TY - JOUR
T1 - A Mr=190,000 glycoprotein phosphorylated on tyrosine residues in epidermal growth factor stimulated KB cells is the product of the C-erbB-2 gene
AU - Kadowaki, Takashi
AU - Kasuga, Masato
AU - Tobe, Kazuyuki
AU - Takaku, Fumimaro
AU - Nishida, Eisuke
AU - Sakai, Hikoichi
AU - Koyasu, Shigeo
AU - Yahara, Ichiro
AU - Toyoshima, Kumao
AU - Yamamoto, Tadashi
AU - Akiyama, Tetsu
N1 - Funding Information:
ACKNOWLEDGEMENTS: We thank Dr. T. Kawamoto (Department of Biochemistry, Okayama University Dental School, Okayama) for kind gift of monoclonal antibody to EGF receptor (528 IgG), and Ms. E. Abe and F. Sameshima for excellent technical assistance. This work has been supported by Grants-in-Aid from the Ministry of Education, Science and Culture of Japan.
PY - 1987/4/29
Y1 - 1987/4/29
N2 - In human epidermoid carcinoma KB cells, a glycoprotein of Mr=190,000 (gp190) has been shown to be phosphorylated on tyrosine residues upon EGF stimulation (Kadowaki et al., 1987, J. Biol. Chem. in press). Using a specific antibody to the c-terminal portion of the human c-erbB-2 gene product, we have found that gp190 is the human c-erbB-2 gene product which is structurally closely related to the epidermal growth factor (EGF) receptor. Since monoclonal antibody specific for the EGF receptor abolished both EGF binding to its receptor and tyrosine phosphorylation of the c-erbB-2 gene product, we have concluded that activation of EGF receptor tyrosine kinase activity upon EGF binding leads to the phosphorylation of the c-erbB-2 gene product on its tyrosine residues.
AB - In human epidermoid carcinoma KB cells, a glycoprotein of Mr=190,000 (gp190) has been shown to be phosphorylated on tyrosine residues upon EGF stimulation (Kadowaki et al., 1987, J. Biol. Chem. in press). Using a specific antibody to the c-terminal portion of the human c-erbB-2 gene product, we have found that gp190 is the human c-erbB-2 gene product which is structurally closely related to the epidermal growth factor (EGF) receptor. Since monoclonal antibody specific for the EGF receptor abolished both EGF binding to its receptor and tyrosine phosphorylation of the c-erbB-2 gene product, we have concluded that activation of EGF receptor tyrosine kinase activity upon EGF binding leads to the phosphorylation of the c-erbB-2 gene product on its tyrosine residues.
UR - http://www.scopus.com/inward/record.url?scp=0023226122&partnerID=8YFLogxK
U2 - 10.1016/S0006-291X(87)80021-9
DO - 10.1016/S0006-291X(87)80021-9
M3 - 学術論文
C2 - 2437918
AN - SCOPUS:0023226122
SN - 0006-291X
VL - 144
SP - 699
EP - 704
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -