Basic fibroblast growth factor (FGF-2) is produced as multiple forms of varying molecular weights, all derived from a single gene through alternative translational initiation sites [9]. One of these forms, 24 kDa FGF-2, has been shown to have dual functions, stimulation of cell proliferation and inhibition of cell migration [10]. Deletion mutagenesis of the 24 kDa FGF2 gene was used to engineer a protein that could inhibit the migration of a variety of tumor and non-tumor pirinixic acid with no effect on cell proliferation. ATE+31 is an 8400 MW protein which inhibits the migration of a variety of normal and malignant cells as well as angiogenesis and tumor growth in vivo [11] and [12].
We report that ATE+31 inhibits glioma cell migration by blocking the phosphorylation of serine732 and tyrosine407 within FAK. The decrease in phosphorylation levels at these specific two sites correlate with the change in the distribution of FAK and other additional phosphotyrosine proteins in focal adhesions, indicating that ATE+31 inhibits cell migration through the suppression of FAK phosphorylation.
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