John J . O ' Shea , and Eric
نویسندگان
چکیده
Ingestion of opsonized foreign particles by phagocytic cells is a critical event in host defense against invading microorganisms, and factors that influence the rate and extent of phagocytosis are of particular interest. Fibronectin, a molecule found both in plasma and as a component of extracellular matrix, binds to phagocytic cells and enhances opsonin-mediated phagocytosis by monocytes, macrophages, and activated polymorphonuclear leukocytes (1-3). This phagocytosis enhancement by fibronectin is a direct effect of the molecule on the phagocyte and occurs for both IgGand complement-opsonized targets. Because of this, we have suggested that the phagocyte-fibronectin interaction may be important for optimal phagocytosis in areas of inflammation (4). This hypothesis raises the possibility that interaction with other extracellular matrix components may also modulate phagocyte function. In this report, we examine the effect of the matrix glycoprotein, laminin, on the phagocytic efficiency of human monocyte-derived macrophages. Laminin, a connective tissue glycoprotein with a molecular weight of 1,000,000, was originally isolated from a murine tumor (5). Laminin has subsequently been found to be a major component of all mammalian basement membranes (6). In vitro, laminin binds to other basement membrane components, notably type IV collagen and basement membrane proteoglycan (7), and mediates epithelial cell adhesion to artificial substrates (8). Unlike fibronectin, which also binds to collagen, proteoglycans, and cells (9), laminin is not normally detectable in the circulation. Recently (10), a laminin receptor on macrophages has been described, but very little is known about the effects of the interaction of laminin with phagocytic cells. We have tested whether macrophage-laminin interactions might, like interaction with fibronectin, modulate macrophage phagocytic function. In this work, we demonstrate that highly purified laminin enhances phagocytosis of IgGor complement-opsonized erythrocytes by human Address reprint requests to J. F. Bohnsack, Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases. National Institutes of Health, Building I0, Room 11N-214, Bethesda, MD 20205.
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