Biofunctional polystyrene derivatives exhibit a high affinity for the epidermal growth factor-receptor (EGF-R): Part I

1996 ◽  
Vol 7 (2) ◽  
pp. 103-107 ◽  
Author(s):  
R. Siali ◽  
J. Correia ◽  
G. Pavon-Djavid ◽  
M. Jozefowicz
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
High Affinity ◽  
Epidermal Growth

scholarly journals High affinity nanobodies against human epidermal growth factor receptor selected on cells byE. colidisplay

mAbs ◽  
2016 ◽  
Vol 8 (7) ◽  
pp. 1286-1301 ◽  
Author(s):  
Valencio Salema ◽  
Carmen Mañas ◽  
Lidia Cerdán ◽  
Carlos Piñero-Lambea ◽  
Elvira Marín ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Human Epidermal Growth Factor ◽  
High Affinity ◽  
Epidermal Growth

scholarly journals Thermodynamic mixing of molecular states of the epidermal growth factor receptor modulates macroscopic ligand binding affinity

2000 ◽  
Vol 352 (1) ◽  
pp. 99-108 ◽  
Author(s):  
Michael R. HOLBROOK ◽  
Linda L. SLAKEY ◽  
David J. GROSS
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Dissociation Constant ◽  
Growth Factor Receptor ◽  
Affinity Binding ◽  
Binding Studies ◽  
High Affinity Binding ◽  
High Affinity ◽  
Epidermal Growth

The epidermal growth factor receptor (EGFr), when expressed on the cell surface, has long been known to display two distinct affinities for epidermal growth factor (EGF) binding. In addition, the treatment of cells expressing the EGFr with phorbol esters has been shown to cause a loss of the high-affinity binding capacity of the receptor. In the present study, point mutations that alter acidic or phosphorylation sites have been made in an intracellular domain near Tyr-992 (residues 988–992) of the EGFr. Equilibrium 125I-EGF binding studies demonstrate that the conversion of Tyr-992 into glutamate induces a 4-fold decrease in the EGFr apparent low-affinity dissociation constant, whereas the mutation of two acidic residues, Asp-988 and Glu-991, or the conversion of Tyr-992 into phenylalanine does not alter EGFr affinity. Phorbol ester treatment of EGFr-expressing Chinese hamster ovary cells results in a loss of high-affinity binding and an increase in the apparent low-affinity dissociation constant of the receptor, similar to the effect of a truncation mutant in which the C-terminal 190 residues are deleted. These results are examined in the context of a new model for regulation of the affinity of the EGFr for EGF in which a cytosolic particle stabilizes the high-affinity conformation of the EGFr and a rapid equilibrium exists between EGFr high-affinity and low-affinity conformations. This model demonstrates that the macroscopic affinities of the EGFr can differ from the affinities of individual EGFr molecules and provides a theoretical framework whereby the measured affinities of the EGFr are modulated by intracellular interactions.

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