scholarly journals Epidermal growth factor receptor in ovarian tumours: correlation of immunohistochemistry with ligand binding assay

1992 ◽  
Vol 66 (6) ◽  
pp. 1015-1021 ◽  
Author(s):  
SC Henzen-Logmans ◽  
EMJJ Berns ◽  
JGM Klijn ◽  
MEL van der Burg ◽  
JA Foekens
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Ligand Binding ◽  
Binding Assay ◽  
Growth Factor Receptor ◽  
Ligand Binding Assay ◽  
Ovarian Tumours ◽  
Epidermal Growth

Ligand binding induces a conformational change in epidermal growth factor receptor dimers

2012 ◽  
Vol 30 (6) ◽  
pp. 394-409 ◽  
Author(s):  
Francesca Walker ◽  
Julie Rothacker ◽  
Christine Henderson ◽  
Edouard C. Nice ◽  
Bruno Catimel ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Ligand Binding ◽  
Conformational Change ◽  
Growth Factor Receptor ◽  
Epidermal Growth ◽  
Receptor Dimers

Radioligand binding assay of epidermal growth factor receptor: causes of variability and standardization of the assay

1990 ◽  
Vol 36 (6) ◽  
pp. 849-854 ◽  
Author(s):  
R Dittadi ◽  
M Gion ◽  
A Brazzale ◽  
G Bruscagnin
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Membrane Fraction ◽  
Binding Assay ◽  
Radioligand Binding ◽  
Growth Factor Receptor ◽  
Nuclear Fraction ◽  
Radioligand Binding Assay ◽  
Epidermal Growth

Abstract Although experimental evidence indicates a probable role of epidermal growth factor receptor (EGFr) in clinical oncology, no standardized method for its determination has been yet described, and discrepant results have been reported in clinical studies. In standardizing a radioligand binding assay for EGFr, we evaluated the causes of variability in each step of the assay. Entrapment of EGFr in the nuclear fraction and contamination of the crude membrane fraction by cytosol protein were eliminated through preliminary purification steps. Both Scatchard and Rosenthal analysis of the saturation reaction of the membrane fraction with a wide range of concentrations of 125I-labeled EGF revealed a double class of binding sites. Study of the saturation reaction showed a partial exchange of 125I-labeled EGF with endogenous EGF within 20 h. The present method--incubation of partly purified membrane fraction with 125I-labeled EGF, 0.5 nmol/L, with and without 100-fold excess of cold EGF, for 20 h at 26 degrees C, followed by centrifugation at 5000 x g for 30 min to separate membrane-bound 125I-labeled EGF--shows good sensitivity, precision, and accuracy; is reasonably simple; and may be suitable for routine clinical use.

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