Phosphorylation of a 72-kDa protein in PDGF-stimulated cells which forms complex with c-Crk, c-Fyn and Eps15
(1997) In FEBS Letters 409(2). p.195-200- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1783929
- author
- Hansen, Klaus ; Rönnstrand, Lars LU ; Claesson-Welsh, Lena and Heldin, Carl-Henrik
- publishing date
- 1997
- type
- Contribution to journal
- publication status
- published
- subject
- 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
- in
- FEBS Letters
- volume
- 409
- issue
- 2
- pages
- 195 - 200
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:0342618377
- ISSN
- 1873-3468
- DOI
- 10.1016/S0014-5793(97)00495-X
- language
- English
- LU publication?
- no
- additional info
- 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)
- id
- 3b4d576b-91cf-4ef2-9001-a4817bfc9c7c (old id 1783929)
- date added to LUP
- 2016-04-04 09:13:45
- date last changed
- 2022-01-29 08:55:17
@article{3b4d576b-91cf-4ef2-9001-a4817bfc9c7c, 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.}}, author = {{Hansen, Klaus and Rönnstrand, Lars and Claesson-Welsh, Lena and Heldin, Carl-Henrik}}, issn = {{1873-3468}}, 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}}, language = {{eng}}, number = {{2}}, pages = {{195--200}}, publisher = {{Wiley-Blackwell}}, series = {{FEBS Letters}}, title = {{Phosphorylation of a 72-kDa protein in PDGF-stimulated cells which forms complex with c-Crk, c-Fyn and Eps15}}, url = {{http://dx.doi.org/10.1016/S0014-5793(97)00495-X}}, doi = {{10.1016/S0014-5793(97)00495-X}}, volume = {{409}}, year = {{1997}}, }