PMID: 11315093Apr 21, 2001Paper

Focal adhesion kinase (FAK) phosphorylation is not required for genistein-induced FAK-beta-1-integrin complex formation

Clinical & Experimental Metastasis
Y LiuRaymond C Bergan

Abstract

It has previously been shown that changes in the activity of focal adhesion kinase (FAK), and its binding to beta-1-integrin, accompany genistein-induced adhesion of prostate cells. Consumption of genistein world wide is associated with a lower incidence of metastatic prostate cancer. Early human clinical trials of genistein are under way to evaluate genistein's potential causal role in this regard. Though an important cell adhesion-associated signaling molecule, FAK's role in regulating prostate cell adhesion was not clear. Elucidation of this process would provide important information relating to both biology and potential clinical endpoints. It was hypothesized that FAK activation and complex formation are temporally related in prostate cells, and can thus be separated. Significant activation of FAK was demonstrated when cells adhered to fibronectin, as compared to poly-L-lysine, thus demonstrating that beta-1-integrin plays a significant role in activating FAK. Neither FAK activation, nor FAK-integrin complex formation, required beta-1-integrin ligand. However, disruption of the cellular cytoskeleton by cytochalasin D prevented FAK activation, but did not block genistein-induced complex formation. In the face of a disrupte...Continue Reading

Citations

Aug 2, 2003·Oncogene·Steven A HayesRaymond C Bergan
Jan 31, 2007·Annals of the New York Academy of Sciences·Shuk-Mei HoIrving Chung
Feb 14, 2007·Cellular & Molecular Biology Letters·Katarzyna Miękus, Zbigniew Madeja
Dec 19, 2013·Journal of Bioenergetics and Biomembranes·Vladimir Z AjdžanovićVerica Lj Milošević
Aug 15, 2002·American Journal of Pharmacogenomics : Genomics-related Research in Drug Development and Clinical Practice·B D JovanovicR C Bergan
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