Antibody-induced activation of the epidermal growth factor receptor tyrosine kinase requires the presence of detergent

• Published in: Biochemical and biophysical research communications Vol. 171; no. 2; pp. 882 - 889
• Main Authors: Spaargaren, Marcel, Defize, Libert H.K., de Laat, Siegfried W., Boonstra, Johannes
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 14.09.1990; Elsevier
• Subjects: Analytical, structural and metabolic biochemistry; Antibodies; Biological and medical sciences; Cell Line; Cell Membrane - enzymology; Detergents - pharmacology; Enzyme Activation; Enzymes and enzyme inhibitors; ErbB Receptors - immunology; ErbB Receptors - metabolism; Fundamental and applied biological sciences. Psychology; Humans; Kinetics; Phosphorylation; Polyethylene Glycols - pharmacology; protein-tyrosine kinase; Protein-Tyrosine Kinases - immunology; Protein-Tyrosine Kinases - metabolism; Surface-Active Agents - pharmacology; Transferases; Autophosphorylation; Immunoprecipitation reaction; Detergent; Epidermal growth factor; Cell line; Antibody; Plasma membrane; Activation; Protein-tyrosine kinase; Biological receptor
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(90)91228-K

Activation of the epidermal growth factor receptor (EGF-R) tyrosine kinase was investigated in membrane preparations as well as intact A431 cells, using anti-EGF-R antibodies directed against extra- and intracellular receptor domains. In vitro assay conditions were mimicked on whole cells by a mild detergent treatment. We show that, irrespective of the recognition site on the EGF-R, antibodies induce EGF-R autophosphorylation and tyrosine kinase activity towards other endogenous and exogenous substrates, but only when detergent is present. We propose that the primary effect of detergent is to create conditions in the lipid environment of the EGF-R that allow antibodies to induce receptor-receptor interactions necessary for tyrosine kinase activation.