Receptor remodeling and regulation in the action of epidermal growth factor

Epidermal growth factor (EGF) initiates a wide variety of events when added to responsive cultured cells. These range from early events requiring only brief exposure to EGF, e.g., stimulation of transport of amino acids or ions, to later events such as commitment of cells to a round of DNA synthesis...

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Bibliographic Details
Published inFederation proceedings Vol. 41; no. 13; p. 2988
Main Authors Fox, C F, Linsley, P S, Wrann, M
Format Journal Article
LanguageEnglish
Published United States 01.11.1982
Subjects
Animals
Cell Division
Cells, Cultured
DNA Replication
Epidermal Growth Factor - physiology
Macromolecular Substances
Mice
Models, Biological
Molecular Weight
Peptide Hydrolases - metabolism
Phosphorylation
Receptor, Epidermal Growth Factor
Receptors, Cell Surface - physiology
Time Factors
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Summary:Epidermal growth factor (EGF) initiates a wide variety of events when added to responsive cultured cells. These range from early events requiring only brief exposure to EGF, e.g., stimulation of transport of amino acids or ions, to later events such as commitment of cells to a round of DNA synthesis, a process requiring 6 h or more of continuous exposure to hormone. EGF binding is followed first by phosphorylation of EGF receptors, which can be detected in purified membranes and permeabilized cells, and then by internalization and proteolytic processing of receptors in lysosomes. Native 160,000-dalton EGF receptors contain a site that is not exposed on the cell surface and is highly sensitive to cleavage by an endogenous protease, which yields a 145,000-dalton receptor fragment that retains phosphate acceptor activity. Cleavage of receptor at a trypsin-sensitive site, also not exposed to the cell surface, yields a 115,000-dalton fragment that binds EGF, but contains no phosphorylated species. The data indicate that the phosphate acceptor sites on EGF receptors are localized on a 45,000-dalton cytosolic region.
ISSN:0014-9446