Fcγ RII expression and release on resting and activated human B lymphocytes

Sármay, Gabriella; Rozsnyay, Zoltán; Gergely, J.

doi:10.1016/0161-5890(90)90022-r

Cited by 16 publications

(5 citation statements)

References 17 publications

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“…Endogenous and recombinant sFcyR have been shown to have both in vitro and in vivo immunoregulatory activity and functional properties (23)(24)(25)(26)(27)(28)(29)(30)(31)(32). In vitro, endogenous sFcyR are released from cells expressing membrane-bound Fc~rR: activated T cells, B cells, macrophages, monocytes, and granulocytes (33)(34)(35)(36)(37)(38)(39). Soluble Fc'yR can be released by proteolysis of membrane-bound Fc'yR.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Recombinant soluble human Fc gamma RII: production, characterization, and inhibition of the Arthus reaction.

Ierino

Powell

McKenzie

et al. 1993

The Journal of Experimental Medicine

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SummaryA recombinant soluble form of human FcTRII (rsFcTRII) was genetically engineered by the insertion of a termination codon 5' of sequences encoding the transmembrane domain of a human FcTRII eDNA. Chinese hamster ovary cells were transfected with the modified cDNA and the secreted rsFcTRII purified from the tissue culture supernatant (to >95%, assessed by SDS-PAGE) using heat aggregated human immunoglobulin G (IgG) immunoaffinity chromatography. The IgG-purified rsFcTRII was relatively homogeneous (•31,000 Me) whereas the total unpurified rsFcTRII secreted into the tissue culture supernatant was heterogeneous relating to N-linked glycosylation differences. Functional in vitro activity of the rsFcTRII was demonstrated by: (a) ability to bind via the Fc portion of human IgG and mouse IgG (IgG2a>IgGl>>IgG2b); (b) complete inhibition of binding of erythrocytes sensitized with rabbit IgG to membrane-bound FcTRII on K562 cells; and (c) inhibition of the anti-Leu4-induced T cell proliferation assay. Blood dearance and biodistribution studies show the rsFcTRII was excreted predominantly through the kidney in a biphasic manner, with an or-phase (tl/2 '~25 min) and a r-phase (tl/2 '~4.6 h); the kidneys were the only organs noted with tissue-specific accumulation. In vivo, the administration of rsFc~RII significantly inhibited the immune complex-mediated inflammatory response induced by the reversed passive Arthus reaction model in rats. There was a specific and dose-dependent relationship between the amount of rsFcTRII administered, and the reduction in the size and severity of the macroscopic inflammatory lesion. Histological analysis of the skin showed a diffuse neutrophil infiltrate in both control and rsFcTRII-treated rats, however the perivascular infiltrate and the red cell extravasation was less intense in the rsFc~RII-treated group. It is likely that complement activation leads to neutrophil chemotaxis, but neutrophil activation via FcyRII, which results in inflammatory mediator release, is inhibited. The data indicate that rsFcyRII is a potential therapeutic agent for the treatment of antibody or immune complex-mediated tissue damage.

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Section: Discussionmentioning

confidence: 99%

“…Soluble Fc'yR can be released by proteolysis of membrane-bound Fc'yR. (28,29,33), or possibly by alternative RNA splicing of the transmembrane exon (40), and can be stimulated by Ig and cytokines (1). Endogenous mouse sFc'yR has a relative molecular mass of 35-40 kD and reacts with an anti-mouse Fc'yRII mAb, 2.4G2.…”

Section: Discussionmentioning

confidence: 99%

Recombinant soluble human Fc gamma RII: production, characterization, and inhibition of the Arthus reaction.

Ierino

Powell

McKenzie

et al. 1993

The Journal of Experimental Medicine

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“…CD32a is shed from Langerhans cells and also expressed as a soluble form (43). CD32b is shed upon activation of B-cells (44). CD16a and CD16b are likewise shed upon activation of NK cells and neutrophils at a known cleavage site by the metalloprotease ADAM17 (45–48).…”

Section: Receptor Presentation At the Cell Surfacementioning

confidence: 99%

Multiple Variables at the Leukocyte Cell Surface Impact Fc γ Receptor-Dependent Mechanisms

2019

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Fc γ receptors (FcγR) expressed on the surface of human leukocytes bind clusters of immunoglobulin G (IgG) to induce a variety of responses. Many therapeutic antibodies and vaccine-elicited antibodies prevent or treat infectious diseases, cancers and autoimmune disorders by binding FcγRs, thus there is a need to fully define the variables that impact antibody-induced mechanisms to properly evaluate candidate therapies and design new intervention strategies. A multitude of factors influence the IgG-FcγR interaction; one well-described factor is the differential affinity of the six distinct FcγRs for the four human IgG subclasses. However, there are several other recently described factors that may prove more relevant for disease treatment. This review covers recent reports of several aspects found at the leukocyte membrane or outside the cell that contribute to the cell-based response to antibody-coated targets. One major focus is recent reports covering post-translational modification of the FcγRs, including asparagine-linked glycosylation. This review also covers the organization of FcγRs at the cell surface, and properties of the immune complex. Recent technical advances provide high-resolution measurements of these often-overlooked variables in leukocyte function and immune system activation.

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“…This soluble isoform of FcRII has been found in serum (85), and can also be released from Langerhans cells (86). In addition, a soluble FcγRIIb produced by proteolytic cleavage of the membrane-bound receptor, is released from activated B cells (87, 88). For human FcγRIII, both isoforms, FcγRIIIa and FcγRIIIb are released by proteolytic cleavage upon NK cell (89, 90) and neutrophil activation (91, 92), respectively, by various stimuli.…”

Section: Fcγ Receptorsmentioning

confidence: 99%

Fcγ Receptor Heterogeneity in Leukocyte Functional Responses

2017

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Antibodies participate in defense of the organism from all types of pathogens, including viruses, bacteria, fungi, and protozoa. IgG antibodies recognize their associated antigen via their two Fab portions and are in turn recognized though their Fc portion by specific Fcγ receptors (FcγRs) on the membrane of immune cells. Multiple types and polymorphic variants of FcγR exist. These receptors are expressed in many cells types and are also redundant in inducing cell responses. Crosslinking of FcγR on the surface of leukocytes activates several effector functions aimed toward the destruction of pathogens and the induction of an inflammatory response. In the past few years, new evidence on how the particular IgG subclass and the glycosylation pattern of the antibody modulate the IgG–FcγR interaction has been presented. Despite these advances, our knowledge of what particular effector function is activated in a certain cell and in response to a specific type of FcγR remains very limited today. On one hand, each immune cell could be programmed to perform a particular cell function after FcγR crosslinking. On the other, each FcγR could activate a particular signaling pathway leading to a unique cell response. In this review, I describe the main types of FcγRs and our current view of how particular FcγRs activate various signaling pathways to promote unique leukocyte functions.

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Fcγ RII expression and release on resting and activated human B lymphocytes

Cited by 16 publications

References 17 publications

Recombinant soluble human Fc gamma RII: production, characterization, and inhibition of the Arthus reaction.

Recombinant soluble human Fc gamma RII: production, characterization, and inhibition of the Arthus reaction.

Multiple Variables at the Leukocyte Cell Surface Impact Fc γ Receptor-Dependent Mechanisms

Fcγ Receptor Heterogeneity in Leukocyte Functional Responses

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