title: Mannan-binding lectin and C1q bind to distinct structures and exert differential effects on macrophages.
abstract: While the interaction of complement component C1q with cellular proteins is extensively studied, much less is known about the binding of the structurally related molecule, mannan-binding lectin (MBL) to various cells. Here we show by cytofluorimetry that the interaction of MBL with immunocompetent cells is much more restricted than that of C1q. It is shown that under conditions of physiological ionic strength MBL binds to human monocyte-derived macrophages (Mphi) and monocytoid cell lines, but not to T and B lymphocytes, in contrast to C1q, which interacts with all these cells under the same conditions. As opposed to the binding of C1q, low ionic strength does not improve the interaction of MBL with Mphi. No competition for cellular binding sites was found when MBL and C1q were added simultaneously to the cells. Studying the functional consequences of the interaction, we found that the release of TNF-alpha from Mphi is induced by C1q but not by MBL. Production of complement C3 by Mphi is stimulated by C1q strongly, while the effect of MBL is much weaker. C3 produced upon C1q-mediated triggering is shown to opsonize RBC, resulting in enhanced phagocytosis. These results suggest that cell membrane molecules binding MBL and C1 q are not identical; moreover, biological functions exerted by these proteins are also markedly different.
authors.affiliation: Department of Immunology and Hungarian Academy of Sciences, Eötvös Loránd University, Göd.
authors.forename: Z
authors.initials: Z
authors.lastname: Bajtay
authors.forename: M
authors.initials: M
authors.lastname: Józsi
authors.forename: Z
authors.initials: Z
authors.lastname: Bánki
authors.forename: S
authors.initials: S
authors.lastname: Thiel
authors.forename: N
authors.initials: N
authors.lastname: Thielens
authors.forename: A
authors.initials: A
authors.lastname: Erdei
mesh_terms: D001665:Binding Sites; D001667:Binding, Competitive; D002352:Carrier Proteins / Q000276:immunology*; D002454:Cell Differentiation; D002478:Cells, Cultured; D037222:Collectins; D015922:Complement C1q / Q000276:immunology*; D003176:Complement C3 / Q000096:biosynthesis; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000276:immunology; D019169:Jurkat Cells; D008264:Macrophages / Q000166:cytology / Q000276:immunology*; D010587:Phagocytosis / Q000276:immunology; D011485:Protein Binding; D014409:Tumor Necrosis Factor-alpha / Q000096:biosynthesis; D020298:U937 Cells
chemical_list: D002352:Carrier Proteins; D037222:Collectins; D003176:Complement C3; D007140:Immunoglobulin Fab Fragments; D014409:Tumor Necrosis Factor-alpha; D015922:Complement C1q