An immunoglobulin-like receptor, Allergin-1, inhibits immunoglobulin E–mediated immediate hypersensitivity reactions
Immunoglobulin E–mediated crosslinking of FɛRI receptors can lead to life-threatening anaphylaxis in sensitized people. Shibuya and colleagues identify a phosphatase-recruiting inhibitory receptor, Allergin-1, that suppresses mast cell degranulation induced by immunoglobulin E–FɛRI. Anaphylaxis is a...
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Veröffentlicht in: | Nature immunology 2010-07, Vol.11 (7), p.601-607 |
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creator | Hitomi, Kaori Tahara-Hanaoka, Satoko Someya, Satoru Fujiki, Akira Tada, Hideaki Sugiyama, Tetsuya Shibayama, Shiro Shibuya, Kazuko Shibuya, Akira |
description | Immunoglobulin E–mediated crosslinking of FɛRI receptors can lead to life-threatening anaphylaxis in sensitized people. Shibuya and colleagues identify a phosphatase-recruiting inhibitory receptor, Allergin-1, that suppresses mast cell degranulation induced by immunoglobulin E–FɛRI.
Anaphylaxis is a life-threatening immediate hypersensitivity reaction triggered by antigen capture by immunoglobulin E (IgE) bound to the high-affinity IgE receptor (FcɛRI) 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 FcɛRI 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. |
doi_str_mv | 10.1038/ni.1886 |
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Anaphylaxis is a life-threatening immediate hypersensitivity reaction triggered by antigen capture by immunoglobulin E (IgE) bound to the high-affinity IgE receptor (FcɛRI) 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 FcɛRI 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.</description><identifier>ISSN: 1529-2908</identifier><identifier>EISSN: 1529-2916</identifier><identifier>DOI: 10.1038/ni.1886</identifier><identifier>PMID: 20526344</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>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</subject><ispartof>Nature immunology, 2010-07, Vol.11 (7), p.601-607</ispartof><rights>Springer Nature America, Inc. 2010</rights><rights>COPYRIGHT 2010 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jul 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c550t-d19dcb809c4516d57b43571ae4d276a56764717a36c09f1e7dd9f25879e34c323</citedby><cites>FETCH-LOGICAL-c550t-d19dcb809c4516d57b43571ae4d276a56764717a36c09f1e7dd9f25879e34c323</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/ni.1886$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/ni.1886$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20526344$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hitomi, Kaori</creatorcontrib><creatorcontrib>Tahara-Hanaoka, Satoko</creatorcontrib><creatorcontrib>Someya, Satoru</creatorcontrib><creatorcontrib>Fujiki, Akira</creatorcontrib><creatorcontrib>Tada, Hideaki</creatorcontrib><creatorcontrib>Sugiyama, Tetsuya</creatorcontrib><creatorcontrib>Shibayama, Shiro</creatorcontrib><creatorcontrib>Shibuya, Kazuko</creatorcontrib><creatorcontrib>Shibuya, Akira</creatorcontrib><title>An immunoglobulin-like receptor, Allergin-1, inhibits immunoglobulin E–mediated immediate hypersensitivity reactions</title><title>Nature immunology</title><addtitle>Nat Immunol</addtitle><addtitle>Nat Immunol</addtitle><description>Immunoglobulin E–mediated crosslinking of FɛRI receptors can lead to life-threatening anaphylaxis in sensitized people. Shibuya and colleagues identify a phosphatase-recruiting inhibitory receptor, Allergin-1, that suppresses mast cell degranulation induced by immunoglobulin E–FɛRI.
Anaphylaxis is a life-threatening immediate hypersensitivity reaction triggered by antigen capture by immunoglobulin E (IgE) bound to the high-affinity IgE receptor (FcɛRI) 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 FcɛRI 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.</description><subject>631/250/2152/2153/1291</subject><subject>631/250/249/2510/9</subject><subject>631/250/2504/223/1630</subject><subject>631/250/516</subject><subject>Amino Acid Sequence</subject><subject>Anaphylaxis</subject><subject>Animals</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bone marrow</subject><subject>Bone Marrow Cells - pathology</subject><subject>Cell activation</subject><subject>Cell Degranulation</subject><subject>Cell receptors</subject><subject>Cells, Cultured</subject><subject>Degranulation</subject><subject>Health aspects</subject><subject>Humans</subject><subject>Hypersensitivity</subject><subject>Hypersensitivity (immediate)</subject><subject>Hypersensitivity, Immediate - genetics</subject><subject>Hypersensitivity, Immediate - immunology</subject><subject>Hypersensitivity, Immediate - metabolism</subject><subject>Immunoglobulin E</subject><subject>Immunoglobulin E - metabolism</subject><subject>Immunoglobulins</subject><subject>Immunology</subject><subject>Immunoreceptor tyrosine-based inhibition motif</subject><subject>Immunosuppression</subject><subject>Infectious Diseases</subject><subject>Inositol</subject><subject>Inositol Polyphosphate 5-Phosphatases</subject><subject>Mast cells</subject><subject>Mast Cells - immunology</subject><subject>Mast Cells - metabolism</subject><subject>Mast Cells - pathology</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Mice, Knockout</subject><subject>Molecular Sequence Data</subject><subject>myo-Inositol-1 (or 4)-monophosphatase</subject><subject>Passive Cutaneous Anaphylaxis - immunology</subject><subject>Phosphoric Monoester Hydrolases - metabolism</subject><subject>Physiological aspects</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 11 - metabolism</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 6 - metabolism</subject><subject>Protein-tyrosine-phosphatase</subject><subject>Receptor Aggregation - 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pathology</topic><topic>Cell activation</topic><topic>Cell Degranulation</topic><topic>Cell receptors</topic><topic>Cells, Cultured</topic><topic>Degranulation</topic><topic>Health aspects</topic><topic>Humans</topic><topic>Hypersensitivity</topic><topic>Hypersensitivity (immediate)</topic><topic>Hypersensitivity, Immediate - genetics</topic><topic>Hypersensitivity, Immediate - immunology</topic><topic>Hypersensitivity, Immediate - metabolism</topic><topic>Immunoglobulin E</topic><topic>Immunoglobulin E - metabolism</topic><topic>Immunoglobulins</topic><topic>Immunology</topic><topic>Immunoreceptor tyrosine-based inhibition motif</topic><topic>Immunosuppression</topic><topic>Infectious Diseases</topic><topic>Inositol</topic><topic>Inositol Polyphosphate 5-Phosphatases</topic><topic>Mast cells</topic><topic>Mast Cells - immunology</topic><topic>Mast Cells - metabolism</topic><topic>Mast Cells - pathology</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Knockout</topic><topic>Molecular Sequence Data</topic><topic>myo-Inositol-1 (or 4)-monophosphatase</topic><topic>Passive Cutaneous Anaphylaxis - immunology</topic><topic>Phosphoric Monoester Hydrolases - metabolism</topic><topic>Physiological aspects</topic><topic>Protein Tyrosine Phosphatase, Non-Receptor Type 11 - metabolism</topic><topic>Protein Tyrosine Phosphatase, Non-Receptor Type 6 - metabolism</topic><topic>Protein-tyrosine-phosphatase</topic><topic>Receptor Aggregation - immunology</topic><topic>Receptors, IgE - metabolism</topic><topic>Receptors, Immunologic - chemistry</topic><topic>Receptors, Immunologic - genetics</topic><topic>Receptors, Immunologic - immunology</topic><topic>Receptors, Immunologic - metabolism</topic><topic>Risk factors</topic><topic>SHP-1 protein</topic><topic>SHP-2 protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hitomi, Kaori</creatorcontrib><creatorcontrib>Tahara-Hanaoka, Satoko</creatorcontrib><creatorcontrib>Someya, Satoru</creatorcontrib><creatorcontrib>Fujiki, Akira</creatorcontrib><creatorcontrib>Tada, Hideaki</creatorcontrib><creatorcontrib>Sugiyama, Tetsuya</creatorcontrib><creatorcontrib>Shibayama, Shiro</creatorcontrib><creatorcontrib>Shibuya, Kazuko</creatorcontrib><creatorcontrib>Shibuya, Akira</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hitomi, Kaori</au><au>Tahara-Hanaoka, Satoko</au><au>Someya, Satoru</au><au>Fujiki, Akira</au><au>Tada, Hideaki</au><au>Sugiyama, Tetsuya</au><au>Shibayama, Shiro</au><au>Shibuya, Kazuko</au><au>Shibuya, Akira</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An immunoglobulin-like receptor, Allergin-1, inhibits immunoglobulin E–mediated immediate hypersensitivity reactions</atitle><jtitle>Nature immunology</jtitle><stitle>Nat Immunol</stitle><addtitle>Nat Immunol</addtitle><date>2010-07-01</date><risdate>2010</risdate><volume>11</volume><issue>7</issue><spage>601</spage><epage>607</epage><pages>601-607</pages><issn>1529-2908</issn><eissn>1529-2916</eissn><abstract>Immunoglobulin E–mediated crosslinking of FɛRI receptors can lead to life-threatening anaphylaxis in sensitized people. Shibuya and colleagues identify a phosphatase-recruiting inhibitory receptor, Allergin-1, that suppresses mast cell degranulation induced by immunoglobulin E–FɛRI.
Anaphylaxis is a life-threatening immediate hypersensitivity reaction triggered by antigen capture by immunoglobulin E (IgE) bound to the high-affinity IgE receptor (FcɛRI) 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 FcɛRI 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.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>20526344</pmid><doi>10.1038/ni.1886</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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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 |
title | An immunoglobulin-like receptor, Allergin-1, inhibits immunoglobulin E–mediated immediate hypersensitivity reactions |
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