Carbohydrate Recognition by a Natural Killer Cell Receptor, Ly-49C
Ly-49 represents a family of type II transmembrane proteins containing C-type lectin domains. At least two members of the Ly-49 family, namely Ly-49A and Ly-49C, are expressed by distinct subsets of natural killer cells and bind to class I major histocompatibility complex antigens on the surface of...
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| Veröffentlicht in: | The Journal of biological chemistry 1995-04, Vol.270 (17), p.9691-9694 |
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| container_title | The Journal of biological chemistry |
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| creator | Brennan, J Takei, F Wong, S Mager, D L |
| description | Ly-49 represents a family of type II transmembrane proteins containing C-type lectin domains. At least two members of the
Ly-49 family, namely Ly-49A and Ly-49C, are expressed by distinct subsets of natural killer cells and bind to class I major
histocompatibility complex antigens on the surface of target cells. In this report we have established that Ly-49C mediates
carbohydrate recognition. The sulfated glycans fucoidan, -carrageenan, and dextran sulfate were found to be potent inhibitors of Ly-49C-mediated cell adhesion, whereas other polysaccharides
of similar size, charge, or sulfate content were noninhibitory. All of the polysaccharides which inhibited Ly-49C adhesion
also blocked the binding of the antibody 5E6 to Ly-49C-expressing COS cells, confirming the direct protein-carbohydrate interaction.
The enzymatic removal of specific carbohydrates from the target cell surface has shown that Ly-49C-mediated adhesion is not
sialic acid-dependent, but is significantly decreased following fucosidase treatment. These results suggest an important role
for carbohydrate recognition by natural killer cell receptors. |
| doi_str_mv | 10.1074/jbc.270.17.9691 |
| format | Article |
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Ly-49 family, namely Ly-49A and Ly-49C, are expressed by distinct subsets of natural killer cells and bind to class I major
histocompatibility complex antigens on the surface of target cells. In this report we have established that Ly-49C mediates
carbohydrate recognition. The sulfated glycans fucoidan, -carrageenan, and dextran sulfate were found to be potent inhibitors of Ly-49C-mediated cell adhesion, whereas other polysaccharides
of similar size, charge, or sulfate content were noninhibitory. All of the polysaccharides which inhibited Ly-49C adhesion
also blocked the binding of the antibody 5E6 to Ly-49C-expressing COS cells, confirming the direct protein-carbohydrate interaction.
The enzymatic removal of specific carbohydrates from the target cell surface has shown that Ly-49C-mediated adhesion is not
sialic acid-dependent, but is significantly decreased following fucosidase treatment. These results suggest an important role
for carbohydrate recognition by natural killer cell receptors.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.270.17.9691</identifier><identifier>PMID: 7730344</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Antigens, Ly ; Binding, Competitive ; Carbohydrate Metabolism ; Cell Adhesion ; Cell Line ; Glycoside Hydrolases - metabolism ; Killer Cells, Natural - metabolism ; Lectins, C-Type ; Membrane Glycoproteins - metabolism ; Receptors, Immunologic - metabolism ; Receptors, NK Cell Lectin-Like ; Recombinant Proteins - metabolism ; Sulfates - metabolism</subject><ispartof>The Journal of biological chemistry, 1995-04, Vol.270 (17), p.9691-9694</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c351t-11f7220b12f69774610ce01b99ee733f14057345ebc855ce345e7f18c7d8e9543</citedby><cites>FETCH-LOGICAL-c351t-11f7220b12f69774610ce01b99ee733f14057345ebc855ce345e7f18c7d8e9543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7730344$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brennan, J</creatorcontrib><creatorcontrib>Takei, F</creatorcontrib><creatorcontrib>Wong, S</creatorcontrib><creatorcontrib>Mager, D L</creatorcontrib><title>Carbohydrate Recognition by a Natural Killer Cell Receptor, Ly-49C</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Ly-49 represents a family of type II transmembrane proteins containing C-type lectin domains. At least two members of the
Ly-49 family, namely Ly-49A and Ly-49C, are expressed by distinct subsets of natural killer cells and bind to class I major
histocompatibility complex antigens on the surface of target cells. In this report we have established that Ly-49C mediates
carbohydrate recognition. The sulfated glycans fucoidan, -carrageenan, and dextran sulfate were found to be potent inhibitors of Ly-49C-mediated cell adhesion, whereas other polysaccharides
of similar size, charge, or sulfate content were noninhibitory. All of the polysaccharides which inhibited Ly-49C adhesion
also blocked the binding of the antibody 5E6 to Ly-49C-expressing COS cells, confirming the direct protein-carbohydrate interaction.
The enzymatic removal of specific carbohydrates from the target cell surface has shown that Ly-49C-mediated adhesion is not
sialic acid-dependent, but is significantly decreased following fucosidase treatment. These results suggest an important role
for carbohydrate recognition by natural killer cell receptors.</description><subject>Animals</subject><subject>Antigens, Ly</subject><subject>Binding, Competitive</subject><subject>Carbohydrate Metabolism</subject><subject>Cell Adhesion</subject><subject>Cell Line</subject><subject>Glycoside Hydrolases - metabolism</subject><subject>Killer Cells, Natural - metabolism</subject><subject>Lectins, C-Type</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Receptors, Immunologic - metabolism</subject><subject>Receptors, NK Cell Lectin-Like</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sulfates - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkN9LwzAQx4Moc06ffRIKgk92yzXp0jxq8RcOBVHwLaTZdc1o15m2SP97UzYEn7yXXLjPfTk-hJwDnQIVfLbOzDQS_iOmci7hgIyBJixkMXwekjGlEYQyipNjctI0a-qLSxiRkRCMMs7H5DbVLquLful0i8Ebmnq1sa2tN0HWBzp40W3ndBk827JEF6RYlgOE27Z218GiD7lMT8lRrssGz_bvhHzc372nj-Hi9eEpvVmExl_ThgC5iCKaQZTPpRB8DtQghUxKRMFYDpzGgvEYM5PEscGhFTkkRiwTlDFnE3K1y926-qvDplWVbYy_SG-w7holRMRkErF_QRBeA0jpwdkONK5uGoe52jpbadcroGrQq7xe5fX6FTXo9RsX--guq3D5y-99-vnlbl7YVfFtHarM1qbA6k_KD9sNfrE</recordid><startdate>19950428</startdate><enddate>19950428</enddate><creator>Brennan, J</creator><creator>Takei, F</creator><creator>Wong, S</creator><creator>Mager, D L</creator><general>American Society for Biochemistry and Molecular 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><scope>7X8</scope></search><sort><creationdate>19950428</creationdate><title>Carbohydrate Recognition by a Natural Killer Cell Receptor, Ly-49C</title><author>Brennan, J ; Takei, F ; Wong, S ; Mager, D L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c351t-11f7220b12f69774610ce01b99ee733f14057345ebc855ce345e7f18c7d8e9543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Animals</topic><topic>Antigens, Ly</topic><topic>Binding, Competitive</topic><topic>Carbohydrate Metabolism</topic><topic>Cell Adhesion</topic><topic>Cell Line</topic><topic>Glycoside Hydrolases - metabolism</topic><topic>Killer Cells, Natural - metabolism</topic><topic>Lectins, C-Type</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Receptors, Immunologic - metabolism</topic><topic>Receptors, NK Cell Lectin-Like</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sulfates - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brennan, J</creatorcontrib><creatorcontrib>Takei, F</creatorcontrib><creatorcontrib>Wong, S</creatorcontrib><creatorcontrib>Mager, D L</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><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brennan, J</au><au>Takei, F</au><au>Wong, S</au><au>Mager, D L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Carbohydrate Recognition by a Natural Killer Cell Receptor, Ly-49C</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1995-04-28</date><risdate>1995</risdate><volume>270</volume><issue>17</issue><spage>9691</spage><epage>9694</epage><pages>9691-9694</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Ly-49 represents a family of type II transmembrane proteins containing C-type lectin domains. At least two members of the
Ly-49 family, namely Ly-49A and Ly-49C, are expressed by distinct subsets of natural killer cells and bind to class I major
histocompatibility complex antigens on the surface of target cells. In this report we have established that Ly-49C mediates
carbohydrate recognition. The sulfated glycans fucoidan, -carrageenan, and dextran sulfate were found to be potent inhibitors of Ly-49C-mediated cell adhesion, whereas other polysaccharides
of similar size, charge, or sulfate content were noninhibitory. All of the polysaccharides which inhibited Ly-49C adhesion
also blocked the binding of the antibody 5E6 to Ly-49C-expressing COS cells, confirming the direct protein-carbohydrate interaction.
The enzymatic removal of specific carbohydrates from the target cell surface has shown that Ly-49C-mediated adhesion is not
sialic acid-dependent, but is significantly decreased following fucosidase treatment. These results suggest an important role
for carbohydrate recognition by natural killer cell receptors.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7730344</pmid><doi>10.1074/jbc.270.17.9691</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1995-04, Vol.270 (17), p.9691-9694 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Animals Antigens, Ly Binding, Competitive Carbohydrate Metabolism Cell Adhesion Cell Line Glycoside Hydrolases - metabolism Killer Cells, Natural - metabolism Lectins, C-Type Membrane Glycoproteins - metabolism Receptors, Immunologic - metabolism Receptors, NK Cell Lectin-Like Recombinant Proteins - metabolism Sulfates - metabolism |
| title | Carbohydrate Recognition by a Natural Killer Cell Receptor, Ly-49C |
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