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<dc:title>CD84 Functions as a homophilic adhesion molecule and enhances IFN- g secretion:adhesion is mediated by Ig-like domain 1</dc:title>
<dc:creator>Martín, Margarita</dc:creator>
<dc:creator>Romero, Xavier</dc:creator>
<dc:creator>Fuente García, Miguel Ángel de la</dc:creator>
<dc:creator>Tovar, Victoria</dc:creator>
<dc:creator>Zapater, Nuria</dc:creator>
<dc:creator>Esplugues, Enric</dc:creator>
<dc:creator>Pizcueta, Pilar</dc:creator>
<dc:creator>Bosch, Jaime</dc:creator>
<dc:creator>Engel, Pablo</dc:creator>
<dc:subject>Biología molecular</dc:subject>
<dc:description>Producción Científica</dc:description>
<dc:description>CD84 is a member of the CD2 subset of the Ig superfamily of cell surface molecules. Its cytoplasmic tail binds to Src homology 2 domain-containing protein 1A (signaling lymphocytic activation molecule-associated protein), a protein encoded by the X-linked lymphoproliferative disease gene. It is preferentially expressed on B lymphocytes, monocytes, and platelets. We show that it is also expressed on thymocytes and T cells. CD84 was positive on CD4 CD8  thymocytes, and its expression decreased with cell maturation. It is expressed on mature T cells preferentially on CD45RO . To identify the CD84 ligand, we generated a soluble&#xd;
Ig fusion protein containing the human CD84 extracellular domains (CD84-Ig). Because receptor-ligand interactions occur between several members of this subfamily, we assayed CD84-Ig binding with all members of the CD2 family. CD84-Ig bound to CD84-transfected cells, whereas no binding was detected with cells expressing other CD2 subfamily receptors, showing that CD84 binds to itself. Anti-CD84 mAbs recognizing epitopes wholly within domain 1 of CD84 blocked the binding of the CD84-Ig fusion protein to CD84-transfected cells and platelets. Data from CD84 domain human/mouse chimeras further revealed that only the first extracellular domain of the molecule is involved in the ligand receptor recognition. The CD84-CD84 interaction was independent of its cytoplasmic tail. Finally, concurrent ligation of human CD84 with mAbs or CD84-Ig and CD3 enhanced IFN-secretion in human lymphocytes. Thus, CD84 is its own ligand and acts as a costimulatory molecule.</dc:description>
<dc:date>2015-04-08T11:33:45Z</dc:date>
<dc:date>2015-04-08T11:33:45Z</dc:date>
<dc:date>2001</dc:date>
<dc:type>info:eu-repo/semantics/article</dc:type>
<dc:identifier>The Journal of Immunology 2001, 167(7): 3668–3676.</dc:identifier>
<dc:identifier>0022-1767</dc:identifier>
<dc:identifier>http://uvadoc.uva.es/handle/10324/10152</dc:identifier>
<dc:identifier>10.4049/jimmunol.167.7.3668</dc:identifier>
<dc:identifier>3668</dc:identifier>
<dc:identifier>7</dc:identifier>
<dc:identifier>3676</dc:identifier>
<dc:identifier>The Journal of Immunology</dc:identifier>
<dc:identifier>167</dc:identifier>
<dc:language>eng</dc:language>
<dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
<dc:rights>http://creativecommons.org/licenses/by-nc-nd/4.0/</dc:rights>
<dc:rights>Attribution-NonCommercial-NoDerivatives 4.0 International</dc:rights>
<dc:publisher>American Association of Immunologists</dc:publisher>
<dc:peerreviewed>SI</dc:peerreviewed>
</ow:Publication>
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