Abstract 2427: Overexpression of insulin/IGF hybrid receptor as predictive biomarker of response to a humanized anti-insulin like growth factor-I receptor monoclonal antibody (CP751,871) in gastric and hepatocellular carcinoma cells

2010 ◽  
Author(s):  
Jun-Gyu Kim ◽  
Hwang Phill Kim ◽  
Young Kwang Yoon ◽  
Sae Won Han ◽  
Seock-Ah Im ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Monoclonal Antibody ◽  
Growth Factor ◽  
Predictive Biomarker ◽  
Carcinoma Cells ◽  
Insulin Like Growth Factor ◽  
Hepatocellular Carcinoma Cells ◽  
Factor I ◽  
Growth Factor I ◽  
Receptor Monoclonal Antibody

scholarly journals Akt/mTOR Counteract the Antitumor Activities of Cixutumumab, an Anti-Insulin–like Growth Factor I Receptor Monoclonal Antibody

2011 ◽  
Vol 10 (12) ◽  
pp. 2437-2448 ◽  
Author(s):  
Dong Hoon Shin ◽  
Hye-Young Min ◽  
Adel K. El-Naggar ◽  
Scott M. Lippman ◽  
Bonnie Glisson ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Growth Factor ◽  
Insulin Like Growth Factor ◽  
Antitumor Activities ◽  
Factor I ◽  
Growth Factor I ◽  
Receptor Monoclonal Antibody

Insulin-like Growth Factor I Receptor: A Novel Target for Hepatocellular Carcinoma Gene Therapy

2019 ◽  
Vol 19 (4) ◽  
pp. 272-280 ◽  
Author(s):  
Li Wang ◽  
Min Yao ◽  
Wenjie Zheng ◽  
Miao Fang ◽  
Mengna Wu ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Gene Therapy ◽  
Growth Factor ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Growth Factor I ◽  
Novel Target

A monoclonal antibody to human insulin-like growth factor-I: characterization, use in radioimmunoassay and effect on the biological activities of the growth factor

1989 ◽  
Vol 2 (3) ◽  
pp. 201-206 ◽  
Author(s):  
D. J. Morrell ◽  
H. Dadi ◽  
J. More ◽  
A. M. Taylor ◽  
A. Dabestani ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Growth Factor ◽  
Binding Site ◽  
Biological Activities ◽  
Rabbit Antiserum ◽  
Affinity Constant ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Igf I ◽  
Growth Factor I

ABSTRACT A monoclonal antibody (BPL-M23) to insulin-like growth factor-I (IGF-I) was obtained following immunization of BALB/c mice with human IGF-I conjugated to ovalbumin. The affinity constant of BPL-M23 for IGF-I was 10·5 litres/nmol and the cross-reactivities of IGF-II, multiplication-stimulating activity III-2 and insulin were 08, 003 and less than 0·0001 % respectively. Porcine, bovine, ovine and rabbit sera, but not rat or mouse sera, showed substantial reactivity with the antibody. Comparison of radioimmunoassay analyses of 54 human serum samples from normal subjects and acromegalic and GH-deficient patients using BPL-M23 and a polyclonal rabbit antiserum (R557A) to human IGF-I showed a high correlation, indicating the usefulness of the monoclonal antibody in radioimmunoassay. Monoclonal antibody BPL-M23 was capable of abolishing the sulphation, mitogenic and insulin-like activities of IGF-I in in-vitro bioassays, suggesting that these activities may rely upon the same receptor-binding site which is near to the antibody-binding site.

scholarly journals Purified hybrid insulin/insulin-like growth factor-I receptors bind insulin-like growth factor-I, but not insulin, with high affinity

1993 ◽  
Vol 290 (2) ◽  
pp. 419-426 ◽  
Author(s):  
M A Soos ◽  
C E Field ◽  
K Siddle
Keyword(s):  
Monoclonal Antibody ◽  
Growth Factor ◽  
Insulin Receptors ◽  
Beta Subunit ◽  
Type I ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Igf Receptors ◽  
Igf I ◽  
Growth Factor I

Hybrid insulin/insulin-like growth factor-I (IGF-I) receptors have previously been described in human placenta, but it has not been possible to study their properties in the presence of classical insulin receptors and type I IGF receptors. To facilitate the purification of hybrids, we produced an anti-peptide monoclonal antibody IGFR 1-2, directed against the C-terminal peptide of the type I IGF receptor beta-subunit. The antibody bound native human and rat type I IGF receptors, and reacted specifically with the beta-subunit on immunoblots. Solubilized placental microsomal membranes were depleted of classical type I IGF receptors by incubation with an immobilized monoclonal antibody IGFR 24-55, which reacts well with type I receptors but very poorly with hybrid receptors. Residual hybrid receptors were then isolated by incubation with immobilized antibody IGFR 1-2, and recovered by elution with excess of synthetic peptide antigen. Binding properties of hybrids were compared with those of immuno-affinity-purified insulin receptors and type I IGF receptors, by using the radioligands 125I-IGF-I and 125I-insulin. Hybrids bound approx. 20 times as much 125I-IGF-I as 125I-insulin at tracer concentrations (approx. 0.1 nM). The binding of 125I-insulin, but not 125I-IGF-I, to hybrids increased after treatment with dithiothreitol to reduce disulphide bonds between the alpha-subunits. Hybrids behaved very similarly to type I receptors with respect to the inhibition of 125I-IGF-I binding by unlabelled IGF-I and insulin. By contrast, the affinity of hybrids for insulin was approx. 10-fold lower than that of classical insulin receptors, as assessed by inhibition of 125I-insulin binding by unlabelled hormone. It is concluded that the properties of insulin receptors, but not IGF receptors, are markedly affected by assembly as hybrid compared with classical structures, and that hybrids are more likely to be responsive to IGF-I than insulin under physiological conditions.

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