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dc.contributor.authorMartín, Margarita
dc.contributor.authorRomero, Xavier
dc.contributor.authorFuente García, Miguel Ángel de la 
dc.contributor.authorTovar, Victoria
dc.contributor.authorZapater, Nuria
dc.contributor.authorEsplugues, Enric
dc.contributor.authorPizcueta, Pilar
dc.contributor.authorBosch, Jaime
dc.contributor.authorEngel, Pablo
dc.date.accessioned2015-04-08T11:33:45Z
dc.date.available2015-04-08T11:33:45Z
dc.date.issued2001
dc.identifier.citationThe Journal of Immunology 2001, 167(7): 3668–3676.es
dc.identifier.issn0022-1767es
dc.identifier.urihttp://uvadoc.uva.es/handle/10324/10152
dc.descriptionProducción Científicaes
dc.description.abstractCD84 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 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.es
dc.format.mimetypeapplication/pdfes
dc.language.isoenges
dc.publisherAmerican Association of Immunologistses
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectBiología moleculares
dc.titleCD84 Functions as a homophilic adhesion molecule and enhances IFN- g secretion:adhesion is mediated by Ig-like domain 1es
dc.typeinfo:eu-repo/semantics/articlees
dc.identifier.doi10.4049/jimmunol.167.7.3668es
dc.identifier.publicationfirstpage3668es
dc.identifier.publicationissue7es
dc.identifier.publicationlastpage3676es
dc.identifier.publicationtitleThe Journal of Immunologyes
dc.identifier.publicationvolume167es
dc.peerreviewedSIes
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International


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