We propose that cell attachment and invasion can be regulated by the modulation of FAK expression in chondrosarcoma cell lines.

The C-terminal domain of FAK (FAK-CD) was transfected by recombinant adenovirus infection in chondrosarcoma cell lines, JJ012 and 105KC. The expression of FAK, FAK-CD and tyrosine phosphorylation were checked. Chondrocytes and chondrosarcoma cells were used in cell attachment tests by blocking or not blocking integrin-beta 1 antibodies and synthetic peptides on type II collagen. To evaluate the effect of cell invasiveness, a wound healing assay and a Boyden chamber assay were done after FAKCD transfection.

We observed higher FAK expression in the chondrosarcoma cells than in chondrocytes. The level of attachment to type II collagen was significantly inhibited by blocking with the antibody of integrin-beta 1 and synthetic RGD peptides. Also, the adenovirus mediated transfection of FAK-CD resulted in the inhibition of the phosphorylation of FAK and significant inhibition of cell attachment in only JJ012, without changing FAK expression. Moreover, migration after transfection with FAK-CD was reduced by up to 79.9% for JJ012 and 75.5% for 105KC.

Attachment of chondrosarcoma cells could be mediated through integrin-beta 1. We conclude that modified FAK expression contributes to the suppression of tumor cell attachment and invasion.