TY - JOUR
T1 - Monoclonal antibody against epidermal growth factor receptor is internalized without stimulating receptor phosphorylation
AU - Sunada, H.
AU - Magun, B. E.
AU - Mendelsohn, J.
AU - MacLeod, C. L.
PY - 1986
Y1 - 1986
N2 - The down-regulation and internalization of the epidermal growth factor (EGF) receptors induced by two separate anti-EGF monoclonal antibodies (mAbs), IgG1 mAb-225 and -455, and by EGF was examined. mAb-225 competitively inhibits EGF binding and it is internalized to an extent comparable to EGF. The antibody down-regulates surface EGF receptors in a dose-dependent manner. In contrast, mAb-455 does not competitively inhibit the binding of EGF or mAb-225, but it specifically immunoprecipitates the EGF receptor. mAb-455 also down-regulates the EGF receptor. Unlike EGF, which elicits phosphorylation of the receptor at tyrosine, threonine, and serine residues, neither of these antibodies elicits phosphorylation of the EGF receptor in intact A431 cells or in KB cells. Our studies suggest that EGF-stimulated phosphorylation of the receptor is not required for the internalization of the ligand-receptor complex.
AB - The down-regulation and internalization of the epidermal growth factor (EGF) receptors induced by two separate anti-EGF monoclonal antibodies (mAbs), IgG1 mAb-225 and -455, and by EGF was examined. mAb-225 competitively inhibits EGF binding and it is internalized to an extent comparable to EGF. The antibody down-regulates surface EGF receptors in a dose-dependent manner. In contrast, mAb-455 does not competitively inhibit the binding of EGF or mAb-225, but it specifically immunoprecipitates the EGF receptor. mAb-455 also down-regulates the EGF receptor. Unlike EGF, which elicits phosphorylation of the receptor at tyrosine, threonine, and serine residues, neither of these antibodies elicits phosphorylation of the EGF receptor in intact A431 cells or in KB cells. Our studies suggest that EGF-stimulated phosphorylation of the receptor is not required for the internalization of the ligand-receptor complex.
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U2 - 10.1073/pnas.83.11.3825
DO - 10.1073/pnas.83.11.3825
M3 - Article
C2 - 2424012
AN - SCOPUS:0008486660
SN - 0027-8424
VL - 83
SP - 3825
EP - 3829
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 11
ER -