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 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 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 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.

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 Neutrophil surface markers in patients with acute leukemia

Blood ◽  
1981 ◽  
Vol 57 (2) ◽  
pp. 372-376
Author(s):  
BG Hofmeister ◽  
CJ Carrera ◽  
SG Barrett
Keyword(s):  
Acute Leukemia ◽  
Fc Receptors ◽  
Complement Receptor ◽  
Surface Markers ◽  
C3b Receptor ◽  
Neutrophil Surface

The presence of complement and Fc receptors on neutrophils from patients with acute leukemia was investigated at different stages of the leukemic process. Both Fc receptors (Fc-H and Fc-R) and one complement receptor (C3d) were normal when patients were studied at diagnosis, in relapse, and in remission. In contrast, the C3b receptor was significantly reduced on te neutrophils at the time of diagnosis, but returned to normal levels when patients entered remission. Variable amounts of C3b activity were observed in patients relapse, with approximately one-half of the patients showing decreased C3b activity. To determine whether the reduction inC3b receptors was specific for patients at diagnosis, three patients were studied at different times during their diseases. Normal receptor levels were detected in these patients during remission, but the C3b receptor was markedly reduced at diagnosis and at relapse.

scholarly journals Immunohistochemical detection of Fc receptor. I. Light microscopic demonstration of Fc receptor by using soluble immune complexes of peroxidase-antiperoxidase immunoglobulin G.

1977 ◽  
Vol 25 (4) ◽  
pp. 252-258 ◽  
Author(s):  
G Itoh ◽  
S Miura ◽  
I Suzuki
Keyword(s):  
Cell Surface ◽  
Immunoglobulin G ◽  
Immune Complexes ◽  
Surface Characterization ◽  
Fc Receptor ◽  
Frozen Sections ◽  
Microscopic Demonstration ◽  
Lymph Node Cells ◽  
Soluble Immune Complexes ◽  
And Control

The mouse mesenteric lymph node cells (in the cell suspension and frozen sections) were incubated in the soluble immune complexes of peroxidase-antiperoxidase immunoglobulin G. After being washed, they were reacted with diaminobenzidine tetrahydrochloride. Light microscopically brown-colored granules were observed on the cell surface of a proportion of small lymphocytes. In frozen sections, a proportion of small lymphocytes were stained dark brown on the cell surface. Characterization and control experiments suggest that the binding of peroxidase-antiperoxidase immunoglobulin G to the cell surface is mediated by Fc receptor. Peroxidase-antiperoxidase immunoglobulin G, therefore, can be used as in indicator of Fc receptor.

scholarly journals Inhibition of Interleukin 10 Signaling after Fc Receptor Ligation and during Rheumatoid Arthritis

2003 ◽  
Vol 197 (11) ◽  
pp. 1573-1583 ◽  
Author(s):  
Jong-Dae Ji ◽  
Ioannis Tassiulas ◽  
Kyung-Hyun Park-Min ◽  
Ani Aydin ◽  
Ingrid Mecklenbräuker ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Immune Complexes ◽  
Inflammatory Responses ◽  
Fc Receptors ◽  
Interleukin 10 ◽  
Interferon Γ ◽  
Fc Receptor ◽  
Receptor Expression ◽  
Inflammatory Factors

Interleukin-10 (IL-10) is a potent deactivator of myeloid cells that limits the intensity and duration of immune and inflammatory responses. The activity of IL-10 can be suppressed during inflammation, infection, or after allogeneic tissue transplantation. We investigated whether inflammatory factors suppress IL-10 activity at the level of signal transduction. Out of many factors tested, only ligation of Fc receptors by immune complexes inhibited IL-10 activation of the Jak-Stat signaling pathway. IL-10 signaling was suppressed in rheumatoid arthritis joint macrophages that are exposed to immune complexes in vivo. Activation of macrophages with interferon-γ was required for Fc receptor–mediated suppression of IL-10 signaling, which resulted in diminished activation of IL-10–inducible genes and reversal of IL-10–dependent suppression of cytokine production. The mechanism of inhibition involved decreased cell surface IL-10 receptor expression and Jak1 activation and was dependent on protein kinase C delta. These results establish that IL-10 signaling is regulated during inflammation and identify Fc receptors and interferon-γ as important regulators of IL-10 activity. Generation of macrophages refractory to IL-10 can contribute to pathogenesis of inflammatory and infectious diseases characterized by production of interferon-γ and immune complexes.

scholarly journals Loss of Fc receptor activity after culture of human monocytes on surface-bound immune complexes. Mediation by cyclic nucleotides.

1980 ◽  
Vol 151 (1) ◽  
pp. 32-44 ◽  
Author(s):  
C G Ragsdale ◽  
W P Arend
Keyword(s):  
Immune Complexes ◽  
Cytochalasin B ◽  
Fc Receptors ◽  
Phosphodiesterase Inhibitor ◽  
Fc Receptor ◽  
Human Monocytes ◽  
Partial Loss ◽  
Mediated Effects ◽  
Receptor Number ◽  
Partial Reversal

Human monocytes cultured on surface-bound immune complexes exhibited a loss of ability to form rosettes with IgG-sensitized sheep erythrocytes (EA). This loss was not a result of inhibition of Fc receptors by solubilized complexes nor of release of soluble factors by the cells. Loss of EA rosetting was not prevented by culture of monocytes at 4 degrees C, or by treatment with colchicine, cytochalasin B, or local anethetic agents. These results suggested that the loss was not secondary to capping or interiorization of Fc receptors. The results of other studies indicated that the Fc receptors were not damaged by lysosomal enzymes or oxygen radicals. Maintenance of EA rosetting ability of monocytes cultured on surface-bound immune complexes was seen after a 3-h preincubation of the cells in 100 mM 2-deoxy-D-glucose (2dG). A similar preincubation in ATP or in 8-bromoadenosine 3':5'-cyclic monophosphoric acid plus the phosphodiesterase inhibitor methyl isobutyl xanthine led to a partial loss of EA rosetting of cells on plain fibrin and to a partial reversal of the effects of 2dG seen with cells on complexes. We conclude that EA rosetting of monocytes cultured on surface-bound immune complexes is reduced by cyclic nucleotide-mediated effects on Fc receptor number or function.

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