연골육종 세포주, 세포 부착, 세포 침습, Focal adhesion kinase, Integrin- 1, FAK-CD
Abstract
Purpose : We propose that cell attachment and invasion can be regulated by the modulation of FAK expression in chondrosarcoma cell lines.
Materials and Methods : 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- 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.
Results : 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- 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.
Conclusion : Attachment of chondrosarcoma cells could be mediated through integrin- 1. We conclude that modified FAK expression contributes to the suppression of tumor cell attachment and invasion.