CR3 is probably the major adhesion molecule on monocytes and neutrophils. Its function as a phagocytic receptor for iC3b-coated particles has been well characterized. CR3 also has binding affinity for other ligands, including those that compete with iC3b such as fibrinogen, factor X, and beta-glucan, and those that do not such as bacterial LPS. CR3 binding to endothelial cells probably plays an important role in the extravascular migration of monocytes and neutrophils, but the ligand that it recognizes on endothelial cells has not been identified. Structurally CR3 belongs to the integrin family, and it shares a common subunit with p150,95 and LFA-1. The expression of these three membrane antigens appear to be limited to leukocytes, and they are sometimes referred to collectively as the leukocyte integrins. All three antigens have a common binding affinity for bacterial LPS. p150,95 also has affinity for iC3b, but p150,95/iC3b-dependent cellular responses has not been demonstrated. Its status as a complement receptor therefore awaits further experimental support.