Type beta transforming growth factor and epidermal growth factor suppress the plasminogen activator activity in a human glioblastoma cell line

1988 ◽  
Vol 6 (3) ◽  
pp. 277-283 ◽  
Author(s):  
Eirik Helseth ◽  
Are Dalen ◽  
Geirmund Unsgaard ◽  
Randi Vik
1988 ◽  
Vol 8 (10) ◽  
pp. 4561-4565 ◽  
Author(s):  
A Wells ◽  
J M Bishop ◽  
D Helmeste

The gene encoding the receptor for epidermal growth factor was amplified two- to fivefold in the human glioblastoma cell line SF268. The amplified gene gave rise to abundant quantities of receptor that bound EGF with a high affinity (Kd, 0.35 nM). The binding of ligand failed to elicit cellular DNA synthesis, however, and the receptor was enzymatically inactive. We presume that the amplified receptor gene carries a mutation(s) that affects several aspects of the receptor's function. Characterization of the mutation(s) may illuminate how structure dictates function in the receptor protein.


1988 ◽  
Vol 8 (10) ◽  
pp. 4561-4565
Author(s):  
A Wells ◽  
J M Bishop ◽  
D Helmeste

The gene encoding the receptor for epidermal growth factor was amplified two- to fivefold in the human glioblastoma cell line SF268. The amplified gene gave rise to abundant quantities of receptor that bound EGF with a high affinity (Kd, 0.35 nM). The binding of ligand failed to elicit cellular DNA synthesis, however, and the receptor was enzymatically inactive. We presume that the amplified receptor gene carries a mutation(s) that affects several aspects of the receptor's function. Characterization of the mutation(s) may illuminate how structure dictates function in the receptor protein.


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