Immunohistochemical detection of Fc receptor. II. Electron microscopic demonstration of Fc receptor by using soluble immune complexes of ferritin-antiferritin immunoglobulin G.

The mouse mesenteric lymph node cells were incubated in the soluble immune complexes of ferritin-antiferritin immunoglobulin G at 37 degrees C for 20 min. After being washed, postfixed with OsO4 and dehydrated by degraded ethanol series, the lymph node cells were observed by electron microscope. Apprroximately 15% of the cells (mainly composed of small lymphocytes) bound ferritin particles to the cell surface. The distribution pattern of the binding of ferritin particles (ferritin-antiferritin immunoglobulin G) took the form of discrete patches of irregular distribution interspaced with unlabeled portions. The electron microscopic features of ferritin particles (ferritin-antiferritin immunoglobulin G) attached to the cell surface suggest that a structure of constant conformation (Fc receptor) situated in the cell membrane takes part in the binding of ferritin-antiferritin immunoglobulin G.

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

Journal of Histochemistry & Cytochemistry ◽

10.1177/25.4.404351 ◽

1977 ◽

Vol 25 (4) ◽

pp. 252-258 ◽

Cited By ~ 11

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.

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A cell-mediated reaction against glomerular-bound immune complexes.

Journal of Experimental Medicine ◽

10.1084/jem.150.6.1410 ◽

1979 ◽

Vol 150 (6) ◽

pp. 1410-1420 ◽

Cited By ~ 61

Author(s):

A K Bhan ◽

A B Collins ◽

E E Schneeberger ◽

R T McCluskey

Keyword(s):

Lymph Node ◽

T Cell ◽

Immune Complexes ◽

Gamma Globulin ◽

Mononuclear Phagocytes ◽

A Cell ◽

Lymph Node Cells ◽

Soluble Immune Complexes ◽

Histologic Changes ◽

Glomerular Capillaries

Lewis rats were given a single i.v. injection of soluble immune complexes containing human serum albumin (HSA) and rabbit anti-HSA antibodies, prepared in antigen excess. This resulted in localization of HSA and rabbit gamma globulin (RGG) in glomerular mesangial regions without producing definite histologic changes. 24 h after the injection of immune complexes, groups of these rats received lymph node cells or T-cell preparations from syngeneic donors sensitized to RGG, HSA, or ovalbumin; another group received no cells. All of these groups and a group of normal control rats were given injections of [3H]thymidine at 18, 27, and 44 h. The animals were killed 48 h after the time of cell transfer. In histologic sections, glomerular abnormalities were found only in some of the animals that had received immune complexes and lymph node cells or T-cell populations from donors sensitized to HSA or RGG; the lesions were characterized by focal and segmental increase in cells in mesangial regions. Autoradiographs revealed significantly greater numbers of labeled cells in mesangial regions and glomerular capillaries in the groups that had received immune complexes and cells from HSA- or RGG-sensitized donors than in any of the other groups. Electronmicroscopic studies suggested that the increase in cellularity in mesangial regions resulted from an influx of mononuclear phagocytes. The findings indicate that cell-mediated reactions can be initiated by the interaction between sensitized T lymphocytes and antigens present in immune complexes within mesangial regions.

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Immunohistochemical demonstration of Fc receptors of human lymph node cells using peroxidase-antiperoxidase (IgG).

Journal of Histochemistry & Cytochemistry ◽

10.1177/28.3.6986436 ◽

1980 ◽

Vol 28 (3) ◽

pp. 271-275 ◽

Cited By ~ 2

Author(s):

G Itoh

Keyword(s):

Lymph Node ◽

Cell Surface ◽

Microscopic Examination ◽

Fc Receptors ◽

Electron Microscopic Examination ◽

Reaction Products ◽

Electron Microscopic ◽

Regional Lymph Nodes ◽

Human Lymph Node ◽

Lymph Node Cells

Human lymph node cells, prepared from regional lymph nodes excised from four patients with gastric cancer, were incubated with peroxidase-antiperoxidase (IgG) (PAPIgG). After being washed, they were reacted with diaminobenzidine tetrahydrochloride in the presence of H2O2. Light microscopic examination revealed that a certain proportion of lymph node cells (18.2-32.2%) were labeled on their cell surface with brown-colored reaction products and that the labeled cells were composed of small lymphocytes. Electron microscopic examination demonstrated electron-dense irregular-shaped aggregates of reaction products on the cell surface of lymphocytes. Characterization experiments confirmed that the immune complexes of PAPIgG bound specifically with Fc receptors. PAPIgG, therefore, can be used as a specific indicator for Fc receptor of human lymph node cells.

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

Journal of Experimental Medicine ◽

10.1084/jem.152.4.905 ◽

1980 ◽

Vol 152 (4) ◽

pp. 905-919 ◽

Cited By ~ 42

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.

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BINDING OF SOLUBLE IMMUNE COMPLEXES TO HUMAN LYMPHOBLASTOID CELLS

Journal of Experimental Medicine ◽

10.1084/jem.140.4.877 ◽

1974 ◽

Vol 140 (4) ◽

pp. 877-894 ◽

Cited By ~ 86

Author(s):

Argyrios N. Theofilopoulos ◽

Frank J. Dixon ◽

Viktor A. Bokisch

Keyword(s):

Cell Surface ◽

B Cell ◽

Cell Lines ◽

Immune Complexes ◽

Surface Membrane ◽

Raji Cells ◽

Human Lymphoblastoid Cell ◽

C Cell ◽

A Cell ◽

Soluble Immune Complexes

In the present work we studied the expression of membrane-bound Ig (MBIg) as well as receptors for IgG Fc and complement on nine human lymphoblastoid cell lines. When MBIg and receptors for IgG Fc were compared, four categories of cell lines could be distinguished: (a) cell lines having both MBIg and receptors for IgG Fc, (b) cell lines having MBIg but lacking receptors for IgG Fc, (c) cell lines lacking MBIg but having receptors for IgG Fc, and (d) cell lines lacking both MBIg and receptors for IgG Fc. Two types of receptors for complement could be detected on the cell lines studied, one for C3-C3b and one for C3d. When sensitized red cells carrying C3b or C3d were used for rosette tests, three categories of cell lines could be distinguished: (a) cell lines having receptors for C3b and C3d, (b) cell lines having receptors only for C3d and (c) cell lines lacking both receptors. However, when a more sensitive immunofluorescent method was used instead of the rosette technique, it was found that cell lines unable to form rosettes with EAC1423bhu were able to bind soluble C3 or C3b which indicated the presence of these receptors on the cell surface. Inhibition experiments showed that receptors for C3-C3b and receptors for C3d are distinct and that receptors for C3-C3b and C3d are different from receptors for IgG Fc. A cell line (Raji) without MBIg but with receptors for IgG Fc, C3-C3b, and C3d was selected for use in studying the binding mechanism of soluble immune complexes to cell surface membrane. Aggregated human gamma globulin was used in place of immune complexes. Immune complexes containing complement bind to Raji cells only via receptors for complement, namely receptors for C3-C3b and C3d. Binding of immune complexes containing complement to cells is much greater than that of complexes without complement. Immune complexes bound to cells via receptors for complement can be partially released from the cell surface by addition of normal human serum as well as isolated human C3 or C3b. We postulate that such release is due to competition of immune complex bound C3b and free C3 or C3b for the receptors on Raji cells.

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Immune reactions in polysaccharide media. The composition of the antigen–antibody complexes in the precipitin reaction

Biochemical Journal ◽

10.1042/bj1140141 ◽

1969 ◽

Vol 114 (1) ◽

pp. 141-144 ◽

Cited By ~ 13

Author(s):

Krister Hellsing

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Immunoglobulin G ◽

Immune Complexes ◽

Aggregate Size ◽

Precipitin Reaction ◽

Soluble Immune Complexes ◽

Immune Aggregates ◽

Antigen Antibody ◽

Free Antigen

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.

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