Open AccessAn immunoglobulin-like receptor, Allergin-1, inhibits immunoglobulin E–mediated immediate hypersensitivity reactions
Author(s) -
Kaori Hitomi,
Satoko TaharaHanaoka,
Satoru Someya,
Akira Fujiki,
Hideaki Tada,
Tetsuya Sugiyama,
Shiro Shibayama,
Kazuko Shibuya,
Akira Shibuya
Publication year - 2010
Publication title -
nature immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.074
H-Index - 388
eISSN - 1529-2916
pISSN - 1529-2908
DOI - 10.1038/ni.1886
Subject(s) - degranulation , immunoglobulin e , mast cell , antibody , protein tyrosine phosphatase , immunoreceptor tyrosine based activation motif , receptor , immunology , anaphylaxis , chemistry , fc receptor , allergy , microbiology and biotechnology , biology , biochemistry , sh2 domain
Anaphylaxis is a life-threatening immediate hypersensitivity reaction triggered by antigen capture by immunoglobulin E (IgE) bound to the high-affinity IgE receptor (FcvarepsilonRI) 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 FcvarepsilonRI 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.
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