Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870141 | FEBS Letters | 2014 | 9 Pages |
Abstract
CD6 is a lymphocyte glycoprotein receptor that physically associates with the antigen-specific receptor complex at the center of the immunological synapse, where it interacts with its ligand CD166/ALCAM. The present work reports the carbohydrate-dependent interaction of CD6 and CD166/ALCAM with Galectin-1 and -3, two well-known soluble mammalian lectins. Both galectins interfered with superantigen-induced T cell proliferation and cell adhesion phenomena mediated by the CD6-CD166/ALCAM pair, while CD6 expression protected cells from galectin-induced apoptosis. The results suggest that interaction of Galectin-1 and -3 with CD6 and CD166/ALCAM might modulate some relevant aspects of T cell physiology.
Keywords
TMBPGNPRRsSEBLTACD6PFACRDTEC3,3′,5,5′-tetramethylbenzidineo/nlipoteichoic acidStaphylococcal enterotoxin BDissociation constantApoptosisRoom temperatureDendritic cellThymic epithelial cellsT-cell activationALCAMactivated leukocyte cell adhesion moleculeparaformaldehydePeptidoglycanCell adhesiongalectinPattern-recognition receptorovernight
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Cristina Escoda-Ferran, Esther Carrasco, Miguel Caballero-Baños, Cristina Miró-Julià , Mario MartÃnez-Florensa, Marta Consuegra-Fernández, Vanesa G. MartÃnez, Fu-Tong Liu, Francisco Lozano,