dc.contributor.author | Martín, Margarita | |
dc.contributor.author | Romero, Xavier | |
dc.contributor.author | Fuente García, Miguel Ángel de la | |
dc.contributor.author | Tovar, Victoria | |
dc.contributor.author | Zapater, Nuria | |
dc.contributor.author | Esplugues, Enric | |
dc.contributor.author | Pizcueta, Pilar | |
dc.contributor.author | Bosch, Jaime | |
dc.contributor.author | Engel, Pablo | |
dc.date.accessioned | 2015-04-08T11:33:45Z | |
dc.date.available | 2015-04-08T11:33:45Z | |
dc.date.issued | 2001 | |
dc.identifier.citation | The Journal of Immunology 2001, 167(7): 3668–3676. | es |
dc.identifier.issn | 0022-1767 | es |
dc.identifier.uri | http://uvadoc.uva.es/handle/10324/10152 | |
dc.description | Producción Científica | es |
dc.description.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 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.mimetype | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | American Association of Immunologists | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | |
dc.subject | Biología molecular | es |
dc.title | CD84 Functions as a homophilic adhesion molecule and enhances IFN- g secretion:adhesion is mediated by Ig-like domain 1 | es |
dc.type | info:eu-repo/semantics/article | es |
dc.identifier.doi | 10.4049/jimmunol.167.7.3668 | es |
dc.identifier.publicationfirstpage | 3668 | es |
dc.identifier.publicationissue | 7 | es |
dc.identifier.publicationlastpage | 3676 | es |
dc.identifier.publicationtitle | The Journal of Immunology | es |
dc.identifier.publicationvolume | 167 | es |
dc.peerreviewed | SI | es |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 International |
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