Omental Immune Aggregates

Keyword(s):  
1976 ◽  
Vol 32 (1) ◽  
pp. 121-139 ◽  
Author(s):  
Morinobu Takahashi ◽  
Joyce Czop ◽  
Arturo Ferreira ◽  
Victor Nussenzweig
Keyword(s):  

2017 ◽  
Vol 108 ◽  
pp. 17-23 ◽  
Author(s):  
Maria Luiza Diniz de Sousa Lopes ◽  
Yi Liu ◽  
Kelly Yi-Ping Liu ◽  
Éricka Janine Dantas da Silveira ◽  
Catherine F. Poh

1993 ◽  
Vol 5 (1) ◽  
pp. 16-20 ◽  
Author(s):  
Renke Larochelle ◽  
Ronald Magar

Protein A-gold (PAG) and a primary porcine antiserum were used in immunogold silver staining (IGSS) for the detection of transmissible gastroenteritis virus (TGEV) in formalin-fixed paraffin-embedded tissue sections of small intestine originating from infected pigs. Immunogold electron microscopy was used to evaluate the reactivity of the prepared PAG marker with the specific porcine TGEV antiserum. Gold particles were closely associated with single virions and immune aggregates of TGEV. When IGSS, using PAG as the marker, was applied to tissue sections, dark staining of TGEV-infected villous enterocytes was observed. Background was low, allowing good visualization by light microscopy of the distribution of viral antigen. Two other gold conjugates, protein A/G-gold (PA/GG) and protein G-gold (PGG), were tested in IGSS. The labeling with PA/GG was comparable to that obtained with PAG. However, no staining was observed when PGG was used. The use of IGSS and PAG offers advantages and may represent a useful technique for the detection of other viral pathogens.


2011 ◽  
pp. 2606-2609
Author(s):  
Edith M. Lord
Keyword(s):  

Blood ◽  
1996 ◽  
Vol 88 (1) ◽  
pp. 184-193 ◽  
Author(s):  
HU Lutz ◽  
P Stammler ◽  
E Jelezarova ◽  
M Nater ◽  
PJ Spath

Abstract Intravenously applied human IgG has beneficial effects in treating inflammatory diseases, presumably because it has a complement attenuating role. This role of IgG was studied in vitro by following C3 activation and inactivation in sera that were supplemented with exogenous human IgG and incubated with immune aggregates. IgG added at 2 to 10 mg/mL stimulated the physiologic inactivation of C3b-containing complexes twofold to threefold in 20% sera. This, in turn, lowered the overall C3 activation by 28%, as new C3 convertases primarily assembled on C3b-containing complexes. Exogenous IgG (5 mg/mL) also stimulated inactivation of purified C3b2-IgG complexes, whereby their half-life dropped from 3–4 to 1.5 minutes in 20% serum. IgG appeared to act like a modulator of factor H and I because it did not stimulate inactivation of C3b-containing complexes in factor I-deficient serum. Thus, the known partial protection of C3bn-IgG complexes from inactivation by factor H and I was downregulated by high concentrations of IgG. The ability of high doses of IgG to stimulate complement inactivation is a novel regulatory role of IgG. This may be one of the molecular principles for its therapeutic efficacy in treating complement-mediated inflammations.


Complement ◽  
1987 ◽  
Vol 4 (1) ◽  
pp. 21-32 ◽  
Author(s):  
J.M. Alcolea ◽  
L.C. Antón ◽  
G. Marqués ◽  
P. Sánchez-Corral ◽  
F. Vivanco

1969 ◽  
Vol 114 (1) ◽  
pp. 141-144 ◽  
Author(s):  
Krister Hellsing

The precipitin reaction is enhanced in the presence of polysaccharides (Hellsing, 1966). This reaction has now been studied in detail with labelled antigen (125I-labelled human serum albumin) and antibody (131I-labelled rabbit anti-albumin immunoglobulin G). The relative proportions of antigen and antibody in the precipitates are unchanged by the addition of dextran in spite of the increased precipitation. The ratio of antibody to antigen in the soluble immune complexes decreases with increasing polysaccharide concentration. This can be interpreted as a decrease in the aggregate size of the complexes. At the same time the amount of free antigen in the solution increases. The results are consistent with a decrease in solubility, primarily of the large immune aggregates, together with a shift in the equilibrium between small and large complexes. The effect is in accord with a steric-exclusion phenomenon.


2009 ◽  
Vol 45 (2-3) ◽  
pp. 185-194 ◽  
Author(s):  
Elizabeth W. Sorensen ◽  
Scott A. Gerber ◽  
Abigail L. Sedlacek ◽  
Viktoriya Y. Rybalko ◽  
Winnie M. Chan ◽  
...  

1959 ◽  
Vol 110 (2) ◽  
pp. 311-339 ◽  
Author(s):  
Abraham G. Osler ◽  
Harry G. Randall ◽  
Betsy M. Hill ◽  
Zoltan Ovary

The interaction of fresh rat and guinea pig serum with washed preformed immune aggregates has been studied with respect to the loss in hemolytic potency of the serum, diminution of the C'3; activity, and appearance of anaphylatoxin. It has been found that the formation of anaphylatoxin, as judged by its effect on capillary permeability and smooth muscle contraction, is coincident with or subsequent to the fixation of all the known C' components. Less anaphylatoxin is formed by aggregates formed with excess antigen than those in equivalence ratio combination. C' fixation, as well as anaphylatoxin production, may be inhibited by chelation of the divalent cations, presumably by interfering with the fixation of C'1, C'4, and C'2. Phlorizin suppresses the utilization of C'3 in immune hemolysis, C' fixation by antigen-antibody aggregates, and the production of anaphylatoxin. The biological activities associated with the fixation of C' are not manifest unless C'3 participates in this process at 37°C. It is concluded that the formation of anaphylatoxin may be regarded as a product of C' fixation.


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