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

Hansen, Klaus; Rönnstrand, Lars LU ; Claesson-Welsh, Lena and Heldin, Carl-Henrik (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)
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author
publishing date
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
id
3b4d576b-91cf-4ef2-9001-a4817bfc9c7c (old id 1783929)
date added to LUP
2011-02-07 15:55:02
date last changed
2017-01-01 07:44:57
@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},
  keyword      = {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},
  volume       = {409},
  year         = {1997},
}