Bronchoconstrictor Effects of Soluble Antigen–Antibody Complexes in Isolated Lung, and their Inhibition by Normal Serum

Soluble antigen-antibody-complement complexes bound to mouse B lymphocytes are rapidly released from the cell membrane in the presence of normal serum from several mammalian species. The release is not the result of antigen-antibody dissociation or extensive degradation of the complexes. However, the released complexes have been altered because they will no longer bind to fresh lymphocytes. The release is not the result of lymphocyte damage mediated by complement. It is complement-dependent, and is generated either preferentially or exclusively via the alternate pathway, since it occurs in C4-deficient serum, is Mg++ but not Ca++ dependent, and requires C3 proactivator. C3 inactivator is not involved. The release activity of the serum, once generated, is unstable at 37°C. The release of complexes from the lymphocyte membrane by serum provides a convenient assay for the functioning of the alternate pathway in the mouse and in other species.

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Interactions between lymphocyte membrane molecules. I. Interaction between B lymphocyte surface IgM and Fc IgG receptors requires ligand occupancy of both receptors.

Journal of Experimental Medicine ◽

10.1084/jem.153.5.1329 ◽

1981 ◽

Vol 153 (5) ◽

pp. 1329-1343 ◽

Cited By ~ 15

Author(s):

H B Dickler ◽

M T Kubicek

Keyword(s):

B Lymphocyte ◽

Surface Membrane ◽

Specific Interaction ◽

Normal Serum ◽

Membrane Receptors ◽

Soluble Antigen ◽

Lymphocyte Surface ◽

Igg Receptors ◽

Antigen Antibody

The independent B lymphocyte surface membrane receptors IgM and Fc IgG receptors were evaluated for interactions using immunoflourescence. Ligand [F(ab')2 anti-mu]-induced capping of surface IgM resulted in capping of Fc IgG receptors only if the latter were occupied during the capping process by: (a) soluble antigen-antibody complexes that themselves provided insufficient cross-linking to result in capping; or (b) monomeric IgG at physiologic concentrations (or less) either purified or as normal serum. Ligand-induced capping of Fc IgG receptors did not result in capping of surface IgM occupied by monomeric F(ab') anti-mu. Control experiments showed that ligand binding to or capping of only one of these two receptors has no effect on the other, and that there were no cross-reactions. The interaction appears specific in that ligand-induced capping of surface IgM did not induce capping of ligand-occupied surface IgD or I-A antigens. Thus, there appears to be a specific interaction between ligand-bound surface IgM and ligand-bound Fc IgG receptors on the B lymphocyte surface. The results also indicate that binding of monomeric IgG produces a reversible alteration in the Fc IgG receptor leading to association with ligand-bound surface IgM. Because Fc IgG receptors are continuously exposed to monomeric IgG in vivo, these results suggest that whenever surface IgM is involved in a B lymphocyte response to an immunologic stimulus, the Fc IgG receptor is also involved.

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THE PATHOLOGIC EFFECTS OF INTRAVENOUSLY ADMINISTERED SOLUBLE ANTIGEN-ANTIBODY COMPLEXES

Journal of Experimental Medicine ◽

10.1084/jem.111.2.195 ◽

1960 ◽

Vol 111 (2) ◽

pp. 195-200 ◽

Cited By ~ 35

Author(s):

Baruj Benacerraf ◽

Jacobus L. Potter ◽

Robert T. McCluskey ◽

Frederick Miller

Keyword(s):

Blood Urea Nitrogen ◽

Intravenous Administration ◽

Acute Glomerulonephritis ◽

Soluble Antigen ◽

Urea Nitrogen ◽

Antigen Antibody

The intravenous administration to rats of soluble antigen-antibody complexes in antigen excess resulted in acute glomerulonephritis. This occurred with both rabbit antiovalbumin and rabbit anti-BSA systems. The rats so treated regularly showed proteinuria and elevation of blood urea nitrogen. These findings are compared with those reported in rats injected with anti-kidney serum.

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Physical Chemical Studies of Soluble Antigen-Antibody Complexes. XI. An Analysis of the Resolution by Electrophoresis and Ultracentrifugation of a Univalent Antigen-Bivalent Antibody System1

Journal of the American Chemical Society ◽

10.1021/ja01524a022 ◽

1959 ◽

Vol 81 (15) ◽

pp. 3887-3891 ◽

Cited By ~ 17

Author(s):

S. J. Singer ◽

Frank A. Pepe ◽

David Ilten

Keyword(s):

Soluble Antigen ◽

Physical Chemical ◽

Chemical Studies ◽

Antigen Antibody

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Activation of the classical pathway of complement by Hageman factor fragment.

Journal of Experimental Medicine ◽

10.1084/jem.153.3.665 ◽

1981 ◽

Vol 153 (3) ◽

pp. 665-676 ◽

Cited By ~ 176

Author(s):

B Ghebrehiwet ◽

M Silverberg ◽

A P Kaplan

Keyword(s):

Normal Serum ◽

Classical Pathway ◽

Hageman Factor ◽

Concomitant Reduction ◽

Dose Dependent Fashion ◽

Total Complement ◽

Trimolecular Complex ◽

Comparable Activity ◽

The Individual ◽

Antigen Antibody

A fragment of activated Hageman factor (HFf) has been demonstrated to activate the classical pathway of complement in a manner that is analogous to complement activation by antigen-antibody complexes or aggregated IgG. Thus C1, C4, C2, C3, and C5 were found to be depleted on addition of HFf to serum. The reduction of serum hemolytic activity was maximal upon addition of 5 micrograms HFf and an incubation time of 60 min at 37 degrees C. Consumption of the total complement activity and of the individual components proceeded in a dose-dependent fashion. No comparable activity was observed when equimolar concentrations of either the native Hageman factor (HF) or two-chain activated form of Hageman factor (HFa) were incubated with serum. Further, the ability of HFf to convert serum C3 and C4 was similar to that of aggregated IgG as assessed by immunoelectrophoresis. This function of HFf appeared to be independent of plasminogen (or plasmin) since plasminogen-free serum was indistinguishable from normal serum. Radial double immunodiffusion experiments using antiserum to C1q, C1r, and C1s on HFf-treated serum demonstrated the dissociation of the C1 trimolecular complex, with concomitant reduction of C1r antigenicity that is indicative of C1 activation. Thus, HFf appears to lead to C1 activation upon incubation with serum or when incubated with partially purified C1. This may represent a control link between activation of the intrinsic coagulation-kinin pathway and the initiation of the classical complement cascade.

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THE EFFECT OF ANTISERUM, ALONE AND WITH HYDROCORTISONE, ON FOETAL MOUSE BONES IN CULTURE

Journal of Experimental Medicine ◽

10.1084/jem.121.4.551 ◽

1965 ◽

Vol 121 (4) ◽

pp. 551-560 ◽

Cited By ~ 65

Author(s):

Honor B. Fell ◽

L. Weiss

Keyword(s):

Lysosomal Enzymes ◽

Protective Action ◽

Rabbit Antiserum ◽

Normal Serum ◽

Rabbit Serum ◽

Normal Rabbit Serum ◽

Limb Bones ◽

Mouse Tissues ◽

Antigen Antibody ◽

Indirect Action

1. The effects of normal rabbit serum and of rabbit antiserum to whole foetal mouse tissues, on the isolated limb bones of late foetal mice were studied in organ culture, and the influence of hydrocortisone on these effects was investigated. 2. Unheated normal serum caused slight loss of metachromatic material from the cartilage matrix, and some resorption of both cartilage and bone. 3. In unheated antiserum to foetal mouse tissues, the terminal cartilage was smaller and less metachromatic than in paired controls in normal serum, while osteoclasis was so intense that in many explants the bone had almost disappeared. The amount of necrosis varied with different batches of antiserum. 4. The changes produced by normal serum and antiserum could be largely prevented by heating the sera to 57°C for 45 minutes. 5. The effects could also be inhibited by the addition of hydrocortisone to the unheated sera; as little as 0.1 µg hydrocortisone per ml of medium had a well marked protective action. 6. It is suggested that (a) unheated antiserum causes a release of lysosomal enzymes with consequent breakdown of intercellular material, (b) this release is due to an indirect action on the lysosome via an increased permeability of the cell membrane, (c) hydrocortisone does not affect the antigen-antibody reaction, but inhibits the autolytic changes that normally follow this reaction, possibly by stabilising both the lysosomal and cell membranes.

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