Abstract
Glycosylation of IgG, including sialylation of the Fc region, influences binding of IgG to receptors. In addition to the classical Fc receptor members, we now know of several sugar-binding lectins that recognize sialylated oligosaccharides of IgG. These lectins, particularly human dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN), may regulate immune reactions and are thus candidate molecules in the initiation of the sequence of IVIG-mediated anti-inflammatory events. This chapter reviews the emerging role of sialylated IgG Fc in the IVIG-mediated therapeutic effect, in particular the importance of DC-SIGN-initiated events.
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Acknowledgements
The author thanks Nicholas Halewood for editorial assistance. This work is supported in part by a Grant-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology of Japan (to TT).
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Takai, T. (2017). Mechanism of Action of Immunoglobulin: Sialylated IgG. In: Saji, B., Newburger, J., Burns, J., Takahashi, M. (eds) Kawasaki Disease. Springer, Tokyo. https://doi.org/10.1007/978-4-431-56039-5_25
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DOI: https://doi.org/10.1007/978-4-431-56039-5_25
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