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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1989-5-9
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lymphocyte Homing
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1045-55
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2647302-Amino Acid Sequence,
pubmed-meshheading:2647302-Animals,
pubmed-meshheading:2647302-Antigens, Surface,
pubmed-meshheading:2647302-Base Sequence,
pubmed-meshheading:2647302-Calcium,
pubmed-meshheading:2647302-Carbohydrate Metabolism,
pubmed-meshheading:2647302-Cell Adhesion,
pubmed-meshheading:2647302-Cell Adhesion Molecules,
pubmed-meshheading:2647302-Cloning, Molecular,
pubmed-meshheading:2647302-DNA,
pubmed-meshheading:2647302-Female,
pubmed-meshheading:2647302-Lectins,
pubmed-meshheading:2647302-Lymphocytes,
pubmed-meshheading:2647302-Membrane Glycoproteins,
pubmed-meshheading:2647302-Mice,
pubmed-meshheading:2647302-Mice, Inbred ICR,
pubmed-meshheading:2647302-Molecular Sequence Data,
pubmed-meshheading:2647302-Receptors, Immunologic,
pubmed-meshheading:2647302-Receptors, Lymphocyte Homing
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pubmed:year |
1989
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pubmed:articleTitle |
Cloning of a lymphocyte homing receptor reveals a lectin domain.
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pubmed:affiliation |
Department of Cardiovascular Research, Genentech, Inc. South San Francisco, California 94080.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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