Purification and properties of sialoadhesin, a sialic acid‐binding receptor of murine tissue macrophages
Macrophage subpopulations in the mouse express a lectin‐like receptor, sialoadhesin (originally named sheep erythrocyte receptor, SER), which selectively recognizes sialoglycoconjugates and is likely to be involved in cellular interactions of stromal macrophages in haematopoietic and lymphoid tissue...
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creator | Crocker, P.R. Kelm, S. Dubois, C. Martin, B. McWilliam, A.S. Shotton, D.M. Paulson, J.C. Gordon, S. |
description | Macrophage subpopulations in the mouse express a lectin‐like receptor, sialoadhesin (originally named sheep erythrocyte receptor, SER), which selectively recognizes sialoglycoconjugates and is likely to be involved in cellular interactions of stromal macrophages in haematopoietic and lymphoid tissues. In this report we describe the purification and ligand specificity of sialoadhesin isolated from mouse spleen. Purified sialoadhesin, a glycoprotein of 185 kd apparent Mr, agglutinated sheep or human erythrocytes at nanomolar concentrations in a sialic acid‐dependent manner. Low angle shadowing and electron microscopy showed that sialoadhesin consisted of a globular head region of approximately 9 nm and an extended tail of approximately 35 nm. To investigate the specificity for sialic acid, we studied the interaction of sialoadhesin with derivatized human erythrocytes, glycoproteins, and glycolipids. In conclusion, sialoadhesin specifically recognizes the oligosaccharide sequence Neu5Ac alpha 2‐‐‐‐3Gal beta 1‐‐‐‐3GalNAc in either sialoglycoproteins or gangliosides. These findings imply that specific sialoglycoconjugates carrying this structure may be involved in cellular interactions between stromal macrophages and subpopulations of haematopoietic cells and lymphocytes. |
doi_str_mv | 10.1002/j.1460-2075.1991.tb07689.x |
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In this report we describe the purification and ligand specificity of sialoadhesin isolated from mouse spleen. Purified sialoadhesin, a glycoprotein of 185 kd apparent Mr, agglutinated sheep or human erythrocytes at nanomolar concentrations in a sialic acid‐dependent manner. Low angle shadowing and electron microscopy showed that sialoadhesin consisted of a globular head region of approximately 9 nm and an extended tail of approximately 35 nm. To investigate the specificity for sialic acid, we studied the interaction of sialoadhesin with derivatized human erythrocytes, glycoproteins, and glycolipids. In conclusion, sialoadhesin specifically recognizes the oligosaccharide sequence Neu5Ac alpha 2‐‐‐‐3Gal beta 1‐‐‐‐3GalNAc in either sialoglycoproteins or gangliosides. These findings imply that specific sialoglycoconjugates carrying this structure may be involved in cellular interactions between stromal macrophages and subpopulations of haematopoietic cells and lymphocytes.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1002/j.1460-2075.1991.tb07689.x</identifier><identifier>PMID: 2050106</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>London: Nature Publishing Group</publisher><subject>Animals ; Biological and medical sciences ; Carbohydrate Sequence ; Chromatography, Thin Layer ; Erythrocyte Aggregation ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Immunobiology ; macrophages ; Macrophages - immunology ; Macrophages - metabolism ; Membrane Glycoproteins - metabolism ; Mice ; Molecular Sequence Data ; Monocytes, macrophages ; Myeloid cells: ontogeny, maturation, markers, receptors ; Oligosaccharides - metabolism ; Receptors, Immunologic - isolation & purification ; sialic acid ; Sialic Acid Binding Ig-like Lectin 1 ; Sialic Acids - metabolism ; Spleen</subject><ispartof>The EMBO journal, 1991-07, Vol.10 (7), p.1661-1669</ispartof><rights>1991 European Molecular Biology Organization</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6059-193bb95181a681825f737f16ed2c5d27308513e631cfca436ab11803182f74763</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC452836/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC452836/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,725,778,782,883,27913,27914,53780,53782</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19672752$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2050106$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Crocker, P.R.</creatorcontrib><creatorcontrib>Kelm, S.</creatorcontrib><creatorcontrib>Dubois, C.</creatorcontrib><creatorcontrib>Martin, B.</creatorcontrib><creatorcontrib>McWilliam, A.S.</creatorcontrib><creatorcontrib>Shotton, D.M.</creatorcontrib><creatorcontrib>Paulson, J.C.</creatorcontrib><creatorcontrib>Gordon, S.</creatorcontrib><title>Purification and properties of sialoadhesin, a sialic acid‐binding receptor of murine tissue macrophages</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>Macrophage subpopulations in the mouse express a lectin‐like receptor, sialoadhesin (originally named sheep erythrocyte receptor, SER), which selectively recognizes sialoglycoconjugates and is likely to be involved in cellular interactions of stromal macrophages in haematopoietic and lymphoid tissues. In this report we describe the purification and ligand specificity of sialoadhesin isolated from mouse spleen. Purified sialoadhesin, a glycoprotein of 185 kd apparent Mr, agglutinated sheep or human erythrocytes at nanomolar concentrations in a sialic acid‐dependent manner. Low angle shadowing and electron microscopy showed that sialoadhesin consisted of a globular head region of approximately 9 nm and an extended tail of approximately 35 nm. To investigate the specificity for sialic acid, we studied the interaction of sialoadhesin with derivatized human erythrocytes, glycoproteins, and glycolipids. In conclusion, sialoadhesin specifically recognizes the oligosaccharide sequence Neu5Ac alpha 2‐‐‐‐3Gal beta 1‐‐‐‐3GalNAc in either sialoglycoproteins or gangliosides. These findings imply that specific sialoglycoconjugates carrying this structure may be involved in cellular interactions between stromal macrophages and subpopulations of haematopoietic cells and lymphocytes.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Carbohydrate Sequence</subject><subject>Chromatography, Thin Layer</subject><subject>Erythrocyte Aggregation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Immunobiology</subject><subject>macrophages</subject><subject>Macrophages - immunology</subject><subject>Macrophages - metabolism</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Monocytes, macrophages</subject><subject>Myeloid cells: ontogeny, maturation, markers, receptors</subject><subject>Oligosaccharides - metabolism</subject><subject>Receptors, Immunologic - isolation & purification</subject><subject>sialic acid</subject><subject>Sialic Acid Binding Ig-like Lectin 1</subject><subject>Sialic Acids - metabolism</subject><subject>Spleen</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkc1u1DAUhS0EKkPhEZAiJFiRcK8dOw4Si1K1_KgIFrC2HMeZ8ShxBjuBdscj8Ix9EpKZaIAVYmVb5zvH1z6EPEHIEIC-2GaYC0gpFDzDssRsqKAQssyu75DVUbpLVkAFpjnK8j55EOMWALgs8IScUOCAIFZk-2kMrnFGD673ifZ1sgv9zobB2Zj0TRKdbntdb2x0_nmi92dnEm1cffvjZ-V87fw6CdbY3dCH2dFNgd4mg4txtEmnzZS30WsbH5J7jW6jfbSsp-TL5cXn87fp1cc3787PrlIjgJcplqyqSo4StZAoKW8KVjQobE0Nr2nBQHJkVjA0jdE5E7pClMAmtCnyQrBT8uqQuxurztbG-iHoVu2C63S4Ub126m_Fu41a999Uzqlks__Z4g_919HGQXUuGtu22tt-jEqCwD36LxB5KXKgMIEvD-D0FzEG2xyHQVBzo2qr5trUXJuaG1VLo-p6Mj_-8zlH61LhpD9ddB2NbpugvXHx9w2lKGjB6cSdHbjvrrU3_zGBuvjw-v1-z34B6azA3Q</recordid><startdate>199107</startdate><enddate>199107</enddate><creator>Crocker, P.R.</creator><creator>Kelm, S.</creator><creator>Dubois, C.</creator><creator>Martin, B.</creator><creator>McWilliam, A.S.</creator><creator>Shotton, D.M.</creator><creator>Paulson, J.C.</creator><creator>Gordon, S.</creator><general>Nature Publishing Group</general><scope>IQODW</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>199107</creationdate><title>Purification and properties of sialoadhesin, a sialic acid‐binding receptor of murine tissue macrophages</title><author>Crocker, P.R. ; Kelm, S. ; Dubois, C. ; Martin, B. ; McWilliam, A.S. ; Shotton, D.M. ; Paulson, J.C. ; Gordon, S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6059-193bb95181a681825f737f16ed2c5d27308513e631cfca436ab11803182f74763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Carbohydrate Sequence</topic><topic>Chromatography, Thin Layer</topic><topic>Erythrocyte Aggregation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Immunobiology</topic><topic>macrophages</topic><topic>Macrophages - immunology</topic><topic>Macrophages - metabolism</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Monocytes, macrophages</topic><topic>Myeloid cells: ontogeny, maturation, markers, receptors</topic><topic>Oligosaccharides - metabolism</topic><topic>Receptors, Immunologic - isolation & purification</topic><topic>sialic acid</topic><topic>Sialic Acid Binding Ig-like Lectin 1</topic><topic>Sialic Acids - metabolism</topic><topic>Spleen</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Crocker, P.R.</creatorcontrib><creatorcontrib>Kelm, S.</creatorcontrib><creatorcontrib>Dubois, C.</creatorcontrib><creatorcontrib>Martin, B.</creatorcontrib><creatorcontrib>McWilliam, A.S.</creatorcontrib><creatorcontrib>Shotton, D.M.</creatorcontrib><creatorcontrib>Paulson, J.C.</creatorcontrib><creatorcontrib>Gordon, S.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Crocker, P.R.</au><au>Kelm, S.</au><au>Dubois, C.</au><au>Martin, B.</au><au>McWilliam, A.S.</au><au>Shotton, D.M.</au><au>Paulson, J.C.</au><au>Gordon, S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and properties of sialoadhesin, a sialic acid‐binding receptor of murine tissue macrophages</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1991-07</date><risdate>1991</risdate><volume>10</volume><issue>7</issue><spage>1661</spage><epage>1669</epage><pages>1661-1669</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Macrophage subpopulations in the mouse express a lectin‐like receptor, sialoadhesin (originally named sheep erythrocyte receptor, SER), which selectively recognizes sialoglycoconjugates and is likely to be involved in cellular interactions of stromal macrophages in haematopoietic and lymphoid tissues. 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subjects | Animals Biological and medical sciences Carbohydrate Sequence Chromatography, Thin Layer Erythrocyte Aggregation Fundamental and applied biological sciences. Psychology Fundamental immunology Immunobiology macrophages Macrophages - immunology Macrophages - metabolism Membrane Glycoproteins - metabolism Mice Molecular Sequence Data Monocytes, macrophages Myeloid cells: ontogeny, maturation, markers, receptors Oligosaccharides - metabolism Receptors, Immunologic - isolation & purification sialic acid Sialic Acid Binding Ig-like Lectin 1 Sialic Acids - metabolism Spleen |
title | Purification and properties of sialoadhesin, a sialic acid‐binding receptor of murine tissue macrophages |
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