<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-04-14T16:56:38Z</responseDate><request verb="GetRecord" identifier="oai:uvadoc.uva.es:10324/10152" metadataPrefix="mods">https://uvadoc.uva.es/oai/request</request><GetRecord><record><header><identifier>oai:uvadoc.uva.es:10324/10152</identifier><datestamp>2022-06-28T07:30:28Z</datestamp><setSpec>com_10324_1133</setSpec><setSpec>com_10324_931</setSpec><setSpec>com_10324_894</setSpec><setSpec>col_10324_1209</setSpec></header><metadata><mods:mods xmlns:mods="http://www.loc.gov/mods/v3" xmlns:doc="http://www.lyncode.com/xoai" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-1.xsd">
<mods:name>
<mods:namePart>Martín, Margarita</mods:namePart>
</mods:name>
<mods:name>
<mods:namePart>Romero, Xavier</mods:namePart>
</mods:name>
<mods:name>
<mods:namePart>Fuente García, Miguel Ángel de la</mods:namePart>
</mods:name>
<mods:name>
<mods:namePart>Tovar, Victoria</mods:namePart>
</mods:name>
<mods:name>
<mods:namePart>Zapater, Nuria</mods:namePart>
</mods:name>
<mods:name>
<mods:namePart>Esplugues, Enric</mods:namePart>
</mods:name>
<mods:name>
<mods:namePart>Pizcueta, Pilar</mods:namePart>
</mods:name>
<mods:name>
<mods:namePart>Bosch, Jaime</mods:namePart>
</mods:name>
<mods:name>
<mods:namePart>Engel, Pablo</mods:namePart>
</mods:name>
<mods:extension>
<mods:dateAvailable encoding="iso8601">2015-04-08T11:33:45Z</mods:dateAvailable>
</mods:extension>
<mods:extension>
<mods:dateAccessioned encoding="iso8601">2015-04-08T11:33:45Z</mods:dateAccessioned>
</mods:extension>
<mods:originInfo>
<mods:dateIssued encoding="iso8601">2001</mods:dateIssued>
</mods:originInfo>
<mods:identifier type="citation">The Journal of Immunology 2001, 167(7): 3668–3676.</mods:identifier>
<mods:identifier type="issn">0022-1767</mods:identifier>
<mods:identifier type="uri">http://uvadoc.uva.es/handle/10324/10152</mods:identifier>
<mods:identifier type="doi">10.4049/jimmunol.167.7.3668</mods:identifier>
<mods:identifier type="publicationfirstpage">3668</mods:identifier>
<mods:identifier type="publicationissue">7</mods:identifier>
<mods:identifier type="publicationlastpage">3676</mods:identifier>
<mods:identifier type="publicationtitle">The Journal of Immunology</mods:identifier>
<mods:identifier type="publicationvolume">167</mods:identifier>
<mods:abstract>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.</mods:abstract>
<mods:language>
<mods:languageTerm>eng</mods:languageTerm>
</mods:language>
<mods:accessCondition type="useAndReproduction">info:eu-repo/semantics/openAccess</mods:accessCondition>
<mods:accessCondition type="useAndReproduction">http://creativecommons.org/licenses/by-nc-nd/4.0/</mods:accessCondition>
<mods:accessCondition type="useAndReproduction">Attribution-NonCommercial-NoDerivatives 4.0 International</mods:accessCondition>
<mods:subject>
<mods:topic>Biología molecular</mods:topic>
</mods:subject>
<mods:titleInfo>
<mods:title>CD84 Functions as a homophilic adhesion molecule and enhances IFN- g secretion:adhesion is mediated by Ig-like domain 1</mods:title>
</mods:titleInfo>
<mods:genre>info:eu-repo/semantics/article</mods:genre>
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