Sialic acid binding receptors (siglecs) expressed by macrophages
Sialic acids are structurally and topographically well‐suited to function as ligands in cellular recognition events. Sialoadhesin (Sn) is a sialic acid binding receptor uniquely expressed by macrophage subsets. It is a member of the immunoglobulin (Ig) superfamily with 17 extracellular domains. Sn i...
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Veröffentlicht in: | Journal of leukocyte biology 1999-11, Vol.66 (5), p.705-711 |
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description | Sialic acids are structurally and topographically well‐suited to function as ligands in cellular recognition events. Sialoadhesin (Sn) is a sialic acid binding receptor uniquely expressed by macrophage subsets. It is a member of the immunoglobulin (Ig) superfamily with 17 extracellular domains. Sn is a prototypical member of the siglec family of sialic acid binding proteins, which includes CD22, myelin‐associated glycoprotein, CD33, and siglec‐5. These membrane proteins are involved in discrete functions in the hemopoietic, immune, and nervous systems. The sialic acid binding region of siglecs is localized within the membrane‐distal, amino‐terminal domain and in the case of Sn, it has been characterized in atomic detail by X‐ray crystallography, nuclear magnetic resonance, and site‐directed mutagenesis. Our studies on Sn indicate that this receptor is likely to function as a macrophage accessory molecule in a variety of cell‐cell and cell‐extracellular matrix interactions. CD33 and siglec‐5 are also expressed on macrophage subsets as well as other myeloid cells. However, unlike Sn, the properties of these molecules indicate a predominant role in signaling functions rather than in cell‐cell interactions. J. Leukoc. Biol. 66: 705–711; 1999. |
doi_str_mv | 10.1002/jlb.66.5.705 |
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Sialoadhesin (Sn) is a sialic acid binding receptor uniquely expressed by macrophage subsets. It is a member of the immunoglobulin (Ig) superfamily with 17 extracellular domains. Sn is a prototypical member of the siglec family of sialic acid binding proteins, which includes CD22, myelin‐associated glycoprotein, CD33, and siglec‐5. These membrane proteins are involved in discrete functions in the hemopoietic, immune, and nervous systems. The sialic acid binding region of siglecs is localized within the membrane‐distal, amino‐terminal domain and in the case of Sn, it has been characterized in atomic detail by X‐ray crystallography, nuclear magnetic resonance, and site‐directed mutagenesis. Our studies on Sn indicate that this receptor is likely to function as a macrophage accessory molecule in a variety of cell‐cell and cell‐extracellular matrix interactions. CD33 and siglec‐5 are also expressed on macrophage subsets as well as other myeloid cells. However, unlike Sn, the properties of these molecules indicate a predominant role in signaling functions rather than in cell‐cell interactions. J. Leukoc. Biol. 66: 705–711; 1999.</description><identifier>ISSN: 0741-5400</identifier><identifier>EISSN: 1938-3673</identifier><identifier>DOI: 10.1002/jlb.66.5.705</identifier><identifier>PMID: 10577497</identifier><language>eng</language><publisher>United States: Society for Leukocyte Biology</publisher><subject>Amino Acid Sequence ; Animals ; Antigens, CD - metabolism ; Antigens, Differentiation, Myelomonocytic - metabolism ; Carbohydrate Metabolism ; CD22 ; CD22 antigen ; CD33 ; CD33 antigen ; Cell Adhesion ; Cell Adhesion Molecules - metabolism ; Humans ; Lectins ; ligands ; Macrophages - metabolism ; Membrane Glycoproteins - metabolism ; Molecular Sequence Data ; myelin‐associated glycoprotein ; N-Acetylneuraminic Acid - metabolism ; Receptors, Cell Surface - metabolism ; Receptors, Immunologic - metabolism ; Sialic Acid Binding Ig-like Lectin 1 ; sialic acid receptors ; sialoadhesin</subject><ispartof>Journal of leukocyte biology, 1999-11, Vol.66 (5), p.705-711</ispartof><rights>1999 Society for Leukocyte Biology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4945-bcab1f99d5b2563d350ea3845aa58024bad7c479f6ccdcd5290ae8fb96067f473</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjlb.66.5.705$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjlb.66.5.705$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10577497$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Munday, James</creatorcontrib><creatorcontrib>Floyd, Helen</creatorcontrib><creatorcontrib>Crocker, Paul R.</creatorcontrib><title>Sialic acid binding receptors (siglecs) expressed by macrophages</title><title>Journal of leukocyte biology</title><addtitle>J Leukoc Biol</addtitle><description>Sialic acids are structurally and topographically well‐suited to function as ligands in cellular recognition events. Sialoadhesin (Sn) is a sialic acid binding receptor uniquely expressed by macrophage subsets. It is a member of the immunoglobulin (Ig) superfamily with 17 extracellular domains. Sn is a prototypical member of the siglec family of sialic acid binding proteins, which includes CD22, myelin‐associated glycoprotein, CD33, and siglec‐5. These membrane proteins are involved in discrete functions in the hemopoietic, immune, and nervous systems. The sialic acid binding region of siglecs is localized within the membrane‐distal, amino‐terminal domain and in the case of Sn, it has been characterized in atomic detail by X‐ray crystallography, nuclear magnetic resonance, and site‐directed mutagenesis. Our studies on Sn indicate that this receptor is likely to function as a macrophage accessory molecule in a variety of cell‐cell and cell‐extracellular matrix interactions. CD33 and siglec‐5 are also expressed on macrophage subsets as well as other myeloid cells. However, unlike Sn, the properties of these molecules indicate a predominant role in signaling functions rather than in cell‐cell interactions. J. Leukoc. Biol. 66: 705–711; 1999.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antigens, CD - metabolism</subject><subject>Antigens, Differentiation, Myelomonocytic - metabolism</subject><subject>Carbohydrate Metabolism</subject><subject>CD22</subject><subject>CD22 antigen</subject><subject>CD33</subject><subject>CD33 antigen</subject><subject>Cell Adhesion</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Humans</subject><subject>Lectins</subject><subject>ligands</subject><subject>Macrophages - metabolism</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>myelin‐associated glycoprotein</subject><subject>N-Acetylneuraminic Acid - metabolism</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Immunologic - metabolism</subject><subject>Sialic Acid Binding Ig-like Lectin 1</subject><subject>sialic acid receptors</subject><subject>sialoadhesin</subject><issn>0741-5400</issn><issn>1938-3673</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kD1PwzAQhi0EoqWwMaMsIJBIOSf-qDc-xKcqMQCz5TiX1shpg00V-u8JSoWYmG557nnvXkIOKYwpQHbx7ouxEGM-lsC3yJCqfJLmQubbZAiS0ZQzgAHZi_EdAPJMwC4ZUOBSMiWH5PLFGe9sYqwrk8ItSreYJQEtNp_LEJPT6GYebTxL8KsJGCN21DqpjQ3LZm5mGPfJTmV8xIPNHJG3u9vXm4d0-nz_eHM1TS1TjKeFNQWtlCp5kXGRlzkHNPmEcWP4BDJWmFJaJlUlrC1tyTMFBidVoQQIWTGZj8hJ723C8mOF8VPXLlr03ixwuYqaSgaKdx-OyHkPdifGGLDSTXC1CWtNQf80prvGtBCa666xDj_aeFdFjeUfuK-oA2gPtM7j-l-ZfppeQy897nfmbjZvXUAda-N9F5Hptm1_w78Bpv2DJQ</recordid><startdate>199911</startdate><enddate>199911</enddate><creator>Munday, James</creator><creator>Floyd, Helen</creator><creator>Crocker, Paul R.</creator><general>Society for Leukocyte Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>H94</scope></search><sort><creationdate>199911</creationdate><title>Sialic acid binding receptors (siglecs) expressed by macrophages</title><author>Munday, James ; Floyd, Helen ; Crocker, Paul R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4945-bcab1f99d5b2563d350ea3845aa58024bad7c479f6ccdcd5290ae8fb96067f473</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antigens, CD - metabolism</topic><topic>Antigens, Differentiation, Myelomonocytic - metabolism</topic><topic>Carbohydrate Metabolism</topic><topic>CD22</topic><topic>CD22 antigen</topic><topic>CD33</topic><topic>CD33 antigen</topic><topic>Cell Adhesion</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Humans</topic><topic>Lectins</topic><topic>ligands</topic><topic>Macrophages - metabolism</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>myelin‐associated glycoprotein</topic><topic>N-Acetylneuraminic Acid - metabolism</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Immunologic - metabolism</topic><topic>Sialic Acid Binding Ig-like Lectin 1</topic><topic>sialic acid receptors</topic><topic>sialoadhesin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Munday, James</creatorcontrib><creatorcontrib>Floyd, Helen</creatorcontrib><creatorcontrib>Crocker, Paul R.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>Journal of leukocyte biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Munday, James</au><au>Floyd, Helen</au><au>Crocker, Paul R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sialic acid binding receptors (siglecs) expressed by macrophages</atitle><jtitle>Journal of leukocyte biology</jtitle><addtitle>J Leukoc Biol</addtitle><date>1999-11</date><risdate>1999</risdate><volume>66</volume><issue>5</issue><spage>705</spage><epage>711</epage><pages>705-711</pages><issn>0741-5400</issn><eissn>1938-3673</eissn><abstract>Sialic acids are structurally and topographically well‐suited to function as ligands in cellular recognition events. Sialoadhesin (Sn) is a sialic acid binding receptor uniquely expressed by macrophage subsets. It is a member of the immunoglobulin (Ig) superfamily with 17 extracellular domains. Sn is a prototypical member of the siglec family of sialic acid binding proteins, which includes CD22, myelin‐associated glycoprotein, CD33, and siglec‐5. These membrane proteins are involved in discrete functions in the hemopoietic, immune, and nervous systems. The sialic acid binding region of siglecs is localized within the membrane‐distal, amino‐terminal domain and in the case of Sn, it has been characterized in atomic detail by X‐ray crystallography, nuclear magnetic resonance, and site‐directed mutagenesis. Our studies on Sn indicate that this receptor is likely to function as a macrophage accessory molecule in a variety of cell‐cell and cell‐extracellular matrix interactions. CD33 and siglec‐5 are also expressed on macrophage subsets as well as other myeloid cells. However, unlike Sn, the properties of these molecules indicate a predominant role in signaling functions rather than in cell‐cell interactions. J. Leukoc. Biol. 66: 705–711; 1999.</abstract><cop>United States</cop><pub>Society for Leukocyte Biology</pub><pmid>10577497</pmid><doi>10.1002/jlb.66.5.705</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
subjects | Amino Acid Sequence Animals Antigens, CD - metabolism Antigens, Differentiation, Myelomonocytic - metabolism Carbohydrate Metabolism CD22 CD22 antigen CD33 CD33 antigen Cell Adhesion Cell Adhesion Molecules - metabolism Humans Lectins ligands Macrophages - metabolism Membrane Glycoproteins - metabolism Molecular Sequence Data myelin‐associated glycoprotein N-Acetylneuraminic Acid - metabolism Receptors, Cell Surface - metabolism Receptors, Immunologic - metabolism Sialic Acid Binding Ig-like Lectin 1 sialic acid receptors sialoadhesin |
title | Sialic acid binding receptors (siglecs) expressed by macrophages |
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