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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 orcid ; 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
; ; and
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
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}},
}