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Prepublished online as a Blood First Edition Paper on August 7, 2003; DOI 10.1182/blood-2003-02-0500. This Article Full Text (PDF) All Versions of this Article: 2003-02-0500v1 102/13/4431    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by de Saint-Vis, B. Articles by Garrone, P. Search for Related Content PubMed PubMed Citation Articles by de Saint-Vis, B. Articles by Garrone, P. Social Bookmarking                   What's this? Submitted February 19, 2003 Accepted July 4, 2003 Human dendritic cells express neuronal Eph receptor tyrosine kinases: role of EphA2 in regulating adhesion to fibronectin Blandine de Saint-Vis*, Caroline Bouchet, Gregory Gautier, Jenny Valladeau, Christophe Caux, and Pierre Garrone Laboratory for Immunological Research, Schering-Plough, Dardilly, France INSERM, Unite 346, Hopital E. Herriot, Lyon, France * Corresponding author; email: blandine.de.saint.vis{at}spcorp.com. Eph receptor tyrosine kinases and their ligands, the ephrins, have been primarily described in the nervous system for their role in axon guidance, development and cell intermingling. Here we addressed whether Eph receptors may also regulate dendritic cells (DC) trafficking. RT-PCR analysis showed that DC derived from CD34+ progenitors, but not from monocytes, expressed several receptors, in particular EphA2, -A4, -A7, -B1, and EphB3 mRNA. EphB3 was specifically expressed by Langerhans cell type, and EphA2 and EphA7 by both Langerhans- and interstitial-type DC. EphA and EphB protein expression on in vitro generated DC was confirmed by staining with ephrin-A3-Fc and ephrin-B3-Fc fusion proteins that bind to different Eph members, in particular EphA2 and EphB3. Immunostaining with anti-EphA2 antibodies demonstrated the expression of EphA2 by immature DC and by ex vivo isolated skin Langerhans cells. Interestingly, ephrin expression was detected in epidermal keratinocytes and also in DC. Adhesion of CD34+-derived DC to fibronectin, but not to poly-L-lysine, was increased in the presence of ephrin-A3-Fc, a ligand of EphA2, through a in vitro 1 integrin activation pathway. As such, EphA2/ephrin-A3 interactions may play a role in the localization and network of Langerhans cells in the epithelium or/and in the regulation of their trafficking. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? 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