ArticleBiochemical and biophysical research communications2009
FAK mediates the inhibition of glioma cell migration by truncated 24 kDa FGF-2.
Article in Biochemical and biophysical research communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- A marine sponge associated fungal metabolite monacolin X suppresses angiogenesis by down regulating VEGFR2 signaling.RSC advances · 2019Article
- Induction of proline-rich tyrosine kinase 2 activation-mediated C6 glioma cell invasion after anti-vascular endothelial growth factor therapy.Journal of translational medicine · 2014Article
- Inhibition of tumor cell migration by LD22-4, an N-terminal fragment of 24-kDa FGF2, is mediated by Neuropilin 1.Cancer research · 2013Article
- A simple knowledge-based mining method for exploring hidden key molecules in a human biomolecular network.BMC systems biology · 2012Article
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
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.
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