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PubMed1976

The erythrocyte-granulocyte rosette. An immune cellular interaction found in some cases of autoimmune hemolytic anemias.

Erythrocyte-granulocyte rosettes (EGR) were found in the capillary blood of two cases of autoimmune haemolytic anemia, the first caused by an IgM non-I antibody and the second by an IgG. Both antibodies activated complement, and C3b was demonstrated on the erythrocytes. The rosettes appeared as arrangements of 6-10 red cells adhering to a central granulocyte; phagocytosis was most generally absent. The finding of EGR in the capillary blood may be useful for the recognition of complement activation up to the C3b stage in some cases of autoimmune haemolytic anemia.

Anemia, Hemolytic, Autoimmune↗
PubMed1986

Prostaglandin E and thromboxane B2 release by PMA-induced U937 cells in response to C3b.

The human monocytic cell lines HL-60 and U937 were examined for their ability to release PGE and TxB2 in response to the C3 cleavage fragment C3b. It was found that U937 responds to C3b by releasing both eicosanoids only after a 48 h induction period in the presence of PMA. HL-60 failed to respond. The response of U937 was further studied and characterized. It was found that the continual presence of PMA in culture was not required for the response to C3b, and that by replenishing the culture medium every 48 hr, the response could be maintained for up to 12 days. This contrasts with the previously observed behavior of human monocytes, which fail to respond after 24 hr in culture. Further studies demonstrated that maximal levels of PGE and TxB2 were elicited by 25-50 micrograms/ml of C3b, and that the kinetics of appearance of these eicosanoids in culture supernatants was very similar to that previously observed for monocytes. Maximal levels of PGE and TxB2 occurred following 24-48 hr in culture. In addition, a monoclonal a-CR1 antibody stimulated PG release by these cells. It is expected that this cell line will provide a model for study of the influence of cell differentiation on the response of human mononuclear phagocytes to C3b.

Cell Differentiation↗
PubMed1988

C3b inactivator in normal mice and mice infected with Plasmodium berghei berghei.

C3b inactivator levels were assayed in clean albino mice and mice infected with Plasmodium berghei berghei. Infected animals (63.1%) had low C3b inactivator levels when compared with 45% of controls with low levels. In the low titre range, infected mice had a significantly lower mean level (P less than 0.001) of the factor than controls. Conversely, in the high titre range, the mean C3b inactivator level is significantly (P less than 0.001) higher in infected than in control mice. Lower levels of the protein were associated with low grade parasitaemia, while raised levels were found in animals with higher parasitaemia. Low grade malaria parasitaemia predisposes to lowered C3b inactivator levels that would enhance persistence of deposited immune complexes, and subsequent tissue damage where C3b receptors are present.

Animals↗
PubMed1989

Monoclonal anti-human C3d antibodies: stabilization of the alternative pathway C3 convertase.

IgG mouse monoclonal antibody (mAb) was prepared by fusion of spleen cells from mice immunized with human C3d (mAb:C3d) using syngeneic thymocytes as feeder cells. mAb:C3d was assessed for its effect on the stabilization of the cell-bound alternative pathway C3 convertase EAC3bBb. It bound to cell-bound C3b and stabilized C3bBb at 30 degrees in the presence of EDTA-GVB. The plasma protein H reduced the stabilization effect of the stabilized C3 convertase. These results suggest that binding of antibody to C3d may stabilize C3bBb. It seems likely that such antibody induces in C3b conformational change, which increases the C3bBb complex stability.

Antibodies, Monoclonal↗
PubMed1981

Augmentation of macrophage complement receptor function in vitro. III. C3b receptors that promote phagocytosis migrate within the plane of the macrophage plasma membrane.

We have previously reported that treatment with a unique lymphokine enables resident mouse peritoneal macrophages to phagocytize via their complement receptors and we have presented evidence that the lymphokine act by enabling complement receptor engagement by C3b ligands to generate a phagocytic signal, thereby linking the cell surface binding event with the intracellular phagocytic machinery. In the present experiments, we used immobilized immune complexes to study the topography of C3b receptors of resident mouse peritoneal macrophages treated with the lymphokine. Our results indicate that lymphokine treatment enables the macrophages' C3b receptors to migrate within the plane of the cells' plasma membrane and that manipulations of macrophages that abrogate one response to the lymphokine, complement receptor mobility, also abrogate the other response, complement receptor-mediated phagocytosis. These findings strongly suggest that lateral mobility of a ligand-bound receptor within the macrophage plasma membrane is an essential component of the phagocytic signal. Moreover, our results indicate that the difference in complement receptor function among various populations of macrophages is not due to the expression of different types of complement receptors by the different macrophage populations but rather to a difference in the relationship of the C3b receptor with other plasma membrane or intracellular components.

Antigen-Antibody Complex↗
PubMed2002

Identification of the streptococcal M protein binding site on membrane cofactor protein (CD46).

Adherence of group A streptococcus (GAS) to keratinocytes is mediated by an interaction between human CD46 (membrane cofactor protein) with streptococcal cell surface M protein. CD46 belongs to a family of proteins that contain structurally related short consensus repeat (SCR) domains and regulate the activation of the complement components C3b and/or C4b. CD46 possesses four SCR domains and the aim of this study was to characterize their interaction with M protein. Following confirmation of the M6 protein-dependent interaction between GAS and human keratinocytes, we demonstrated that M6 protein binds soluble recombinant CD46 protein and to a CD46 construct containing only SCRs 3 and 4. M6 protein did not bind to soluble recombinant CD46 chimeric proteins that had the third and/or fourth SCR domains replaced with the corresponding domains from another complement regulator, CD55 (decay-accelerating factor). Homology-based molecular modeling of CD46 SCRs 3 and 4 revealed a cluster of positively charged residues between the interface of these SCR domains similar to the verified M protein binding sites on the plasma complement regulators factor H and C4b-binding protein. The presence of excess M6 protein did not inhibit the cofactor activity of CD46 and the presence of excess C3b did not inhibit the ability of CD46 to bind M6 protein by ELISA. In conclusion, 1) adherence of M6 GAS to keratinocytes is M protein dependent and 2) a major M protein binding site is located within SCRs 3 and 4, probably at the interface of these two domains, at a site distinct from the C3b-binding and cofactor site of CD46.

Amino Acid Sequence↗
PubMed1985

Determination of C3b receptors on normal and patient polymorphonuclear neutrophils with C3b-coated fluorescent microspheres.

A method, devised in the authors' laboratories, for the determination of C3b receptors on normal and patient neutrophils using C3b-coated fluorescent microspheres, was applied to the quantitation of C3b receptors on the neutrophils of several patients suffering from burns and trauma and a patient with pancreatitis. From three to 11 days in the clinical course the relative number of C3b receptors was, or rose to, two to ten times the number of receptors present at later times in the clinical course and, in most of the cases studied, the increase in C3b receptor number coincided with enhanced neutrophil bactericidal function. The rise in C3b receptor number was ascribed to up-regulation by C3a and C5a des Arg from complement activation and also, in the cases where sepsis occurred, to the presence of bacterial chemotactic peptides. Preliminary experiments with zymosan-activated serum and the chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine confirmed this explanation.

Blood Bactericidal Activity↗
PubMed1978

Receptor specific clearance by the reticuloendothelial system in chronic liver diseases. Demonstration of defective C3b-specific clearance in primary biliary cirrhosis.

An approach to the assessment of reticuloendothelial function that quantitates clearance specifically mediated by membrane receptors for C3b and immunoglobulin (Ig)G has been applied in man. Clearance of isologous erythrocytes coated with IgM or C3b or coated with IgG were examined in patients with primary biliary cirrhosis (PBC), chronic hepatitis, or alcoholic cirrhosis and normal control subjects and compared with the clearance of aggregated human serum albumin. Clearance of these three types of particles varied independently. None of the patients studied had a defect in the clearance of aggregated albumin. No patient with PBC (0:6) had delayed clearance of IgG-coated erythrocytes; one of six patients with chronic hepatitis had delayed clearance of these cells. Indeed, four of six with PBC had increased rates of IgG-mediated clearance. In contrast, six out of six patients with PBC had an unequivocal defect in clearance mediated by C3b receptors. The patients with PBC varied widely in terms of duration of symptoms, degree of cholestasis, and histologic stage of disease. No defect of C3b-mediated erythrocyte clearance was found in the patients with chronic hepatitis or alcoholic cirrhosis. Furthermore, a patient with severe cholestasis secondary to large duct biliary obstruction exhibited normal C3b-mediated clearance. The defect in C3b-mediated clearance in PBC did not correlate with serum levels of individual complement components or inhibitors or with the presence of circulating immune complexes as measured by the Clq precipitation assay. Thus, measurements of receptor specific clearance, but not clearance of aggregated proteins, have revealed a highly specific defect in reticuloendothelial function in PBC.

Adolescent↗
PubMed1990

A mechanism of activation of the alternative complement pathway by the classical pathway: protection of C3b from inactivation by covalent attachment to C4b.

In this work we studied the role of the classical pathway complement component C4b in the activation of the alternative pathway. It was found that nascent C3b attaches with high efficiency to C4b and that C3b in C4bC3b complexes is protected from inactivation by factors H and I. Activation of C3 by factors B and D in the presence of Mg2+ ions and excess C4b led to 35% incorporation of nascent C3b into C4bC3b complexes in the fluid phase. In comparison, when human IgG was tested as an acceptor under similar conditions, only 12% of generated C3b was incorporated into IgGC3b complexes. The half-life time of dissociation of C3b from purified C4bC3b complexes was approximately 2.3 h at 37 degrees C. C4b in these complexes protected C3b from inactivation as effectively as any known alternative pathway activator. Thus, C3b bound to C4b was tenfold more stable than free C3b or C3b bound to a nonactivating surface. In comparison, the protection provided by attachment to human IgG was only 67% of that of C4b. The results provide an explanation for observations of alternative pathway recruitment following classical pathway activation and for the stability of the classical pathway C5 convertase on surfaces which do not provide protection for C3b from factors H and I.

Complement C3-C5 Convertases↗