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We examined the integrin expression in 19 human lung cancer cell lines with monoclonal antibodies to the integrin subunits alpha 1, alpha 2, alpha 3, alpha 4, alpha 5, alpha 6, beta 1, beta 2, and beta 4. We measured their ability to adhere to the extracellular matrix (ECM) and human umbilical vein endothelial cells (HUVECs). Almost all lines expressed the beta 1 subunit and approximately half of the lines expressed the beta 4 subunit; by contrast, none expressed the beta 2 subunit. Subunits alpha 2, alpha 3, alpha 5 and alpha 6 were frequently expressed, whereas very few lines expressed alpha 1 and alpha 4. Most lines adhered strongly to ECM (type I collagen, laminin and fibronectin) in correspondence to their expression of integrins. Binding by most lines to fibronectin was completely inhibited by arginine-glycine-aspartic acid (RGD) peptide. Three lines that expressed few or no integrins had very weak ability to adhere to ECM. Strong binding to HUVECs was found in most lines, but the three lines had very little ability to adhere to HUVECs. Binding to HUVECs was strongly inhibited at 4 degrees C, under divalent cation-free conditions and by antibodies to the beta 1 subunit. These results suggest that lung cancer cells adhere to ECM and endothelial cells through integrins, especially the beta 1 subfamily.

Integrin expression and ability to adhere to extracellular matrix proteins and endothelial cells in human lung cancer lines