scholarly journals Insulin-like Growth Factor-binding Protein-5 Inhibits the Growth of Human Breast Cancer Cellsin Vitroandin Vivo

2003 ◽  
Vol 278 (32) ◽  
pp. 29676-29685 ◽  
Author(s):  
Alison J. Butt ◽  
Kristie A. Dickson ◽  
Fiona McDougall ◽  
Robert C. Baxter
Keyword(s):  
Breast Cancer ◽  
Growth Factor ◽  
Human Breast Cancer ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Human Breast ◽  
Factor Binding

scholarly journals Effect of insulin-like growth factor binding protein-1 on integrin signalling and the induction of apoptosis in human breast cancer cells

1999 ◽  
Vol 22 (2) ◽  
pp. 141-150 ◽  
Author(s):  
CM Perks ◽  
PV Newcomb ◽  
MR Norman ◽  
JM Holly
Keyword(s):  
Breast Cancer ◽  
Growth Factor ◽  
Human Breast Cancer ◽  
Binding Protein ◽  
Cell Counting ◽  
Insulin Like Growth Factor ◽  
Human Breast ◽  
Integrin Receptors ◽  
Factor Binding ◽  
Induction Of Apoptosis

Interaction of epithelial cells with the extracellular matrix is mediated through integrin receptors, which transmit signals regulating cell growth, differentiation and death. Occupation of these receptors, via Arg-Gly-Asp (RGD) recognition sequences, leads to activation of focal adhesion kinase (FAK). We treated human breast cancer cell lines with RGD-containing peptides, which can disrupt integrin attachment, and investigated alterations in FAK phosphorylation, cell detachment and death. Cells grown in vitro were treated with insulin-like growth factor-binding protein-1 (IGFBP-1) and a small, synthetic RGD-containing peptide (Gly-Arg-Gly-Asp-Thr-Pro) and its negative control peptide RGE (Arg-Gly-Glu-Ser) for either 30 min followed by immunoprecipitation of cell lysates with anti-phosphotyrosine and Western immunoblotting with anti-FAK or for 24 h followed by cell counting, immunocytochemistry and flow cytometry. Both IGFBP-1 (0-800 ng/ml) and the synthetic RGD-containing peptide (1-100 microg/ml) caused significant dephosphorylation of FAK. Furthermore, after 24 h both peptides caused detachment from the matrix and the induction of apoptosis. We conclude from these data that IGFBP-1 can interact with integrin receptors to induce FAK dephosphorylation and subsequently influence attachment and cell death.

Sign in / Sign up

Export Citation Format

Share Document