Loading…
Siglecs--the major subfamily of I-type lectins
Animal glycan-recognizing proteins can be broadly classified into two groups--lectins (which typically contain an evolutionarily conserved carbohydrate-recognition domain [CRD]) and sulfated glycosaminoglycan (SGAG)-binding proteins (which appear to have evolved by convergent evolution). Proteins ot...
Saved in:
| Published in: | Glycobiology (Oxford) 2006, Vol.16 (1), p.1R-27R |
|---|---|
| Main Authors: | , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c419t-2ecf3d8f377e03bc16815520920b122f9bcc4c0e8ddd5d09f19162e43061cfa73 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c419t-2ecf3d8f377e03bc16815520920b122f9bcc4c0e8ddd5d09f19162e43061cfa73 |
| container_end_page | 27R |
| container_issue | 1 |
| container_start_page | 1R |
| container_title | Glycobiology (Oxford) |
| container_volume | 16 |
| creator | Varki, Ajit Angata, Takashi |
| description | Animal glycan-recognizing proteins can be broadly classified into two groups--lectins (which typically contain an evolutionarily conserved carbohydrate-recognition domain [CRD]) and sulfated glycosaminoglycan (SGAG)-binding proteins (which appear to have evolved by convergent evolution). Proteins other than antibodies and T-cell receptors that mediate glycan recognition via immunoglobulin (Ig)-like domains are called "I-type lectins." The major homologous subfamily of I-type lectins with sialic acid (Sia)-binding properties and characteristic amino-terminal structural features are called the "Siglecs" (Sia-recognizing Ig-superfamily lectins). The Siglecs can be divided into two groups: an evolutionarily conserved subgroup (Siglecs-1, -2, and -4) and a CD33/Siglec-3-related subgroup (Siglecs-3 and -5-13 in primates), which appear to be rapidly evolving. This article provides an overview of historical and current information about the Siglecs. |
| doi_str_mv | 10.1093/glycob/cwj008 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_70198507</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>70198507</sourcerecordid><originalsourceid>FETCH-LOGICAL-c419t-2ecf3d8f377e03bc16815520920b122f9bcc4c0e8ddd5d09f19162e43061cfa73</originalsourceid><addsrcrecordid>eNpd0E1P3DAQBmALFZUt9MgVIg69GWb8lfhYoW5BXdTDFglxsRzHXrIkm62diO6_b1ZZFamnOcyjd0YvIecI1wia36yanevKG_e2BiiOyAyFAsoE4x_IDLTUVClZnJBPKY0AFRbyIzlBBShyoWfkelmvGu8Spf2Lz1q77mKWhjLYtm52WReye9rvtj4bTV9v0hk5DrZJ_vNhnpLH-bdft3d08fP7_e3XBXUCdU-Zd4FXReB57oGXDlWBUjLQDEpkLOjSOeHAF1VVyQp0QI2KecFBoQs256fky5S7jd3vwafetHVyvmnsxndDMjmgLiTs4dV_cN0NcTP-ZhgCR9Rqj-iEXOxSij6YbaxbG3cGwexbNFOLZmpx9BeH0KFsffWuD7W9B9ap93_-7W18NeO5XJq7p2fzPJ8_CL78YRajv5x8sJ2xq1gn87hkgBwQhMil5n8BnYGFyg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>210311967</pqid></control><display><type>article</type><title>Siglecs--the major subfamily of I-type lectins</title><source>Oxford Journals Online</source><creator>Varki, Ajit ; Angata, Takashi</creator><creatorcontrib>Varki, Ajit ; Angata, Takashi</creatorcontrib><description>Animal glycan-recognizing proteins can be broadly classified into two groups--lectins (which typically contain an evolutionarily conserved carbohydrate-recognition domain [CRD]) and sulfated glycosaminoglycan (SGAG)-binding proteins (which appear to have evolved by convergent evolution). Proteins other than antibodies and T-cell receptors that mediate glycan recognition via immunoglobulin (Ig)-like domains are called "I-type lectins." The major homologous subfamily of I-type lectins with sialic acid (Sia)-binding properties and characteristic amino-terminal structural features are called the "Siglecs" (Sia-recognizing Ig-superfamily lectins). The Siglecs can be divided into two groups: an evolutionarily conserved subgroup (Siglecs-1, -2, and -4) and a CD33/Siglec-3-related subgroup (Siglecs-3 and -5-13 in primates), which appear to be rapidly evolving. This article provides an overview of historical and current information about the Siglecs.</description><identifier>ISSN: 0959-6658</identifier><identifier>EISSN: 1460-2423</identifier><identifier>DOI: 10.1093/glycob/cwj008</identifier><identifier>PMID: 16014749</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>5-N-glycolylneuraminic acid ; 5‐N-acetylneuraminic acid ; Animals ; B-cell receptor ; BCR ; Cell Communication - physiology ; central nervous system ; cluster of differentiation antigen ; CNS ; EST ; evolution ; Evolution, Molecular ; expressed sequence tag ; Fuc ; fucose ; Gal ; galactose ; Humans ; IgSF ; immunoglobulin superfamily ; immunoreceptor tyrosine-based inhibitory motif ; ITIM ; lectins ; Lectins - metabolism ; lipopolysaccharide ; LPS ; MAG ; myelin-associated glycoprotein ; natural killer ; Neu5Ac ; Neu5Gc ; P-selection glycoprotein ligand ; peripheral nervous system ; PNS ; Polysaccharides - metabolism ; Protein Binding - physiology ; protein tyrosine phosphatase ; PSGL ; PTP ; Schwann cell myelin protein ; SGAG ; Sia ; sialic acid ; Sialic Acid Binding Immunoglobulin-like Lectins ; sialic acids ; Sialic Acids - metabolism ; sialoadhesin ; Siglecs ; SMP ; sulfated glycosaminoglycan ; type unspecified</subject><ispartof>Glycobiology (Oxford), 2006, Vol.16 (1), p.1R-27R</ispartof><rights>Copyright Oxford University Press(England) Jan 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c419t-2ecf3d8f377e03bc16815520920b122f9bcc4c0e8ddd5d09f19162e43061cfa73</citedby><cites>FETCH-LOGICAL-c419t-2ecf3d8f377e03bc16815520920b122f9bcc4c0e8ddd5d09f19162e43061cfa73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16014749$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Varki, Ajit</creatorcontrib><creatorcontrib>Angata, Takashi</creatorcontrib><title>Siglecs--the major subfamily of I-type lectins</title><title>Glycobiology (Oxford)</title><addtitle>Glycobiology</addtitle><description>Animal glycan-recognizing proteins can be broadly classified into two groups--lectins (which typically contain an evolutionarily conserved carbohydrate-recognition domain [CRD]) and sulfated glycosaminoglycan (SGAG)-binding proteins (which appear to have evolved by convergent evolution). Proteins other than antibodies and T-cell receptors that mediate glycan recognition via immunoglobulin (Ig)-like domains are called "I-type lectins." The major homologous subfamily of I-type lectins with sialic acid (Sia)-binding properties and characteristic amino-terminal structural features are called the "Siglecs" (Sia-recognizing Ig-superfamily lectins). The Siglecs can be divided into two groups: an evolutionarily conserved subgroup (Siglecs-1, -2, and -4) and a CD33/Siglec-3-related subgroup (Siglecs-3 and -5-13 in primates), which appear to be rapidly evolving. This article provides an overview of historical and current information about the Siglecs.</description><subject>5-N-glycolylneuraminic acid</subject><subject>5‐N-acetylneuraminic acid</subject><subject>Animals</subject><subject>B-cell receptor</subject><subject>BCR</subject><subject>Cell Communication - physiology</subject><subject>central nervous system</subject><subject>cluster of differentiation antigen</subject><subject>CNS</subject><subject>EST</subject><subject>evolution</subject><subject>Evolution, Molecular</subject><subject>expressed sequence tag</subject><subject>Fuc</subject><subject>fucose</subject><subject>Gal</subject><subject>galactose</subject><subject>Humans</subject><subject>IgSF</subject><subject>immunoglobulin superfamily</subject><subject>immunoreceptor tyrosine-based inhibitory motif</subject><subject>ITIM</subject><subject>lectins</subject><subject>Lectins - metabolism</subject><subject>lipopolysaccharide</subject><subject>LPS</subject><subject>MAG</subject><subject>myelin-associated glycoprotein</subject><subject>natural killer</subject><subject>Neu5Ac</subject><subject>Neu5Gc</subject><subject>P-selection glycoprotein ligand</subject><subject>peripheral nervous system</subject><subject>PNS</subject><subject>Polysaccharides - metabolism</subject><subject>Protein Binding - physiology</subject><subject>protein tyrosine phosphatase</subject><subject>PSGL</subject><subject>PTP</subject><subject>Schwann cell myelin protein</subject><subject>SGAG</subject><subject>Sia</subject><subject>sialic acid</subject><subject>Sialic Acid Binding Immunoglobulin-like Lectins</subject><subject>sialic acids</subject><subject>Sialic Acids - metabolism</subject><subject>sialoadhesin</subject><subject>Siglecs</subject><subject>SMP</subject><subject>sulfated glycosaminoglycan</subject><subject>type unspecified</subject><issn>0959-6658</issn><issn>1460-2423</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNpd0E1P3DAQBmALFZUt9MgVIg69GWb8lfhYoW5BXdTDFglxsRzHXrIkm62diO6_b1ZZFamnOcyjd0YvIecI1wia36yanevKG_e2BiiOyAyFAsoE4x_IDLTUVClZnJBPKY0AFRbyIzlBBShyoWfkelmvGu8Spf2Lz1q77mKWhjLYtm52WReye9rvtj4bTV9v0hk5DrZJ_vNhnpLH-bdft3d08fP7_e3XBXUCdU-Zd4FXReB57oGXDlWBUjLQDEpkLOjSOeHAF1VVyQp0QI2KecFBoQs256fky5S7jd3vwafetHVyvmnsxndDMjmgLiTs4dV_cN0NcTP-ZhgCR9Rqj-iEXOxSij6YbaxbG3cGwexbNFOLZmpx9BeH0KFsffWuD7W9B9ap93_-7W18NeO5XJq7p2fzPJ8_CL78YRajv5x8sJ2xq1gn87hkgBwQhMil5n8BnYGFyg</recordid><startdate>2006</startdate><enddate>2006</enddate><creator>Varki, Ajit</creator><creator>Angata, Takashi</creator><general>Oxford University Press</general><general>Oxford Publishing Limited (England)</general><scope>FBQ</scope><scope>BSCLL</scope><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>7QL</scope><scope>7QO</scope><scope>7TK</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>2006</creationdate><title>Siglecs--the major subfamily of I-type lectins</title><author>Varki, Ajit ; Angata, Takashi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c419t-2ecf3d8f377e03bc16815520920b122f9bcc4c0e8ddd5d09f19162e43061cfa73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>5-N-glycolylneuraminic acid</topic><topic>5‐N-acetylneuraminic acid</topic><topic>Animals</topic><topic>B-cell receptor</topic><topic>BCR</topic><topic>Cell Communication - physiology</topic><topic>central nervous system</topic><topic>cluster of differentiation antigen</topic><topic>CNS</topic><topic>EST</topic><topic>evolution</topic><topic>Evolution, Molecular</topic><topic>expressed sequence tag</topic><topic>Fuc</topic><topic>fucose</topic><topic>Gal</topic><topic>galactose</topic><topic>Humans</topic><topic>IgSF</topic><topic>immunoglobulin superfamily</topic><topic>immunoreceptor tyrosine-based inhibitory motif</topic><topic>ITIM</topic><topic>lectins</topic><topic>Lectins - metabolism</topic><topic>lipopolysaccharide</topic><topic>LPS</topic><topic>MAG</topic><topic>myelin-associated glycoprotein</topic><topic>natural killer</topic><topic>Neu5Ac</topic><topic>Neu5Gc</topic><topic>P-selection glycoprotein ligand</topic><topic>peripheral nervous system</topic><topic>PNS</topic><topic>Polysaccharides - metabolism</topic><topic>Protein Binding - physiology</topic><topic>protein tyrosine phosphatase</topic><topic>PSGL</topic><topic>PTP</topic><topic>Schwann cell myelin protein</topic><topic>SGAG</topic><topic>Sia</topic><topic>sialic acid</topic><topic>Sialic Acid Binding Immunoglobulin-like Lectins</topic><topic>sialic acids</topic><topic>Sialic Acids - metabolism</topic><topic>sialoadhesin</topic><topic>Siglecs</topic><topic>SMP</topic><topic>sulfated glycosaminoglycan</topic><topic>type unspecified</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Varki, Ajit</creatorcontrib><creatorcontrib>Angata, Takashi</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Glycobiology (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Varki, Ajit</au><au>Angata, Takashi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Siglecs--the major subfamily of I-type lectins</atitle><jtitle>Glycobiology (Oxford)</jtitle><addtitle>Glycobiology</addtitle><date>2006</date><risdate>2006</risdate><volume>16</volume><issue>1</issue><spage>1R</spage><epage>27R</epage><pages>1R-27R</pages><issn>0959-6658</issn><eissn>1460-2423</eissn><abstract>Animal glycan-recognizing proteins can be broadly classified into two groups--lectins (which typically contain an evolutionarily conserved carbohydrate-recognition domain [CRD]) and sulfated glycosaminoglycan (SGAG)-binding proteins (which appear to have evolved by convergent evolution). Proteins other than antibodies and T-cell receptors that mediate glycan recognition via immunoglobulin (Ig)-like domains are called "I-type lectins." The major homologous subfamily of I-type lectins with sialic acid (Sia)-binding properties and characteristic amino-terminal structural features are called the "Siglecs" (Sia-recognizing Ig-superfamily lectins). The Siglecs can be divided into two groups: an evolutionarily conserved subgroup (Siglecs-1, -2, and -4) and a CD33/Siglec-3-related subgroup (Siglecs-3 and -5-13 in primates), which appear to be rapidly evolving. This article provides an overview of historical and current information about the Siglecs.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>16014749</pmid><doi>10.1093/glycob/cwj008</doi><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0959-6658 |
| ispartof | Glycobiology (Oxford), 2006, Vol.16 (1), p.1R-27R |
| issn | 0959-6658 1460-2423 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70198507 |
| source | Oxford Journals Online |
| subjects | 5-N-glycolylneuraminic acid 5‐N-acetylneuraminic acid Animals B-cell receptor BCR Cell Communication - physiology central nervous system cluster of differentiation antigen CNS EST evolution Evolution, Molecular expressed sequence tag Fuc fucose Gal galactose Humans IgSF immunoglobulin superfamily immunoreceptor tyrosine-based inhibitory motif ITIM lectins Lectins - metabolism lipopolysaccharide LPS MAG myelin-associated glycoprotein natural killer Neu5Ac Neu5Gc P-selection glycoprotein ligand peripheral nervous system PNS Polysaccharides - metabolism Protein Binding - physiology protein tyrosine phosphatase PSGL PTP Schwann cell myelin protein SGAG Sia sialic acid Sialic Acid Binding Immunoglobulin-like Lectins sialic acids Sialic Acids - metabolism sialoadhesin Siglecs SMP sulfated glycosaminoglycan type unspecified |
| title | Siglecs--the major subfamily of I-type lectins |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T15%3A48%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Siglecs--the%20major%20subfamily%20of%20I-type%20lectins&rft.jtitle=Glycobiology%20(Oxford)&rft.au=Varki,%20Ajit&rft.date=2006&rft.volume=16&rft.issue=1&rft.spage=1R&rft.epage=27R&rft.pages=1R-27R&rft.issn=0959-6658&rft.eissn=1460-2423&rft_id=info:doi/10.1093/glycob/cwj008&rft_dat=%3Cproquest_cross%3E70198507%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c419t-2ecf3d8f377e03bc16815520920b122f9bcc4c0e8ddd5d09f19162e43061cfa73%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=210311967&rft_id=info:pmid/16014749&rfr_iscdi=true |