel substrate of 72 kDa. The 72-kDa component could be co-immunoprecipitated in complex with the adaptor protein c-Crk, the non-receptor tyrosine kinase c-Fyn and the signaling molecule Eps15. The results obtained suggests that the 72-kDa protein might play an important role in signaling via the PDGF beta-receptor, coupling non-receptor tyrosine kinases of the Src family with c-Crk and Eps15.

Publishing year

1997

Language

English

Pages

195-200

Publication/Series

FEBS Letters

Volume

409

Issue

2

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • Medicinal Chemistry

Keywords

  • Animals Aorta Calcium-Binding Proteins/chemistry/*metabolism Cells
  • Gel
  • Two-Dimensional Endothelium
  • Vascular/chemistry/cytology/*metabolism Molecular Weight Phosphoproteins/chemistry/*metabolism Phosphorylation/drug effects Platelet-Derived Growth Factor/*pharmacology Precipitin Tests Protein-Tyrosine Kinases/chemistry/metabolism Proto-Oncogene Proteins/chemistry/*metabolism Proto-Oncogene Proteins c-crk Proto-Oncogene Proteins c-fyn Swine
  • Cultured Electrophoresis

Status

Published

ISBN/ISSN/Other

  • ISSN: 1873-3468