The role of EGF receptor transmodulation in embryonal carcinoma‐derived growth factor‐induced mitogenesis

Exposure of quiescent 10T1/2 fibroblast cells to embryonal carcinoma‐derived growth factor (ECDGF) results in a rapid temperature and ECDGF concentration‐dependent inhibition of [125I]EGF binding to the epidermal growth factor (EGF) receptor (transmodulation). ECDGF predominantly inhibits the associ...

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Bibliographic Details
Published inThe EMBO journal Vol. 5; no. 8; pp. 1809 - 1814
Main Authors Heath, J.K., Mahadevan, L., Foulkes, J.G.
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group 01.08.1986
Subjects
Animals
Biological and medical sciences
Cell physiology
Cells, Cultured
Epidermal Growth Factor - metabolism
Epidermal Growth Factor - pharmacology
ErbB Receptors - drug effects
ErbB Receptors - physiology
Fibroblasts - cytology
Fibroblasts - drug effects
Fundamental and applied biological sciences. Psychology
Growth Substances - pharmacology
Kinetics
Mice
Mice, Inbred C3H
Molecular and cellular biology
Peptides
Phosphorylation
Responses to growth factors, tumor promotors, other factors
Tetradecanoylphorbol Acetate - pharmacology
Epidermal growth factor
Molecular interaction
Mitogen
Mechanism of action
Biological activity
Embryonal carcinoma
Growth factor
Biological receptor
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Summary:Exposure of quiescent 10T1/2 fibroblast cells to embryonal carcinoma‐derived growth factor (ECDGF) results in a rapid temperature and ECDGF concentration‐dependent inhibition of [125I]EGF binding to the epidermal growth factor (EGF) receptor (transmodulation). ECDGF predominantly inhibits the association of [125I]EGF with a high affinity subclass of EGF receptors, and induces increased phosphorylation of the EGF receptor on serine and threonine residues. No mitogenic effect of EGF can be detected in the presence of ECDGF concentrations which induce maximal EGF receptor transmodulation. ECDGF‐induced EGF receptor transmodulation is sensitive to phorbol ester‐induced desensitization whereas ECDGF‐induced DNA synthesis is unaffected by prolonged pre‐treatment with biologically active phorbol ester. These findings suggest that EGF receptor transmodulation is not essential for ECDGF mitogenicity but may inhibit EGF‐induced DNA synthesis.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1986.tb04430.x