scholarly journals Effects of immobilized immune complexes on Fc- and complement-receptor function in resident and thioglycollate-elicited mouse peritoneal macrophages.

1979 ◽  
Vol 150 (3) ◽  
pp. 607-621 ◽  
Author(s):  
J Michl ◽  
M M Pieczonka ◽  
J C Unkeless ◽  
S C Silverstein
Keyword(s):  
Immune Complexes ◽  
Fc Receptors ◽  
Cell Types ◽  
Peritoneal Macrophages ◽  
Complement Receptor ◽  
Complement Receptors ◽  
Receptor Function ◽  
Rabbit Antibody ◽  
Coated Surfaces ◽  
Mouse Peritoneal Macrophages

We have examined the Fc- and complement-receptor function of resident and thioglycollate-elicited mouse peritoneal macrophages plated on surfaces coated with rabbit antibody-antigen complexes and with complement. We derive four major conclusions from these studies. (a) The trypsin-resistant Fc receptors of resident and thioglycollate-elicited macrophages are completely modulated when these cells are plated on rabbit antibody-antigen complexes. Residual Fc receptor activity is a result of the incomplete modulation of trypsin-sensitive IgG2a receptors. (b) The complement receptors of thioglycollate-elicited macrophages, but not of resident macrophages, are modulated when these cells are plated on complement-coated surfaces. The capacity of the two cell types to modulate their complement receptors is correlated with their ability to ingest complement-coated erythrocytes. (c) The complement and Fc receptors of both types of macrophages move independently of one another. (d) Complement masks the Fc segments of IgG in immune complexes thereby rendering them ineffective as ligands for macrophage Fc receptors.

scholarly journals Effects of soluble immune complexes on Fc receptor- and C3b receptor-mediated phagocytosis by macrophages.

1980 ◽  
Vol 152 (4) ◽  
pp. 905-919 ◽  
Author(s):  
F M Griffin
Keyword(s):  
Immune Complexes ◽  
Fc Receptors ◽  
Fc Receptor ◽  
Complement Receptor ◽  
Complement Receptors ◽  
Phagocytic Function ◽  
Receptor Function ◽  
Coated Particles ◽  
C3b Receptor ◽  
Soluble Immune Complexes

The effects of ingestion of soluble immune complexes upon macrophage phagocytic function was studied. Ingestion of immune complexes severely impaired the macrophage's ability to ingest IgG-coated particles but did not alter its ability to interact with particles by means other than its Fc receptors. Treatment of macrophages that had ingested immune complexes with supernates containing the previously described lymphokine that augments macrophage complement receptor function failed to enhance the cells' interaction with either IgG-coated erythrocytes or zymosan particles but markedly enhanced their ability to phagocytize via their complement receptors. The possible significance of these findings in immunologically mediated inflammation is discussed.

scholarly journals The effect of complement on the ingestion of soluble antigen-antibody complexes and IgM aggregates by mouse peritoneal macrophages.

1978 ◽  
Vol 148 (4) ◽  
pp. 903-914 ◽  
Author(s):  
J L van Snick ◽  
P L Masson
Keyword(s):  
Immune Complexes ◽  
Degradation Products ◽  
Fc Receptors ◽  
Peritoneal Macrophages ◽  
Soluble Antigen ◽  
Complement Receptors ◽  
Human Transferrin ◽  
Particulate Antigen ◽  
Antigen Antibody ◽  
Mouse Peritoneal Macrophages

Complement was found to stimulate markedly the ingestion of soluble antigen-antibody complexes by mouse peritoneal macrophages. This was shown indirectly by measuring the release of degradation products when the complexes were labeled with 125I, or directly when the antigen, that was human transferrin, was labeled with 59Fe. In this case, the metal which was released from human transferrin inside the cells was not excreted, and its accumulation in the macrophages was a direct index of the uptake of immune complexes. The decay of radioactivity in macrophages after ingestion of 125I-labeled complexes was similar when they were taken up with or without complement, indicating that complement acts primarily on ingestion and not on digestion or excretion. The ingestion of complexes was morphologically confirmed using fluorescein-labeled antigen in the immune complexes. The opsonic effect of complement was also observed with IgM aggregates indicating that soluble complexes can be ingested through complement receptors without involvement of Fc-receptors, as required for particulate antigen-antibody complexes.

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

1981 ◽  
Vol 154 (2) ◽  
pp. 291-305 ◽  
Author(s):  
F M Griffin ◽  
P J Mullinax
Keyword(s):  
Plasma Membrane ◽  
Peritoneal Macrophages ◽  
Complement Receptor ◽  
Complement Receptors ◽  
Receptor Function ◽  
Surface Binding ◽  
The Difference ◽  
Macrophage Populations ◽  
Mouse Peritoneal Macrophages

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.

scholarly journals Augmentation of macrophage complement receptor function in vitro. I. Characterization of the cellular interactions required for the generation of a T-lymphocyte product that enhances macrophage complement receptor function.

1979 ◽  
Vol 150 (3) ◽  
pp. 653-675 ◽  
Author(s):  
J A Griffin ◽  
F M Griffin
Keyword(s):  
T Lymphocytes ◽  
Complex Disease ◽  
Peritoneal Macrophages ◽  
Fc Receptor ◽  
Microbial Pathogens ◽  
Complement Receptor ◽  
Complement Receptors ◽  
Cellular Interactions ◽  
Receptor Function

The function of complement receptors of mouse peritoneal macrophages was converted in vitro from mediating only attachment of macrophage complement receptor function was achieved by treating freshly explanted macrophages with supernates from cultures containing T lymphocytes and appropriately triggered macrophages. Fc receptor-mediated phagocyctosis by macrophages was required for the production of active supernates, for neither ingestion via the cells' complement receptors nor ingestion via nonimmunologic means was a sufficient stimulus for the macrophages' participation in the generation of supernatant activity. Fc receptor-triggered macrophages interacted by a contact dependent, but histocompatibility independent, mechanism with T lymphocytes, thereby signalling the lymphocytes to elaborate the active product. The possible significance of enhanced macrophage complement receptor function in inflammation, host defense against microbial pathogens, immune complex disease, and neoplasia is discussed.

scholarly journals Studies of the macrophage complement receptor. Alteration of receptor function upon macrophage activation.

1975 ◽  
Vol 141 (6) ◽  
pp. 1278-1290 ◽  
Author(s):  
C Bianco ◽  
F M Griffin ◽  
S C Silverstein
Keyword(s):  
Macrophage Activation ◽  
Quantitative Difference ◽  
Qualitative Difference ◽  
Fc Receptors ◽  
Significant Degree ◽  
Peritoneal Macrophages ◽  
Fc Receptor ◽  
Complement Receptor ◽  
Complement Receptors ◽  
Activated Macrophages

We have examined the roles of Fc receptors and complement receptors in mediating the interaction of sensitized sheep erythrocytes (E) with activated and with nonactivated mouse peritoneal macrophages. Both activated and nonactivated macrophages ingest IgG-coated erythrocytes [E(IgG)]; activated cells intest 1.5-2 times as man E(IgG) as do nonactivated macrophages. Thus, there is a quantitative difference in Fc receptor-mediated ingestion between activated and nonactivated macrophages. There is, however, a qualitative difference in function of complement receptors of activated and nonactivated macrophages. Nonactivated macrophages avidly bind complement-coated E [E(IgM)Ia1, but do not ingest them to a significant degree. Activated macrophages, on the other hand, bind and ingest E(IgM)C. The possibility of Fc receptor participation in mediating ingestion of E(IgM)C by activated macrophages was eliminated by blocking Fc receptors with an antimacrophage IgG fraction. Activated macrophages treated with antimacrophage IgG did not ingest E(igG) but did ingest both E(IgM)C AND E(IgM)C. Nonactivated macrophages treated with antimacrophage IgG did not interact at all with E(IgG). These cells bound, but did not ingest, E(IgM)C and E(IgM)C. Complement receptor-mediated ingestion is a marker for macrophage activation and may be physiologically important in the elimination of complement-coated particles.

scholarly journals Activation of mouse peritoneal macrophages by monoclonal antibodies to Mac-1 (complement receptor type 3).

1987 ◽  
Vol 165 (3) ◽  
pp. 733-749 ◽  
Author(s):  
A Ding ◽  
S D Wright ◽  
C Nathan
Keyword(s):  
Macrophage Activation ◽  
Time Course ◽  
Peritoneal Macrophages ◽  
Receptor Type ◽  
Tnf Alpha ◽  
Complement Receptor ◽  
Complement Receptor Type ◽  
Coated Surfaces ◽  
Type 3 ◽  
Mouse Peritoneal Macrophages

Several features of activation of mouse peritoneal macrophages were elicited by 1-2-d exposure to submicrogram concentrations of anti-Mac-1 (M1/70), a rat monoclonal antibody that reacts with the alpha chain of complement receptor type 3 (Mac-1). The changes induced included enhanced capacity to secrete H2O2 when triggered with PMA, decreased secretion of proteins, increased expression of Ia antigen and decreased phagocytosis of particles. These changes closely resembled those induced by rIFN-gamma in type, extent, and time course. The concentration of M1/70 IgG resulting in 50% of the maximal activation of macrophage H2O2-releasing capacity averaged 0.18 +/- 0.03 micrograms/ml. This activation was not blocked by anti-FcR mAb, and could be reproduced with M18/2, a mAb against beta chain of Mac-1, suggesting that a direct ligation of Mac-1 with mAb was responsible for the activation. Neither depletion of T cells nor addition of neutralizing Abs to IFN-gamma or TNF-alpha prevented M1/70-mediated macrophage activation. Moreover, F(ab')2 of M1/70, or plating of macrophages on C3bi-coated surfaces, inhibited the activation of macrophages by rIFN-gamma. These findings suggest that Mac-1 (CR3) may play an important role in macrophage activation.

scholarly journals In vivo activation of macrophage C3 receptors for phagocytosis.

1985 ◽  
Vol 162 (1) ◽  
pp. 352-357 ◽  
Author(s):  
F M Griffin ◽  
P J Mullinax
Keyword(s):  
T Lymphocytes ◽  
Immune Complexes ◽  
Fc Receptors ◽  
Peritoneal Macrophages ◽  
Fc Receptor ◽  
Athymic Mice ◽  
Receptor Function ◽  
C3 Receptors

We assessed the effects of exposure to immune complexes in vivo on macrophages' Fc receptor function and C3 receptor function. Peritoneal macrophages from mice injected intraperitoneally with immune complexes were markedly impaired in their ability to phagocytize via their Fc receptors but had acquired the ability to phagocytize via their C3 receptors. In vivo activation of macrophages' C3 receptors for phagocytosis required T lymphocytes, because macrophages from athymic mice could not be activated by injection of immune complexes. The requirement for both T lymphocytes and immune complexes for activation of macrophages' C3 receptors in vivo is identical to the requirements for activation of macrophages' C3 receptors in vitro, suggesting that the mechanisms we have identified for activation of these receptors in vitro are the same mechanisms by which the receptors are activated for phagocytosis in vivo. The susceptibility of macrophages' Fc receptors to blockade by immune complexes and the activation of their C3 receptors for phagocytosis in a milieu containing immune complexes suggest that it may be macrophages' C3 receptors, not their Fc receptors, that are primarily responsible for promoting phagocytosis of opsonized microorganisms in immune hosts.

scholarly journals Regulation of elastase and plasminogen activator secretion in resident and inflammatory macrophages by receptors for the Fc domain of immunoglobulin G.

1984 ◽  
Vol 159 (1) ◽  
pp. 152-166 ◽  
Author(s):  
R Takemura ◽  
Z Werb
Keyword(s):  
Plasminogen Activator ◽  
Control Level ◽  
Fc Receptors ◽  
Fc Receptor ◽  
Complement Receptor ◽  
Complement Receptors ◽  
Membrane Bound ◽  
Inflammatory Macrophages ◽  
Secretion Rates ◽  
Stimulation Of

We have determined that the interaction of IgG-coated erythrocytes (EIgG) and complement-coated erythrocytes (EIgMC) with macrophage Fc and complement receptors, respectively, modulates the secretion of the neutral proteinases, elastase, and plasminogen activator. EIgG binding and ingestion stimulated secretion of elastase and plasminogen activator less than or equal to 6-fold and 20-fold, respectively, over the 3 d following treatment. Stimulation was dependent on the IgG titer bound to each erythrocyte and was detectable at greater than 6.2 X 10(3) molecules IgG/ erythrocyte (total 0.99 nM IgG in the culture). Cytochalasin B did not inhibit stimulation, indicating that the ingestion of ligands was not necessary. Binding of EIgG to the three subclass-specific Fc receptors (IgG2a, IgG2b/IgG1, IgG3) was effective. Stimulation of elastase secretion required continued exposure of ligands to cells for up to 24 h, whereas production of plasminogen activator, which has plasma membrane-bound forms as well as secreted forms, was stimulated by exposure for 2 h. The stimulated production of elastase and plasminogen activator by triggering Fc receptors was seen only when the initial secretion rates were low. Periodate- or thioglycollate-elicited macrophages, which have high rates of proteinase secretion, were not stimulated further. EIgMC, which are bound but not ingested by resident macrophages, stimulated elastase secretion transiently, and the rate of secretion returned to the control level by 24 h. Therefore, the mode of stimulation of neutral proteinase secretion by complement receptor differed from that of Fc receptor; stimulation by complement receptor possibly involves a limited release of enzyme from intracellular stores, rather than stimulating accelerated synthesis of enzyme. Erythrocytes coated with both complement and IgG showed both the transient increase in elastase typical of complement-mediated secretion and the sustained increase typical of Fc receptor-mediated secretion. These results suggest that macrophage Fc and complement receptors regulate secretion of proteinases by receptor-specific mechanisms.

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