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<title>CD84 Functions as a homophilic adhesion molecule and enhances IFN- g secretion:adhesion is mediated by Ig-like domain 1</title>
<creator>Martín, Margarita</creator>
<creator>Romero, Xavier</creator>
<creator>Fuente García, Miguel Ángel de la</creator>
<creator>Tovar, Victoria</creator>
<creator>Zapater, Nuria</creator>
<creator>Esplugues, Enric</creator>
<creator>Pizcueta, Pilar</creator>
<creator>Bosch, Jaime</creator>
<creator>Engel, Pablo</creator>
<subject>Biología molecular</subject>
<description>Producción Científica</description>
<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.</description>
<date>2015-04-08</date>
<date>2015-04-08</date>
<date>2001</date>
<type>info:eu-repo/semantics/article</type>
<identifier>The Journal of Immunology 2001, 167(7): 3668–3676.</identifier>
<identifier>0022-1767</identifier>
<identifier>http://uvadoc.uva.es/handle/10324/10152</identifier>
<identifier>10.4049/jimmunol.167.7.3668</identifier>
<identifier>3668</identifier>
<identifier>7</identifier>
<identifier>3676</identifier>
<identifier>The Journal of Immunology</identifier>
<identifier>167</identifier>
<language>eng</language>
<rights>info:eu-repo/semantics/openAccess</rights>
<rights>http://creativecommons.org/licenses/by-nc-nd/4.0/</rights>
<rights>Attribution-NonCommercial-NoDerivatives 4.0 International</rights>
<publisher>American Association of Immunologists</publisher>
</thesis></metadata></record></GetRecord></OAI-PMH>