Literature DB >> 7835961

The functional activity of human monocytes passively sensitized with monoclonal anti-D suggests a novel role for Fc gamma RI in the immune destruction of blood cells.

H L Griffiths1, B M Kumpel, C J Elson, A G Hadley.   

Abstract

The role of Fc gamma RI in the immune destruction of blood cells is uncertain as serum IgG levels are sufficient to competitively inhibit interactions between this high-affinity receptor and sensitized red cells. In the current study, it is proposed that, rather than functioning as a receptor for opsonized red cells, Fc gamma RI might, under appropriate conditions, mediate the passive sensitization (or 'arming') of human macrophages with IgG antibodies resulting in the in vivo destruction of unsensitized cells expressing the corresponding antigen. To examine this hypothesis, Fc gamma RI-bearing human monocytes and U937 cells were first passively sensitized by incubation in vitro with human monoclonal anti-D, and then incubated with D-positive red cells. The uptake of monoclonal anti-D by U937 cells was rapid and, in the presence of 2.5 micrograms/ml IgG1 or IgG3 anti-D, was almost complete after 5 min at 37 degrees. Subsequent incubation of passively sensitized U937 cells in an IgG-free medium for 1 hr at 37 degrees resulted in the loss from the cell surface of approximately 50% cell-bound IgG; the remaining cell-bound IgG was lost more slowly despite repeated washing. In functional assays, passively sensitized monocytes (M-IgG) mediated adherent, phagocytic and chemiluminescent (CL) responses to D-positive red cells. After incubation of M-IgG in 50% v/v fresh normal human serum (FNHS) for 2 hr, sufficient anti-D remained bound to monocytes to promote the adherence of red cells. The adherence and phagocytosis of red cells by M-IgG was enhanced by the simultaneous addition of 50% FNHS, probably owing to the binding of low levels of C3bi to red cells. In contrast, phagocytic and CL responses of unsensitized monocytes to anti-D-sensitized red cells (E-IgG) were abrogated in the presence of 0.25% v/v FNHS, presumably owing to blocking of Fc gamma RI by IgG. It is considered that in vivo, Fc gamma RI may mediate the passive sensitization of macrophages in close proximity with antibody-secreting cells in the reticular network of the splenic cords. Once 'armed' in this way, macrophages may destroy cells expressing the appropriate antigen.

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Year:  1994        PMID: 7835961      PMCID: PMC1415029     

Source DB:  PubMed          Journal:  Immunology        ISSN: 0019-2805            Impact factor:   7.397


  28 in total

1.  The adsorption of antigen by spleen cells previously treated with antiserum in vitro.

Authors:  S V BOYDEN; E SORKIN
Journal:  Immunology       Date:  1960-07       Impact factor: 7.397

2.  Quantitative influence of antibody and complement coating of red cells on monocyte-mediated cell lysis.

Authors:  R J Kurlander; W F Rosse; G L Logue
Journal:  J Clin Invest       Date:  1978-05       Impact factor: 14.808

Review 3.  The receptor with high affinity for immunoglobulin E.

Authors:  H Metzger; G Alcaraz; R Hohman; J P Kinet; V Pribluda; R Quarto
Journal:  Annu Rev Immunol       Date:  1986       Impact factor: 28.527

4.  Treatment of refractory immune thrombocytopenic purpura with an anti-Fc gamma-receptor antibody.

Authors:  S B Clarkson; J B Bussel; R P Kimberly; J E Valinsky; R L Nachman; J C Unkeless
Journal:  N Engl J Med       Date:  1986-05-08       Impact factor: 91.245

Review 5.  The receptor on mast cells and related cells with high affinity for IgE.

Authors:  H Metzger
Journal:  Contemp Top Mol Immunol       Date:  1983

6.  The IgG subclasses of red cell antibodies and relationship to monocyte binding.

Authors:  N Abramson; P H Schur
Journal:  Blood       Date:  1972-10       Impact factor: 22.113

7.  Three rat monoclonal antibodies to human C3.

Authors:  P J Lachmann; R G Oldroyd; C Milstein; B W Wright
Journal:  Immunology       Date:  1980-11       Impact factor: 7.397

8.  Membrane-bound immunoglobulins and complement components on young and old red cells.

Authors:  J Freedman
Journal:  Transfusion       Date:  1984 Nov-Dec       Impact factor: 3.157

9.  Recombinant immune interferon increases immunoglobulin G Fc receptors on cultured human mononuclear phagocytes.

Authors:  P M Guyre; P M Morganelli; R Miller
Journal:  J Clin Invest       Date:  1983-07       Impact factor: 14.808

10.  Characterization of the Fc receptor for IgG on a human macrophage cell line, U937.

Authors:  C L Anderson; G N Abraham
Journal:  J Immunol       Date:  1980-12       Impact factor: 5.422

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  5 in total

Review 1.  Functions of the Fc receptors for immunoglobulin G.

Authors:  B K Flesch; J Neppert
Journal:  J Clin Lab Anal       Date:  2000       Impact factor: 2.352

2.  Monocyte-bound monoclonal antibodies inhibit the Fc gamma RI-mediated phagocytosis of sensitized red cells: the efficiency and mechanism of inhibition are determined by the nature of the antigen.

Authors:  S L Shepard; A G Hadley
Journal:  Immunology       Date:  1997-02       Impact factor: 7.397

3.  Enhanced opsonisation of Rhesus D-positive human red blood cells by recombinant polymeric immunoglobulin G anti-G antibodies.

Authors:  Dylana Díaz-Solano; Jaheli Fuenmayor; Ramon F Montaño
Journal:  Blood Transfus       Date:  2017-05-30       Impact factor: 3.443

4.  Investigation of whether the acute hemolysis associated with Rh(o)(D) immune globulin intravenous (human) administration for treatment of immune thrombocytopenic purpura is consistent with the acute hemolytic transfusion reaction model.

Authors:  Ann Reed Gaines; Hallie Lee-Stroka; Karen Byrne; Dorothy E Scott; Lynne Uhl; Ellen Lazarus; David F Stroncek
Journal:  Transfusion       Date:  2009-02-09       Impact factor: 3.157

Review 5.  Red blood cell destruction in autoimmune hemolytic anemia: role of complement and potential new targets for therapy.

Authors:  Sigbjørn Berentsen; Tatjana Sundic
Journal:  Biomed Res Int       Date:  2015-01-29       Impact factor: 3.411

  5 in total

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