Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation
By Y. Kaneko, F. Nimmerjahn, J. Ravetch. Science, 2006
1,795 citations recorded by the source corpus.
Subfields: Immunology, Molecular Biology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/b528fd03fd3d3d81e45c3942f28445e4c46ce2dd
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In Immunology
- F. Nimmerjahn
- R. Jefferis
- J. Ravetch
- Gabriel A. Rabinovich
- K. Ohtsubo
- I. Waldhauer
- J. Marth
- Y. Kooyk
In Molecular Biology
- R. Jefferis
- F. Nimmerjahn
- J. Ravetch
- Gabriel A. Rabinovich
- Kentaro Shimizu
- K. Ohtsubo
- J. Marth
- Y. Kooyk
In Radiology, Nuclear Medicine and Imaging
Citations in the corpus
- Post-translational modifications in the context of therapeutic proteins (2006, neutral): “A recent study has shown, in a mouse model, that the presence of terminal sialic acid residues can compromise FcγR-mediated responses but enhance anti-inflammatory activit”
- Unique carbohydrate–carbohydrate interactions are required for high affinity binding between FcγRIII and antibodies lacking core fucose (2011, background): “In contrast, Fc-oligosaccharide sialylation, shown to reduce binding to Fcγ receptors and in addition facilitate binding to the lectin specific Icam-3 grabbing nonintegrin-related 1 (SIGN-R1), has been associated with an anti-inflammatory activity of immunoglobulins (7, 8).”
- IgG Subclasses and Allotypes: From Structure to Effector Functions (2014, background): “In proof of this, actual comparisons of IgG with or without Fc-sialylation have confirmed this (124), and mouse IgG decreased affinity to mouse FcγR in general (125), although systematic analyzes of the importance of this for human IgG-FcγR binding is lacking.”
- Fcγ receptors as regulators of immune responses (2008, background): “Evidence that this sugar residue is involved in immune regulatory processes was obtained by studying the mechanism of the anti-inflammatory activity of IVIG therap”
- Intravenous gammaglobulin suppresses inflammation through a novel TH2 pathway (2011, background): “This anti-inflammatory activity of intravenous immunoglobulin is triggered by a minor population of IgG crystallizable fragments (Fcs), with glycans terminating in a2,6 sialic acids (sFc) that target myeloid regulatory cells expressing the lectin dendritic-cell-specific ICAM-3 grabbing non-integrin ”
- Protein-glycan interactions in the control of innate and adaptive immune responses (2008, background): “Hence, differential sialylation of cell surface glycoproteins may serve as an 'on-off' switch that controls the decisions between immune cell responsiveness or toleranc”
- Glycosylation in cellular mechanisms of health and disease. (2006, background): “In addition, the anti-inflammatory property of IgG binding to Fc receptors is elevated among the subset of total circulating IgGs that are sialylated, compared to the fraction of IgGs that have fewer or no sialic acid linkages (Kaneko et al., 2006).”
- IgEb immune complexes activate macrophages through FcγRIV binding (2007, background): “Sialylation of the immunoglobulin Fc regions may modify their binding affinities with FcR”
- Glycosylation as a strategy to improve antibody-based therapeutics (2009, background): “Small but possibly significant differences in the affinities of sialylated and non-sialylated IgG Fc for FcγR have been reporte”