Mapping surface structures of the human insulin receptor with monoclonal antibodies: localization of main immunogenic regions to the receptor kinase domain

Biochemistry ◽  
1986 ◽  
Vol 25 (6) ◽  
pp. 1364-1371 ◽  
Author(s):  
David O. Morgan ◽  
Richard A. Roth
1985 ◽  
Vol 13 (1) ◽  
pp. 95-96
Author(s):  
MARIA SOOS ◽  
MICHAEL D. BARON ◽  
KENNETH SIDDLE

1986 ◽  
Vol 235 (1) ◽  
pp. 199-208 ◽  
Author(s):  
M A Soos ◽  
K Siddle ◽  
M D Baron ◽  
J M Heward ◽  
J P Luzio ◽  
...  

Monoclonal antibodies for the human insulin receptor were produced following immunization of mice with IM-9 lymphocytes and/or purified placental receptor. Four separate fusions yielded 28 antibodies, all of which reacted with receptor from human placenta, liver and IM-9 cells. Some antibodies cross-reacted to varying degrees with receptor from rabbit, cow, pig and sheep, but none reacted with rat receptor. At least 10 distinct epitopes were recognized as indicated by species specificity and binding competition experiments. All of these epitopes appeared to be on extracellular domains of the receptor as shown by binding of antibodies to intact cells. In some cases the epitopes were further localized to alpha or beta subunits by immunoblotting. Several antibodies inhibited binding of 125I-insulin to the receptor, some had no effect on binding, and others enhanced the binding of 125I-insulin. It is concluded that these antibodies will be valuable probes of receptor structure and function.


1989 ◽  
Vol 17 (5) ◽  
pp. 899-899
Author(s):  
ROBERT A. ATKINSON ◽  
WAYNE J. FAIRBROTHER ◽  
BARRY A. LEVINE ◽  
JEREMY TAVARÈ ◽  
BEA CLACK ◽  
...  

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