Cloning of a lymphocyte homing receptor reveals a lectin domain
Lymphocytes express cell surface molecules, termed homing receptors, that mediate their selective attachment to specialized high endothelial venules found within secondary lymphoid organs. Previous work has demonstrated that the adhesive interaction between lymphocytes and the endothelium of periphe...
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| Veröffentlicht in: | Cell 1989-03, Vol.56 (6), p.1045-1055 |
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| container_title | Cell |
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| creator | Lasky, Laurence A. Singer, Mark S. Yednock, Ted A. Dowbenko, Donald Fennie, Christopher Rodriguez, Henry Nguyen, Thu Stachel, Scott Rosen, Steven D. |
| description | Lymphocytes express cell surface molecules, termed homing receptors, that mediate their selective attachment to specialized high endothelial venules found within secondary lymphoid organs. Previous work has demonstrated that the adhesive interaction between lymphocytes and the endothelium of peripheral lymph nodes appears to involve a lectin-like activity. Moreover, MEL-14, a monoclonal antibody that blocks lymphocyte-peripheral lymph node binding and presumably recognizes the homing receptor mediating this adhesive interaction, appeared to detect the lectin-like receptor. In this paper we describe the cloning of a murine cDNA that encodes the antigen recognized by the MEL-14 antibody. Characterization of the cDNA encoding the putative mouse peripheral lymph node-specific homing receptor shows that it contains a lectin domain that appears to be involved in the binding of lymphocytes to peripheral lymph node endothelium, thus defining a new type of cellular adhesion molecule. This result supports a novel mechanism for the distribution of lymphocyte populations to various lymphoid organs. |
| doi_str_mv | 10.1016/0092-8674(89)90637-5 |
| format | Article |
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Previous work has demonstrated that the adhesive interaction between lymphocytes and the endothelium of peripheral lymph nodes appears to involve a lectin-like activity. Moreover, MEL-14, a monoclonal antibody that blocks lymphocyte-peripheral lymph node binding and presumably recognizes the homing receptor mediating this adhesive interaction, appeared to detect the lectin-like receptor. In this paper we describe the cloning of a murine cDNA that encodes the antigen recognized by the MEL-14 antibody. Characterization of the cDNA encoding the putative mouse peripheral lymph node-specific homing receptor shows that it contains a lectin domain that appears to be involved in the binding of lymphocytes to peripheral lymph node endothelium, thus defining a new type of cellular adhesion molecule. This result supports a novel mechanism for the distribution of lymphocyte populations to various lymphoid organs.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/0092-8674(89)90637-5</identifier><identifier>PMID: 2647302</identifier><identifier>CODEN: CELLB5</identifier><language>eng</language><publisher>Cambridge, MA: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Antigens, Surface - analysis ; Antigens, Surface - genetics ; Base Sequence ; Biological and medical sciences ; Calcium - pharmacology ; Carbohydrate Metabolism ; Cell Adhesion ; Cell Adhesion Molecules ; Cell receptors ; Cell structures and functions ; Cloning, Molecular ; DNA - analysis ; DNA - isolation & purification ; Female ; Fundamental and applied biological sciences. Psychology ; Lectins - analysis ; Lectins - genetics ; lymphocytes ; Lymphocytes - cytology ; MEL-14 antigen ; Membrane Glycoproteins - analysis ; Membrane Glycoproteins - physiology ; Mice ; Mice, Inbred ICR ; Molecular and cellular biology ; Molecular Sequence Data ; Receptors, Immunologic - analysis ; Receptors, Immunologic - genetics ; Receptors, Lymphocyte Homing</subject><ispartof>Cell, 1989-03, Vol.56 (6), p.1045-1055</ispartof><rights>1989</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c507t-9039e465ae098cedb8fb0adf3336073b6284715b7969f2b0787282eea13caa783</citedby><cites>FETCH-LOGICAL-c507t-9039e465ae098cedb8fb0adf3336073b6284715b7969f2b0787282eea13caa783</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0092-8674(89)90637-5$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6851996$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2647302$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lasky, Laurence A.</creatorcontrib><creatorcontrib>Singer, Mark S.</creatorcontrib><creatorcontrib>Yednock, Ted A.</creatorcontrib><creatorcontrib>Dowbenko, Donald</creatorcontrib><creatorcontrib>Fennie, Christopher</creatorcontrib><creatorcontrib>Rodriguez, Henry</creatorcontrib><creatorcontrib>Nguyen, Thu</creatorcontrib><creatorcontrib>Stachel, Scott</creatorcontrib><creatorcontrib>Rosen, Steven D.</creatorcontrib><title>Cloning of a lymphocyte homing receptor reveals a lectin domain</title><title>Cell</title><addtitle>Cell</addtitle><description>Lymphocytes express cell surface molecules, termed homing receptors, that mediate their selective attachment to specialized high endothelial venules found within secondary lymphoid organs. Previous work has demonstrated that the adhesive interaction between lymphocytes and the endothelium of peripheral lymph nodes appears to involve a lectin-like activity. Moreover, MEL-14, a monoclonal antibody that blocks lymphocyte-peripheral lymph node binding and presumably recognizes the homing receptor mediating this adhesive interaction, appeared to detect the lectin-like receptor. In this paper we describe the cloning of a murine cDNA that encodes the antigen recognized by the MEL-14 antibody. Characterization of the cDNA encoding the putative mouse peripheral lymph node-specific homing receptor shows that it contains a lectin domain that appears to be involved in the binding of lymphocytes to peripheral lymph node endothelium, thus defining a new type of cellular adhesion molecule. This result supports a novel mechanism for the distribution of lymphocyte populations to various lymphoid organs.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antigens, Surface - analysis</subject><subject>Antigens, Surface - genetics</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Calcium - pharmacology</subject><subject>Carbohydrate Metabolism</subject><subject>Cell Adhesion</subject><subject>Cell Adhesion Molecules</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Cloning, Molecular</subject><subject>DNA - analysis</subject><subject>DNA - isolation & purification</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Lectins - analysis</subject><subject>Lectins - genetics</subject><subject>lymphocytes</subject><subject>Lymphocytes - cytology</subject><subject>MEL-14 antigen</subject><subject>Membrane Glycoproteins - analysis</subject><subject>Membrane Glycoproteins - physiology</subject><subject>Mice</subject><subject>Mice, Inbred ICR</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Receptors, Immunologic - analysis</subject><subject>Receptors, Immunologic - genetics</subject><subject>Receptors, Lymphocyte Homing</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1r3DAQhkVoSLZp_kECPpTSHtyOJOvrklKWNgkEemnOQpbHjYptbSRvYP995e6yx_Q0w7zPDMNDyBWFzxSo_AJgWK2laj5q88mA5KoWJ2RFwai6oYq9Iasjck7e5vwHALQQ4oycMdkoDmxFvq6HOIXpdxX7ylXDbtw8Rb-bsXqK4zJO6HEzx1SaF3RDXiD0c5iqLo4uTO_IaV_GeHmoF-Txx_df67v64eft_frbQ-0FqLk2wA02UjgEoz12re5bcF3POZegeCuZbhQVrTLS9KwFpRXTDNFR7p1Tml-QD_u7mxSft5hnO4bscRjchHGbrdJaSwPwX5AKBkoaU8BmD_oUc07Y200Ko0s7S8Eugu1izy72rDb2n2Arytr14f62HbE7Lh2Mlvz9IXfZu6FPbvIhHzGpBTVGFuxmj2GR9hIw2ewDTkVNKMpn28Xw-h9_AWU8lXg</recordid><startdate>19890324</startdate><enddate>19890324</enddate><creator>Lasky, Laurence A.</creator><creator>Singer, Mark S.</creator><creator>Yednock, Ted A.</creator><creator>Dowbenko, Donald</creator><creator>Fennie, Christopher</creator><creator>Rodriguez, Henry</creator><creator>Nguyen, Thu</creator><creator>Stachel, Scott</creator><creator>Rosen, Steven D.</creator><general>Elsevier Inc</general><general>Cell Press</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>7QL</scope><scope>7T5</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M81</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19890324</creationdate><title>Cloning of a lymphocyte homing receptor reveals a lectin domain</title><author>Lasky, Laurence A. ; Singer, Mark S. ; Yednock, Ted A. ; Dowbenko, Donald ; Fennie, Christopher ; Rodriguez, Henry ; Nguyen, Thu ; Stachel, Scott ; Rosen, Steven D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c507t-9039e465ae098cedb8fb0adf3336073b6284715b7969f2b0787282eea13caa783</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antigens, Surface - analysis</topic><topic>Antigens, Surface - genetics</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Calcium - pharmacology</topic><topic>Carbohydrate Metabolism</topic><topic>Cell Adhesion</topic><topic>Cell Adhesion Molecules</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Cloning, Molecular</topic><topic>DNA - analysis</topic><topic>DNA - isolation & purification</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Lectins - analysis</topic><topic>Lectins - genetics</topic><topic>lymphocytes</topic><topic>Lymphocytes - cytology</topic><topic>MEL-14 antigen</topic><topic>Membrane Glycoproteins - analysis</topic><topic>Membrane Glycoproteins - physiology</topic><topic>Mice</topic><topic>Mice, Inbred ICR</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Receptors, Immunologic - analysis</topic><topic>Receptors, Immunologic - genetics</topic><topic>Receptors, Lymphocyte Homing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lasky, Laurence A.</creatorcontrib><creatorcontrib>Singer, Mark S.</creatorcontrib><creatorcontrib>Yednock, Ted A.</creatorcontrib><creatorcontrib>Dowbenko, Donald</creatorcontrib><creatorcontrib>Fennie, Christopher</creatorcontrib><creatorcontrib>Rodriguez, Henry</creatorcontrib><creatorcontrib>Nguyen, Thu</creatorcontrib><creatorcontrib>Stachel, Scott</creatorcontrib><creatorcontrib>Rosen, Steven D.</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids 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>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lasky, Laurence A.</au><au>Singer, Mark S.</au><au>Yednock, Ted A.</au><au>Dowbenko, Donald</au><au>Fennie, Christopher</au><au>Rodriguez, Henry</au><au>Nguyen, Thu</au><au>Stachel, Scott</au><au>Rosen, Steven D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning of a lymphocyte homing receptor reveals a lectin domain</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1989-03-24</date><risdate>1989</risdate><volume>56</volume><issue>6</issue><spage>1045</spage><epage>1055</epage><pages>1045-1055</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><coden>CELLB5</coden><abstract>Lymphocytes express cell surface molecules, termed homing receptors, that mediate their selective attachment to specialized high endothelial venules found within secondary lymphoid organs. Previous work has demonstrated that the adhesive interaction between lymphocytes and the endothelium of peripheral lymph nodes appears to involve a lectin-like activity. Moreover, MEL-14, a monoclonal antibody that blocks lymphocyte-peripheral lymph node binding and presumably recognizes the homing receptor mediating this adhesive interaction, appeared to detect the lectin-like receptor. In this paper we describe the cloning of a murine cDNA that encodes the antigen recognized by the MEL-14 antibody. Characterization of the cDNA encoding the putative mouse peripheral lymph node-specific homing receptor shows that it contains a lectin domain that appears to be involved in the binding of lymphocytes to peripheral lymph node endothelium, thus defining a new type of cellular adhesion molecule. This result supports a novel mechanism for the distribution of lymphocyte populations to various lymphoid organs.</abstract><cop>Cambridge, MA</cop><pub>Elsevier Inc</pub><pmid>2647302</pmid><doi>10.1016/0092-8674(89)90637-5</doi><tpages>11</tpages></addata></record> |
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| ispartof | Cell, 1989-03, Vol.56 (6), p.1045-1055 |
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| subjects | Amino Acid Sequence Animals Antigens, Surface - analysis Antigens, Surface - genetics Base Sequence Biological and medical sciences Calcium - pharmacology Carbohydrate Metabolism Cell Adhesion Cell Adhesion Molecules Cell receptors Cell structures and functions Cloning, Molecular DNA - analysis DNA - isolation & purification Female Fundamental and applied biological sciences. Psychology Lectins - analysis Lectins - genetics lymphocytes Lymphocytes - cytology MEL-14 antigen Membrane Glycoproteins - analysis Membrane Glycoproteins - physiology Mice Mice, Inbred ICR Molecular and cellular biology Molecular Sequence Data Receptors, Immunologic - analysis Receptors, Immunologic - genetics Receptors, Lymphocyte Homing |
| title | Cloning of a lymphocyte homing receptor reveals a lectin domain |
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