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Control of immune complex and zymosan-mediated anaphylatoxin generation by proteins B and H of the alternative complement pathway.

The generation of histamine releasing activity (HRA) from human basophils in fresh serum by tetanus toxoid (Te)/anti-Te complexes or by zymosan can be modulated through introduction of incremental amounts of proteins B and H of the alternative complement pathway. Serum treated at 50 degrees in order to abolish alternative pathway-mediated haemolytic activity, lost 90% of its capacity to generate HRA upon addition of Te/aTe; such loss could be reversed through additions of purified B. Amounts of B sufficient to restore normal alternative pathway haemolytic activity also restored HRA induced by Te/aTe; as little as a 33% increase above the normal serum concentration of B increased the capacity to support Te/aTe induced HRA by a factor of 1.4. In contrast, additions of incremental doses of purified H to fresh serum reduced generation of HRA by both Te/aTe and zymosan. Total inhibition was achieved by increasing the serum H concentration by 12.5-30%; further increases of H up to 200% again permitted HRA generation induced by immune complexed aTe. H also inhibited Te/aTe induced HRA in a serum heated at 50 degrees but only 30% inhibition of HRA could be achieved over a range of H inputs up to 187% above normal serum concentration. Additions of H also inhibited HRA generation in fresh serum when induced with plain or C3b-coated zymosan (Z) particles. By increasing the serum concentration of H from 12.5 to 125%, dose-dependent inhibition of HRA generation was observed; the H input necessary to suppress 48% of HRA generation was ten times higher when HRA was generated by Z-C3b than by plain zymosan. Thus, the complement-dependent generation of HRA from fresh serum strongly depends on modest variations in the concentrations of the two regulatory proteins B and H of the alternative complement pathway, suggesting their direct effect on generation of anaphylatoxins C3a and C5a.

Anaphylatoxins

The requirement of specific antibody for the killing of E. coli by the alternate complement pathway in bovine serum.

Experiments using the selective divalent cation chelator, ethylene glycol tetraacetic acid (EGTA) showed that the alternate complement pathway was involved in the bactericidal action of bovine serum on two strains of E. coli. The bactericidal system was shown, in experiments involving EGTA and epsilon-amino caproic acid, to be independent of Ca++ and the C1 unit of complement. The fixation of the complement components C3-C9 by endotoxin does not require a functional classical pathway ((C1, C4 and C2). In the case of one coliform strain (W1) however, there was an almost total dependence on a factor absorbable at 0 degrees with homologous bacteria, and which appeared to be a natural antibody. These results suggest that in certain circumstances in the cow, gamma globulins may be directly involved in the activation of the alternate complement pathway.

Animals

Activation of the alternative pathway of complement by apoptotic Jurkat cells.

Jurkat T cells die of apoptosis upon exposure to anti-Fas mAb. Here we show that although the alternative complement pathway generally does not attack homologous cells, anti-Fas-induced apoptotic Jurkat T cells were attacked antibody-independently by the alternative pathway of human complement and opsonized with iC3b, which is a ligand of the complement receptor type 3 (CR3) of phagocytes. These results suggest that apoptotic cells become the targets of the homologous alternative complement pathway, which facilitates the clearance of apoptotic cells by phagocytes.

Antibodies, Monoclonal

Alternative complement pathway in bovine serum: lysis of human erythrocytes.

The hemolysis of unsensitized human erythrocytes by fresh bovine serums was investigated. Lysis occurred in ethylene glycol bis-amino tetraacetate buffers and with serums depleted of Clq. Serums extensively absorbed with packed human erythrocytes at 0 C effectively lysed human erythrocytes, but optimal lytic capacity required target cells "sensitized" with a heat-stable serum factor. Lysis did not occur with serums absorbed with zymosan at 17 C or heat inactivated at 50 C. These results indicate that human erythrocytes can activate the alternative pathway of complement in bovine serums. Lysis can proceed in the apparent absence of antibodies, although their presence may enhance the reaction.

ABO Blood-Group System

Natural hemolytic and bactericidal activities of sea bream Sparus aurata serum are effected by the alternative complement pathway.

Sea bream serum displayed bactericidal and hemolytic activities. These activities were depleted when serum was incubated with different activators of the alternative complement pathway (ACP). Ethylenediaminetetraacetic acid (EDTA) inhibited both the hemolytic and bactericidal activities, while ethyleneglycol-bis (B-aminoethyl ether)-N, N, N'-tetraacetic acid (EGTA) was not inhibitory. An antibody against the putative third component of sea bream component (C3) was produced. It was observed by immunoelectrophoresis that the sea bream C3 and human C3 migrated in the same position. Crossed immunoelectrophoresis showed that sea bream C3 exhibited a similar pattern of activation when compared with its human counterpart. The anti-sea bream C3 antibody inhibited both bactericidal and hemolytic activities. It was concluded that both serum actions were displayed by the ACP. The best conditions for the sea bream ACP titration were investigated. Of all mammal erythrocytes tested, rabbit erythrocytes (RaRBC) were found to be the best ACP activators and thus were used for the titration. Sea bream showed very high ACP titers when compared with those of mammals. Absorption of naturally occurring antibodies against rabbit RaRBC did not influence the ACP titers. Enzymatic removal of sialic acid from different mammalian erythrocytes increased the sensitivity of these cells to hemolysis mediated by the sea bream ACP.

Animals

Incorporation of a 35-kilodalton purified protein from Loxosceles intermedia spider venom transforms human erythrocytes into activators of autologous complement alternative pathway.

Cutaneous inoculation of Loxosceles spp. spider venoms produces local necrosis, occasionally accompanied by systemic intravascular clotting and hemolysis. In this work, we analyzed the role of the C system on the lysis of human erythrocytes (Eh) induced by Loxosceles venoms in vitro. Eh were treated with whole venom of Loxosceles laeta, Loxosceles gaucho, or Loxosceles intermedia, or with purified venom proteins, and incubated with C-sufficient (Cs-NHS) or C9-depleted autologous (C9d-NHS) serum. Hemolysis was determined spectrophotometrically, and deposition of C components or removal of C regulatory proteins was analyzed by FACS. Eh suspensions exposed to venoms or to a purified 35-kDa protein from L. intermedia were lysed after incubation with Cs-NHS, but not with C9d-NHS. Lysis was blocked by heating the serum at 50 degrees C or Ca2+/Mg2+ chelation by EDTA, but not by Ca2+ chelation with EGTA. Deposition of C1, C2, C3, C4, C5, and factor B on the venom-treated Eh occurred during activation of autologous C. Regulatory proteins decay-accelerating factor (DAF) and CD59 were not altered significantly. Conversion of C-resistant Eh into C-susceptible Eh by the L. intermedia venom was accompanied by incorporation of a 35-kDa venom protein onto the cell surface. Thirty-five-kilodalton-related proteins were detected in the two other Loxosceles venoms by ELISA, using rabbit antiserum against the L. intermedia 35-kDa protein. These data suggest that the C system mediates the lysis of human erythrocytes and, by extension, of other cell types able to incorporate the lytic factor of Loxosceles venoms on their cell surfaces.

Animals

Malignant cells isolated from Burkitt's lymphoma but not other forms of leukemia activate the alternative complement pathway in human serum.

Cells isolated directly from primary biopsies of Burkitt's lymphoma were found to activate the alternative complement pathway in hypogammaglobulinemic human serum. In contrast, cells isolated from patients with either acute lymphoblastic leukemia, chronic lymphocytic leukemia or chronic myeloid leukemia did not activate. No defects in the ability of Burkitt's lymphoma sera to support alternative pathway activation were detected.

Burkitt Lymphoma

Structures of the asparagine-linked oligosaccharides of guinea-pig factor B of the alternative complement pathway.

This paper describes the structures of the asparagine-linked oligosaccharides of two forms of guinea-pig Factor B of the alternative complement pathway with different Mr values. Oligosaccharides were quantitatively liberated from both glycoproteins by hydrazinolysis, fractionated by paper electrophoresis and Bio-Gel P-4 column chromatography, and their structures determined by sequential exoglycosidase digestions in conjunction with methylation analysis. Both glycoproteins were shown to have the same biantennary complex-type oligosaccharides but it is suggested that they contain different numbers of oligosaccharide chains.

Animals

Classical and alternative complement pathway activation by pneumococci.

Sixty-two strains of Streptococcus pneumoniae were studied for their abilities to consume selected components of classical and alternative complement pathways in human sera. The classical pathway was blocked by chelating calcium with ethyleneglycol-bios (beta-aminoethyl ether)-N,N-tetraacetic acid and by removing C4. The alternative pathway was blocked by removing factor B. Each strain's activation of the two pathways was compared with its nonimmune reactivity with the Fc region of immunoglobulin G (IgG). Activation of the classical complement pathway appeared to be independent of such Fc reactivity. Highly Fc-reactive strains, however, were shown to activate the alternative pathway more effectively than did less Fc-reactive strains. Since pneumococcal activation of the alternative pathway requires non-immunospecific IgG, these findings suggest that nonimmune binding of IgG on the pneumococcal surface endows it with complement-activating properties.

Complement System Proteins

An improved fluorogenic substrate for the alternative complement pathway C3/5 converting enzyme CVFBb.

By lengthening the sequence of a previously available tripeptide to a pentapeptide, we were able to increase the specificity of the substrate for the complement enzyme CVFBb (EC 3.4.21.47) over Factor Xa (EC 3.4.21.6). This increase in specificity was achieved by both an increase in the kcat/Km for CVFBb for the longer substrate compared to the original substrate, and a decrease in the kcat/Km for Factor Xa. The new substrate, Boc-Nle-Gln-Leu-Gly-Arg-amino methyl coumarin (AMC) was synthesized by coupling Boc-Nle-Gln-Leu-Gly to Arg-AMC in solution. p-Toluenesulfonic acid was added to the coupling mixture to improve the solubility of the arginine derivative and avoid the need for covalent protection.

Chromatography, High Pressure Liquid