The role of beta 1 integrins in adhesion of two XXXX cell lines to a model endothelium.

@entity5 @entity0 @entity3 @entity2931
Interactions between @entity5 cells and the endothelium are vital to the formation of haematogenous @entity3 . Binding to model endothelium of one @entity2931 receptor positive @entity0 cell line (MCF-7) and one receptor negative line (HS578T) was examined in vitro together with endothelial retraction induced by these @entity5 cells. Adhesion was inhibited by monoclonal antibodies specific for the VLA integrins and by peptides containing the RGD motif which is commonly recognised as a ligand by the VLA adhesion molecules. However, binding of the two @entity5 cell lines was inhibited by monoclonal antibodies specific for different VLA molecules; anti-alpha 6 beta 1 inhibited MCF-7 adhesion but anti-alpha 5 beta 1 inhibited Hs578T. These results were consistent with flow cytometric quantification of the expression of these VLA integrins on the surfaces of the two @entity5 cell lines. Enzyme-linked immunosorbent assays (ELISA) demonstrated that laminin was present on the endothelial cell surface but collagen IV was absent. ELISA failed to detect increased exposure of the subendothelial matrix during the first hour after addition of either @entity5 cell type. This was supported by assays which demonstrated maintenance of the endothelial permeability barrier during this period. Slight endothelial retraction was detected within 2 hours of the addition of @entity5 cells. It is concluded that binding between @entity5 cells and confluent endothelium is inhibited by the blockade of adhesion molecules which are normally associated with interactions between the cell and the subendothelial matrix. @entity5 cell to matrix interactions rather than direct @entity5 to endothelial cell adhesion may be the limiting step in @entity5 cell binding to the endothelium.
