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FAK mediates the inhibition of glioma cell migration by truncated 24 kDa FGF-2.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Lin AH,Eliceiri BP,Levin EG

doi

10.1016/j.bbrc.2009.03.084

subject

Has Abstract

pub_date

2009-05-08 00:00:00

pages

503-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)00485-9

journal_volume

382

pub_type

杂志文章

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