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FAK mediates the inhibition of glioma cell migration by truncated 24 kDa FGF-2
Amy H Lin1, Brian P Eliceiri, Eugene G Levin
1Torrey Pines Institute for Molecular Studies, 3550 General Atomics Court, San Diego, CA 92121, United States.
Abstract:
A truncated form of 24kDa FGF-2 consisting of 86 NH(2)-terminal amino acids (ATE+31) inhibits cell migration in vitro and tumor development and angiogenesis in vivo. Focal adhesion kinase (FAK) is phosphorylated on tyrosine and serine sites after cell stimulation by growth factors. This study examined the effect of ATE+31 on FAK phosphorylation in human glioma cells. FAK and Pyk phosphorylation were evaluated at serines known to be involved with cell migration. We demonstrated that ATE+31 at 3 x 10(-11)M decreases phosphorylation levels of Tyr(407)-FAK and Ser(732)-FAK in the presence of platelet-derived growth factor (PDGF), that ATE+31 in the presence of PDGF alters the distribution of FAK and other phosphotyrosine proteins in the adhesion contacts, and that ATE+31 in the presence of PDGF has no effect on the activation of Pyk2. These data suggest that the inhibition of cell migration by ATE+31 occurs via Tyr(407)-FAK and Ser(732)-FAK.
Insights
A truncated FGF-2 peptide (ATE+31) inhibits glioma cell migration by reducing focal adhesion kinase (FAK) phosphorylation at key sites. This peptide impacts FAK distribution, offering a potential therapeutic target for gliomas.
Area of Science:
- Oncology
- Cell Biology
- Biochemistry
Background:
- Fibroblast Growth Factor 2 (FGF-2) plays a role in tumor development and angiogenesis.
- Focal Adhesion Kinase (FAK) phosphorylation is crucial for cell migration, regulated by growth factors like Platelet-Derived Growth Factor (PDGF).
Purpose of the Study:
- To investigate the effect of a truncated FGF-2 form (ATE+31) on FAK phosphorylation in human glioma cells.
- To elucidate the mechanism by which ATE+31 inhibits cell migration.
Main Methods:
- Human glioma cells were treated with ATE+31 and PDGF.
- FAK and Pyk2 phosphorylation levels at specific tyrosine and serine sites were assessed.
- Immunofluorescence was used to analyze the distribution of FAK and phosphotyrosine proteins.
Main Results:
- ATE+31 significantly decreased phosphorylation of Tyr(407)-FAK and Ser(732)-FAK in the presence of PDGF.
- PDGF-induced alterations in FAK and phosphotyrosine protein distribution within adhesion contacts were modified by ATE+31.
- ATE+31 did not affect Pyk2 activation.
Conclusions:
- The inhibition of glioma cell migration by ATE+31 is mediated through its effects on Tyr(407)-FAK and Ser(732)-FAK phosphorylation.
- ATE+31 represents a potential therapeutic agent targeting FAK signaling pathways in gliomas.
