Antigen responsive antibody-receptor kinase chimera.
We have constructed chimeric receptors, combining murine IgM and the cytoplasmic portion of human epidermal growth factor receptor (EGFR), with the aim of developing a novel immunosensor with antigen-dependent phosphorylation activity. When intact IgM was used, the chimeric receptor showed both antigen binding and protein tyrosine kinase activity, but the kinase activity was constitutive and independent of antigen binding. However, with IgM lacking the CH2 domain, the autophosphorylation activity increased with increasing concentrations of anti-IgM or hapten-BSA conjugate. Monovalent hapten could not induce phosphorylation but inhibited stimulation by hapten-conjugated BSA.
Department of Chemical Engineering, Faculty of Engineering, University of Tokyo, Japan.
H
H
Ueda
M
M
Kikuchi
S
S
Yagi
H
H
Nishimura
D000818:Animals; D000951:Antigens, Neoplasm / Q000276:immunology*; D001483:Base Sequence; D001704:Biopolymers; D002999:Clone Cells; D066246:ErbB Receptors / Q000378:metabolism*; D005822:Genetic Vectors / Q000235:genetics; D007075:Immunoglobulin M / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D010766:Phosphorylation; D010954:Plasmacytoma / Q000378:metabolism; D010957:Plasmids / Q000235:genetics; D011233:Precipitin Tests; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D014162:Transfection / Q000235:genetics
D000951:Antigens, Neoplasm; D001704:Biopolymers; D007075:Immunoglobulin M; D011994:Recombinant Proteins; D066246:ErbB Receptors; D011505:Protein-Tyrosine Kinases