An immunoglobulin-like receptor, Allergin-1, inhibits immunoglobulin E–mediated immediate hypersensitivity reactions

• Published in: Nature immunology Vol. 11; no. 7; pp. 601 - 607
• Main Authors: 田原 聡子, 渋谷 和子, 渋谷 彰, Hitomi Kaori, Tahara-Hanaoka Satoko, Someya Satoru, Fujiki Akira, Tada Hideaki, Sugiyama Tetsuya, Shibayama Shiro, Shibuya Kazuko, Shibuya Akira
• Format: Journal Article
• Language: English
• Published: New York Nature America Inc 01.07.2010; Nature Publishing Group US; Nature Publishing Group
• Subjects: 631/250/2152/2153/1291; 631/250/249/2510/9; 631/250/2504/223/1630; 631/250/516; Amino Acid Sequence; Anaphylaxis; Animals; Biomedical and Life Sciences; Biomedicine; Bone marrow; Bone Marrow Cells - pathology; Cell activation; Cell Degranulation; Cell receptors; Cells, Cultured; Degranulation; Health aspects; Humans; Hypersensitivity; Hypersensitivity (immediate); Hypersensitivity, Immediate - genetics; Hypersensitivity, Immediate - immunology; Hypersensitivity, Immediate - metabolism; Immunoglobulin E; Immunoglobulin E - metabolism; Immunoglobulins; Immunology; Immunoreceptor tyrosine-based inhibition motif; Immunosuppression; Infectious Diseases; Inositol; Inositol Polyphosphate 5-Phosphatases; Mast cells; Mast Cells - immunology; Mast Cells - metabolism; Mast Cells - pathology; Mice; Mice, Inbred C57BL; Mice, Knockout; Molecular Sequence Data; myo-Inositol-1 (or 4)-monophosphatase; Passive Cutaneous Anaphylaxis - immunology; Phosphoric Monoester Hydrolases - metabolism; Physiological aspects; Protein Tyrosine Phosphatase, Non-Receptor Type 11 - metabolism; Protein Tyrosine Phosphatase, Non-Receptor Type 6 - metabolism; Protein-tyrosine-phosphatase; Receptor Aggregation - immunology; Receptors, IgE - metabolism; Receptors, Immunologic - chemistry; Receptors, Immunologic - genetics; Receptors, Immunologic - immunology; Receptors, Immunologic - metabolism; Risk factors; SHP-1 protein; SHP-2 protein; Japan
• ISSN: 1529-2908; 1529-2916; 1529-2916
• DOI: 10.1038/ni.1886

Anaphylaxis is a life-threatening immediate hypersensitivity reaction triggered by antigen capture by immunoglobulin E (IgE) bound to the high-affinity IgE receptor (FcεRI) on mast cells. However, the regulatory mechanism of mast cell activation is not completely understood. Here we identify an immunoglobulin-like receptor, Allergin-1, that contains an immunoreceptor tyrosine-based inhibitory motif (ITIM)-like domain, and show it was preferentially expressed on mast cells. Mouse Allergin-1 recruited the tyrosine phosphatases SHP-1 and SHP-2 and the inositol phosphatase SHIP. Coligation of Allergin-1 and FcεRI suppressed IgE-mediated degranulation of bone marrow–derived cultured mast cells. Moreover, mice deficient in Allergin-1 developed enhanced passive systemic and cutaneous anaphylaxis. Thus, Allergin-1 suppresses IgE-mediated, mast cell–dependent anaphylaxis in mice.