Differential expression of alphav integrins in K1735 XXXX cells.

@entity5 @entity19 @entity18755 @entity3 @entity21464 @entity320
@entity5 cell adherence to and migration on the extracellular matrix is an important aspect of @entity5 progression. This interaction with the extracellular matrix is mediated primarily through the integrin class of cell adhesion molecules. We identified a restricted expression of alphavbeta3 in highly metastatic K1735M2 and of alphavbeta5 in poorly metastatic K1735C23 @entity19 @entity320 cells. The highly metastatic cells were ten times more motile on @entity18755 and fibronectin and approximately three times more invasive through a reconstituted basement membrane than the poorly metastatic cells. This motility was inhibited by addition of anti- @entity21464 antibodies. Injection of the alphavbeta3-negative K1735C23 cells into syngeneic @entity19 resulted in the generation of a metastatic variant (K1735C23PM) that neo expressed the alphavbeta3 complex, indicating that expression of alphavbeta3 is required for K1735 @entity320 @entity3 . Injection of highly metastatic K1735M2 cells in the presence of blocking antibody to @entity21464 reduced @entity5 size by approximately 80%. Treatment of the K1735M2 cells with a retroviral antisense @entity21464 construct significantly reduced their expression of alphavbeta3 and also reduced their motility on extracellular matrix ligands and their invasion through a reconstituted basement membrane. In contrast, when the K1735C23 cells were treated with a construct containing the full-length @entity21464 cDNA, their motility on extracellular matrix proteins and invasion of a reconstituted basement membrane were significantly increased. These results indicate that alphavbeta3 is required for migration and invasion of K1735 @entity320 cells in vitro and primary @entity5 growth and @entity3 in vivo.
