Abstract
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.
Original language | English |
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Pages (from-to) | 195-200 |
Journal | FEBS Letters |
Volume | 409 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1997 |
Externally published | Yes |
Bibliographical note
The information about affiliations in this record was updated in December 2015.The record was previously connected to the following departments: Experimental Clinical Chemistry (013016010)
Subject classification (UKÄ)
- Medicinal Chemistry
Free 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