There Is (Scientific) Strength in Numbers: A Comprehensive Quantitation of Fc Gamma Receptor Numbers on Human and Murine Peripheral Blood Leukocytes

Kerntke, Christina; Nimmerjahn, Falk; Biburger, Markus

doi:10.3389/fimmu.2020.00118

Cited by 70 publications

(74 citation statements)

References 79 publications

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“…In addition, the inhibitory receptor FcγRIIB is expressed on B cells as well as monocytes and macrophages; mouse FcγRIII was described on NK cells, neutrophils, monocytes, and macrophages (31). In addition to relative expression patterns, in a recent comprehensive study using mouse and human peripheral blood, Kerntke et al quantified the number of cell surface FcγR on derived immune cells including potential APCs such as B cells and monocytes (39). The authors found that on human monocytes, more FcγRIIA molecules were expressed compared to FcγRIIB.…”

Section: Overview Of Fcγrs and Igg Bindingmentioning

confidence: 99%

Fc Gamma Receptors and Their Role in Antigen Uptake, Presentation, and T Cell Activation

2020

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The cellular uptake, intracellular processing, and presentation of foreign antigen are crucial processes for eliciting an effective adaptive host response to the majority of pathogens. The effective recognition of antigen by T cells requires that it is first processed and then presented on MHC molecules that are expressed on other cells. A critical step leading to the presentation of antigen is delivering the foreign cargo to an intracellular compartment where the antigen can be processed and loaded onto MHC molecules. Fc-gamma receptors (FcγRs) recognize IgG-coated targets, such as opsonized pathogens or immune complexes (ICs). Cross-linking leads to internalization of the cargo with associated activation of downstream signaling cascades. FcγRs vary in their affinity for IgG and intracellular trafficking, and therefore have an opportunity to regulate antigen presentation by controlling the shuttling and processing of their cargos. In this way, they critically influence physiological and pathophysiological adaptive immune cell functions. In this review, we will cover the contribution of FcγRs to antigenpresentation with a focus on the intracellular trafficking of IgG-ICs and the pathways that support this function. We will also discuss genetic evidence linking FcγR biology to immune cell activation and autoimmune processes as exemplified by systemic lupus erythematosus (SLE).

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Section: Overview Of Fcγrs and Igg Bindingmentioning

confidence: 99%

Fc Gamma Receptors and Their Role in Antigen Uptake, Presentation, and T Cell Activation

2020

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“…FcγRIIa is widely expressed on innate immune cells (including neutrophils and both monocyte subsets). These cell types may also express the closely related inhibitory FcγRIIb (95,96). This further complicates interpretation of data because of high homology of the extracellular domains.…”

Section: Fcγriiamentioning

confidence: 99%

Impact of Plasma Membrane Domains on IgG Fc Receptor Function

et al. 2020

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Lipid cell membranes not only represent the physical boundaries of cells. They also actively participate in many cellular processes. This contribution is facilitated by highly complex mixtures of different lipids and incorporation of various membrane proteins. One group of membrane-associated receptors are Fc receptors (FcRs). These cell-surface receptors are crucial for the activity of most immune cells as they bind immunoglobulins such as immunoglobulin G (IgG). Based on distinct mechanisms of IgG binding, two classes of Fc receptors are now recognized: the canonical type I FcγRs and select C-type lectin receptors newly referred to as type II FcRs. Upon IgG immune complex induced cross-linking, these receptors are known to induce a multitude of cellular effector responses in a cell-type dependent manner, including internalization, antigen processing, and presentation as well as production of cytokines. The response is also determined by specific intracellular signaling domains, allowing FcRs to either positively or negatively modulate immune cell activity. Expression of cell-type specific combinations and numbers of receptors therefore ultimately sets a threshold for induction of effector responses. Mechanistically, receptor cross-linking and localization to lipid rafts, i.e., organized membrane microdomains enriched in intracellular signaling proteins, were proposed as major determinants of initial FcR activation. Given that immune cell membranes might also vary in their lipid compositions, it is reasonable to speculate, that the cell membrane and especially lipid rafts serve as an additional regulator of FcR activity. In this article, we aim to summarize the current knowledge on the interplay of lipid rafts and IgG binding FcRs with a focus on the plasma membrane composition and receptor localization in immune cells, the proposed mechanisms underlying this localization and consequences for FcR function with respect to their immunoregulatory capacity.

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“…Glycosylation of IgG molecules is essential for its binding with all receptors through the maintenance of an open conformation of the two heavy chains, whereas deglycosylated IgG antibodies are unable to mediate the inflammatory response triggered in vivo. A therapeutic application of gamma globulins intravenously indicates how these acts as anti-inflammatory [55].…”

Section: Immunity and Inflammationmentioning

confidence: 99%

Protein Glycosylation Investigated by Mass Spectrometry: An Overview

Illiano

Pinto

Melchiorre

et al. 2020

Cells

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The protein glycosylation is a post-translational modification of crucial importance for its involvement in molecular recognition, protein trafficking, regulation, and inflammation. Indeed, abnormalities in protein glycosylation are correlated with several disease states such as cancer, inflammatory diseases, and congenial disorders. The understanding of cellular mechanisms through the elucidation of glycan composition encourages researchers to find analytical solutions for their detection. Actually, the multiplicity and diversity of glycan structures bond to the proteins, the variations in polarity of the individual saccharide residues, and the poor ionization efficiencies make their detection much trickier than other kinds of biopolymers. An overview of the most prominent techniques based on mass spectrometry (MS) for protein glycosylation (glycoproteomics) studies is here presented. The tricks and pre-treatments of samples are discussed as a crucial step prodromal to the MS analysis to improve the glycan ionization efficiency. Therefore, the different instrumental MS mode is also explored for the qualitative and quantitative analysis of glycopeptides and the glycans structural composition, thus contributing to the elucidation of biological mechanisms.

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There Is (Scientific) Strength in Numbers: A Comprehensive Quantitation of Fc Gamma Receptor Numbers on Human and Murine Peripheral Blood Leukocytes

Cited by 70 publications

References 79 publications

Fc Gamma Receptors and Their Role in Antigen Uptake, Presentation, and T Cell Activation

Fc Gamma Receptors and Their Role in Antigen Uptake, Presentation, and T Cell Activation

Impact of Plasma Membrane Domains on IgG Fc Receptor Function

Protein Glycosylation Investigated by Mass Spectrometry: An Overview

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