Mechanism of action of immunoglobulin: Sialylated IgG

Toshiyuki Takai

doi:10.1007/978-4-431-56039-5_25

Mechanism of action of immunoglobulin: Sialylated IgG

Toshiyuki Takai

Division of Aging Science

Research output: Chapter in Book/Report/Conference proceeding › Chapter

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.

Original language	English
Title of host publication	Kawasaki Disease
Subtitle of host publication	Current Understanding of the Mechanism and Evidence-Based Treatment
Publisher	Springer Japan
Pages	223-230
Number of pages	8
ISBN (Electronic)	9784431560395
ISBN (Print)	9784431560371
DOIs	https://doi.org/10.1007/978-4-431-56039-5_25
Publication status	Published - 2016 Jan 1

Keywords

DC-SIGN
Dendritic cell
Fc receptor
Lectin
Oligosaccharide

ASJC Scopus subject areas

Medicine(all)
Immunology and Microbiology(all)

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10.1007/978-4-431-56039-5_25

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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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AB - 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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KW - Fc receptor

KW - Lectin

KW - Oligosaccharide

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BT - Kawasaki Disease

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ER -

Mechanism of action of immunoglobulin: Sialylated IgG

Abstract

Keywords

ASJC Scopus subject areas

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