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Modulation of CD6 function through interaction with Galectin‐1 and ‐3
Author(s) -
Escoda-Ferran Cristina,
Carrasco Esther,
Caballero-Baños Miguel,
Miró-Julià Cristina,
Martínez-Florensa Mario,
Consuegra-Fernández Marta,
Martínez Vanesa G.,
Liu Fu-Tong,
Lozano Francisco
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.05.064
Subject(s) - alcam , galectin , microbiology and biotechnology , receptor , galectin 1 , t cell , biology , chemistry , cell adhesion molecule , immunology , biochemistry , immune system
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.
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