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Epidermal growth factor induces tyrosine phosphorylation of epidermal growth factor receptors not occupied with ligand in intact A431 cells. FEBS Lett 1990 Jul 30;268(1):121-4

Date

07/30/1990

Pubmed ID

1696547

DOI

10.1016/0014-5793(90)80988-u

Scopus ID

2-s2.0-0025341290 (requires institutional sign-in at Scopus site)   1 Citation

Abstract

The mechanism of epidermal growth factor receptor (EGF-R) autophosphorylation in intact A431 cells was studied. We detected epidermal growth factor (EGF) induced tyrosine phosphorylation of EGF-R not occupied with ligand. Cell monolayers were subjected to irradiation after incubation with photoreactive derivative of EGF and uncoupled EGF was extracted by acidic treatment. Subsequent immunoprecipitation with antiphosphotyrosine antibodies resulted in precipitation of both EGF-R complexes with EGF and EGF-R with unoccupied ligand-binding site. The fact of precipitation of EGF-R with unoccupied ligand-binding site in conjunction with our finding of rapid dephosphorylation of EGF-R after EGF extraction by acidic treatment, strongly supports the interpretation that cross-phosphorylation of EGF-R may take place in intact cells.

Author List

Sorokin AB, Reshetnikova GF, Kudryavtseva NV, Nikolsky NN

Author

Andrey Sorokin PhD Professor in the Medicine department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Epidermal Growth Factor
ErbB Receptors
Humans
In Vitro Techniques
Ligands
Phosphorylation
Phosphotyrosine
Tumor Cells, Cultured
Tyrosine