TY - JOUR
T1 - Interaction between major histocompatibility complex antigens and epidermal growth factor receptors on human cells
AU - Schreiber, A. B.
AU - Schlessinger, J.
AU - Edidin, M.
PY - 1984
Y1 - 1984
N2 - It has been suggested that products of the major histocompatibility complex, the MHC, of vertebrates function in many processes of recognition and ligand binding at the cell surface. Here we show that binding of polyclonal and monoclonal antibodies against human MHC antigens, HLA, reduced the binding of epidermal growth factor (EGF) to its membrane receptors on A-431 tumor cells and on normal human fibroblasts. Binding of EGF at 37°C similarly inhibited the binding of Fab fragments and intact Ig anti-HLA to human cells. The inhibitory effect of anti-HLA antibodies was rapid and dependent upon temperature and antibody concentration and valence. Fluorescence microscopy qualitatively confirmed the binding data and showed that MHC antigens and EGF-receptors do not co-cluster in the membrane.
AB - It has been suggested that products of the major histocompatibility complex, the MHC, of vertebrates function in many processes of recognition and ligand binding at the cell surface. Here we show that binding of polyclonal and monoclonal antibodies against human MHC antigens, HLA, reduced the binding of epidermal growth factor (EGF) to its membrane receptors on A-431 tumor cells and on normal human fibroblasts. Binding of EGF at 37°C similarly inhibited the binding of Fab fragments and intact Ig anti-HLA to human cells. The inhibitory effect of anti-HLA antibodies was rapid and dependent upon temperature and antibody concentration and valence. Fluorescence microscopy qualitatively confirmed the binding data and showed that MHC antigens and EGF-receptors do not co-cluster in the membrane.
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U2 - 10.1083/jcb.98.2.725
DO - 10.1083/jcb.98.2.725
M3 - Article
C2 - 6319431
AN - SCOPUS:0021327659
SN - 0021-9525
VL - 98
SP - 725
EP - 731
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 2
ER -