Lectin-like oxidized low density lipoprotein receptor-1 (LOX-1) supports cell adhesion to fibronectin.

Lectin-like oxidized lipoprotein receptor-1 (LOX-1) is a specific receptor for atherogenic oxidized low density lipoprotein (OxLDL) which belongs to the scavenger receptor family. In the present report, we show that LOX-1 can also support cell adhesion to fibronectin (FN) in a divalent cation-independent fashion. CHO-K1 cells stably expressing bovine LOX-1 (BLOX-1-CHO), but not untransfected CHO-K1 cells, can adhere to FN-coated plates, but not to collagen-coated plates, in the presence of EDTA. BLOX-1-CHO adhesion to FN-coated plates can also be suppressed by scavenger receptor ligands, such as OxLDL, polyinosinic acid (poly I), and dextran sulfate, but not by native LDL, acetylated LDL, polycytidylic acid (poly C), or chondroitin sulfate. Cultured bovine aortic endothelial cells can similarly adhere to FN-coated plates, which was inhibited by OxLDL, poly I, and dextran sulfate in the presence of EDTA. LOX-1 may play an important role in cell adhesion to FN in an integrin-independent manner.