The presence of two Fc receptors on mouse macrophages: evidence from a variant cell line and differential trypsin sensitivity.

Unkeless, Jay C.

doi:10.1084/jem.145.4.931

Cited by 217 publications

(81 citation statements)

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“…Expressed on monocytes and macrophages and induced by interferon-␥ (IFN-␥) 1 on neutrophils (3)(4)(5), Fc␥RI functions by linking the humoral and cellular responses. Although functions mediated by mouse Fc␥RI are less well characterized, cross-linking of human Fc␥RI on myeloid cells leads to events such as tyrosine phosphorylation (6), Ca 2ϩ flux (7), superoxide generation (8), inflammatory mediator release (9), antibody-dependent cellular cytotoxicity (10), and internalization of small immune complexes (11).…”

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Extracellular Mutations of Non-obese Diabetic Mouse FcγRI Modify Surface Expression and Ligand Binding

Gavin

Hamilton

Hogarth

1996

Journal of Biological Chemistry

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The non-obese diabetic mouse (NOD) expresses a unique form of the high affinity receptor for IgG (Fc␥RI), containing multiple mutations that result in substitutions and insertions of amino acids and a truncated cytoplasmic tail. As a result of these major changes, receptor affinity for IgG increases 10-fold over that of wild-type Fc␥RI from BALB/c mice, while the specificity for ligand is retained. Kinetic analysis revealed that while the association rate of IgG with Fc␥RI from NOD mice (Fc␥RI-NOD) and Fc␥RI from BALB/c mice (Fc␥RI-BALB) is similar, IgG bound much more tightly to Fc␥RI-NOD as revealed by a profoundly diminished dissociation rate.Transfection studies demonstrated that Fc␥RI-NOD was expressed at one-tenth of the level of Fc␥RI-BALB. Although mouse Fc␥RI was previously not known to associate with the Fc⑀RI ␥-subunit, transfection of COS-7 cells demonstrates that like human Fc␥RI, mouse Fc␥RI is also able to associate with this signaling subunit. Furthermore, expression levels of Fc␥RI-NOD were not restored by the presence of the Fc⑀RI ␥-subunit. The difference in the levels of expression was mapped to mutations in the extracellular region of Fc␥RI-NOD as replacement of the extracellular domains with those of human Fc␥RI or Fc␥RI-BALB restored expression to that of human Fc␥RI or Fc␥RI-BALB.

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Extracellular Mutations of Non-obese Diabetic Mouse FcγRI Modify Surface Expression and Ligand Binding

Gavin

Hamilton

Hogarth

1996

Journal of Biological Chemistry

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“…To remove the uncoupled hapten, the mixture was passed over a small Sephadex G25 column . The molar ratio of BSA/TNP was 1 :20 (8) . Anti-DNP antibody U7 .6 (IgGl) was conjugated with FITC, and an optimum ratio of FITC-U7 .6/DNP2o-BSA for binding of immune complexes to J774 cells was determined by FACS .…”

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Autoimmune mice make anti-Fc gamma receptor antibodies.

Boros

Chen

Bona

et al. 1990

The Journal of Experimental Medicine

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Hallmarks of autoimmune diseases such as SLE are hypergammaglobulinemia, the production of autoantibodies, and elevated levels of circulating immune complexes . Several mouse strains are used as models of SLE (see reference 1 for review), including NZB, NZB/NZW Ft , MRL/lpr, and BXSB . In human and murine SLE, there is frequently a .pronounced inhibition of macrophage binding and phagocytosis of IgG-sensitized erythrocytes and immune complexes (2-4) . One possible reason for this inhibition is the downmodulation of the macrophage Fcy R after binding of immune complexes . An alternate explanation for the inhibition of Fc yR function might be the binding of anti-Fcy R autoantibody to the macrophage FcyR .In this study, we have used a recombinant truncated FcyR (tFcyR) t to screen murine sera and mAbs for naturally occurring anti-Fcy R antibody. The tFcyR is derived from murine FcyRIIf, and consists of the two external Ig-like domains of muFcy RIIa, but lacks the transmembrane and cytoplasmic domains of the receptor (5) . We report here the presence and characterization of anti-Fcy R antibodies in sera ofsome mice genetically prone to autoimmune diseases and anti-Fc yR hybridomas derived from NZB and motheaten (me") mice.Volume 171 May 1990 1581-1595 AUTOIMMUNE MICE MAKE ANTI-Fcy RECEPTOR ANTIBODIES Materials and Methods mAbs and Sera. The mAbs that we screened for anti-FcyR activity were derived from fusions with spleen cells from old NZB mice or young NZB mice after stimulation with LPS (6) . Other hybridomas screened were from unstimulated viable me' mice (7) . The IgM mAbs were all purified by affinity chromatography on an anti-tc IgG-Sepharose column and were eluted from the column with 0 .1 M glycine HCI, pH 2 .3 . Samples of sera from NZB, NZB/NZW F,, MRL/lpr, and BXSB mice were kindly given to us by Dr. Argyris Theofilopoulos (Scripps Clinic, La Jolla, CA) . Sera from me', tightskin mouse (TSK), C57B1 .6pa/pa, and C58/J were obtained from animals purchased from The Jackson Laboratory (Bar Harbor, ME). Anti-DNP hybridomas DHK109 .3 (IgGl) and DHK10 .12 (IgG2b)

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“…2.4G2 Fab fragments were obtained by papain digestion (13). Dinitrophenol-modified bovine serum albumin (17) The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.…”

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Macrophage membrane potential changes associated with gamma 2b/gamma 1 Fc receptor-ligand binding.

Young¹,

Unkeless²,

Kaback³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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(1,2) and the secretion of arachidonic acid metabolites (3, 4), activated oxygen intermediates (5, 6), and hydrolytic enzymes (5, 7). Like many other receptor-ligand interactions, the initial signal transmitted 'to the cell by the receptor and the subsequent steps leading to the activation of the host defense mechanisms are unclear.Our interest in FcR-mediated events stemmed from the association of early membrane potential (AT) changes with the activation of leukocytes by concanavalin A, phorbol myristic acetate, sand zymosan (8-12 The monoclonal antibody 2.4G2 was prepared as described (13). Other monoclonal antibodies (1.21J, 2D2C, and 2E2A) directed against major membrane proteins of mouse macrophages (16) were similarly purified. 2.4G2 Fab fragments were obtained by papain digestion (13). Dinitrophenol-modified bovine serum albumin (17) (11 mol of DNP per mol of albumin; DNP11-albumin) was separated from free DNP by elution through a DEAE-52 column. Rabbit antibody against DNP (anti-DNP IgG) was prepared by affinity chromatography (17). Soluble immunocomplexes were formed by mixing rabbit anti-DNP IgG and DNP11-albumin at an IgG/DNP11-albumin molar ratio of 6:1. Insoluble immunocomplexes were formed by mixing equal volumes of rabbit anti-horseradish peroxidase (HRP) antiserum (courtesy of R. Steinman, The'Rockefeller University), with 0.25 mg of HRP per ml of phosphate-buffered saline. After 30 min at 40C, the complexes were collected by centrifugation (15 min; Eppendorf Microfuge) and resuspended in buffer at a HRP concentration of 1 mg/ml. The 2.4G2 IgG Fab fragment, intact IgG, and DNP11-albumin were coupled to CNBr-activated Sephadex G-25, superfine 10-40 ,um (14, 16 albumin, DNP-modified bovine serum albumin (molar ratio, 11:1); DNP11-albumin-Sephadex, Sephadex G-25 beads covalently modified with DNP11-albumin; anti-DNP IgG, rabbit antibody against DNP. 1357The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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The presence of two Fc receptors on mouse macrophages: evidence from a variant cell line and differential trypsin sensitivity.

Cited by 217 publications

References 31 publications

Extracellular Mutations of Non-obese Diabetic Mouse FcγRI Modify Surface Expression and Ligand Binding

Extracellular Mutations of Non-obese Diabetic Mouse FcγRI Modify Surface Expression and Ligand Binding

Autoimmune mice make anti-Fc gamma receptor antibodies.

Macrophage membrane potential changes associated with gamma 2b/gamma 1 Fc receptor-ligand binding.

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