Characterization of C1q by monoclonal antibodies. 1984

H P Heinz, and M Loos

The effect of a purified monoclonal anti-C1q antibody (Ab 242 G3) on the function of C1q, a subcomponent of the first component of complement C1, was studied. No inhibition of purified activated C1 was observed, whereas binding of the Ab to fluid phase C1q, to C1q bound to immune complexes (EAC1q), or to serum C1 in fluid phase resulted in a dose-dependent inhibition of the hemolytic activity of C1. In contrast, when the effect of the Ab on serum C1 bound to immune complexes (EAC1) was measured, no inhibition but a dose-dependent enhancement of the hemolytic activity was obtained. The dose-response curve of the Ab-treated cell bound serum C1 was indistinguishable from that of activated C1. Isolated Fab fragments of this Ab did not cause an increase in C1 activity. After separation of the A, B, and C chains of C1q by SDS-PAGE, Ab 242 G3 reacted in immunoblotting selectively within the C chain. These data indicate that cross-linking of C1q via the C chain of C1q might lead to an internal activation of C1. One out of seven monoclonal antibodies generated against mouse macrophages (M phi was found) to recognize isolated heterologous C1q. This antibody was shown to be cytotoxic and to react in a strain independent way with mouse M phi derived from bone marrow cells as well as with M phi from the peritoneal activity. However, it did not react with mouse granulocytes, thymocytes, T- and B-lymphocytes. The hemolytic activity of fluid phase C1q was inhibited to 50% at a 2 X 10(-4) dilution of hybridoma supernatant, whereas a 100-fold higher concentration was required to inhibit C1q bound to immune complexes (EAC1q) to the same extent. It was demonstrated that this antibody recognizes the isolated globular, Fc-binding portions of the C1q molecule and react with the A and B chains. Since M phi have been shown to synthesize C1q, the Fc-recognizing subcomponent of the first component of complement, evidence was provided that endogenous C1q can serve as an Fc receptor on M phi during secretion. This was demonstrated by a dose-dependent inhibition of Fc receptor activity for EIgG by the F (ab')2 fragment of this monoclonal antibody. In a fluorescence activated cell sorter (FACS) analysis Ab 146 F (ab')2 recognizes up to 75% of unstimulated NMRI peritoneal exudate cells (PEC), 60% and 53% of cells stimulated by thioglycollate and ConA, respectively.(ABSTRACT TRUNCATED AT 400 WORDS)

UI MeSH Term Description Entries
D007074 Immunoglobulin G The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B. Gamma Globulin, 7S,IgG,IgG Antibody,Allerglobuline,IgG(T),IgG1,IgG2,IgG2A,IgG2B,IgG3,IgG4,Immunoglobulin GT,Polyglobin,7S Gamma Globulin,Antibody, IgG,GT, Immunoglobulin
D008264 Macrophages The relatively long-lived phagocytic cell of mammalian tissues that are derived from blood MONOCYTES. Main types are PERITONEAL MACROPHAGES; ALVEOLAR MACROPHAGES; HISTIOCYTES; KUPFFER CELLS of the liver; and OSTEOCLASTS. They may further differentiate within chronic inflammatory lesions to EPITHELIOID CELLS or may fuse to form FOREIGN BODY GIANT CELLS or LANGHANS GIANT CELLS. (from The Dictionary of Cell Biology, Lackie and Dow, 3rd ed.) Bone Marrow-Derived Macrophages,Monocyte-Derived Macrophages,Macrophage,Macrophages, Monocyte-Derived,Bone Marrow Derived Macrophages,Bone Marrow-Derived Macrophage,Macrophage, Bone Marrow-Derived,Macrophage, Monocyte-Derived,Macrophages, Bone Marrow-Derived,Macrophages, Monocyte Derived,Monocyte Derived Macrophages,Monocyte-Derived Macrophage
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011961 Receptors, Fc Molecules found on the surface of some, but not all, B-lymphocytes, T-lymphocytes, and macrophages, which recognize and combine with the Fc (crystallizable) portion of immunoglobulin molecules. Fc Receptors,Fc Receptor,Receptor, Fc
D003166 Complement Activating Enzymes Enzymes that activate one or more COMPLEMENT PROTEINS in the complement system leading to the formation of the COMPLEMENT MEMBRANE ATTACK COMPLEX, an important response in host defense. They are enzymes in the various COMPLEMENT ACTIVATION pathways. Activating Enzymes, Complement,Enzymes, Complement Activating
D003167 Complement Activation The sequential activation of serum COMPLEMENT PROTEINS to create the COMPLEMENT MEMBRANE ATTACK COMPLEX. Factors initiating complement activation include ANTIGEN-ANTIBODY COMPLEXES, microbial ANTIGENS, or cell surface POLYSACCHARIDES. Activation, Complement,Activations, Complement,Complement Activations
D003172 Complement C1 The first complement component to act in the activation of CLASSICAL COMPLEMENT PATHWAY. It is a calcium-dependent trimolecular complex made up of three subcomponents: COMPLEMENT C1Q; COMPLEMENT C1R; and COMPLEMENT C1S at 1:2:2 ratios. When the intact C1 binds to at least two antibodies (involving C1q), C1r and C1s are sequentially activated, leading to subsequent steps in the cascade of COMPLEMENT ACTIVATION. C1 Complement,Complement 1,Complement Component 1,C1, Complement,Complement, C1,Component 1, Complement
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D000911 Antibodies, Monoclonal Antibodies produced by a single clone of cells. Monoclonal Antibodies,Monoclonal Antibody,Antibody, Monoclonal

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