Modulation of CD6 function through interaction with Galectin-1 and -3

  • FEBS Lett. 2014 Aug 25;588(17):2805-13. doi: 10.1016/j.febslet.2014.05.064.
Cristina Escoda-Ferran  1 ,  Esther Carrasco  1 ,  Miguel Caballero-Baños  2 ,  Cristina Miró-Julià  1 ,  Mario Martínez-Florensa  1 ,  Marta Consuegra-Fernández  1 ,  Vanesa G Martínez  1 ,  Fu-Tong Liu  3 ,  Francisco Lozano  4
Affiliations
  • 1. From Institut d'Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), Centre Esther Koplowitz, 08036 Barcelona, Spain.
  • 2. Servei d'Immunologia, Centre de Diagnòstic Biomèdic, Hospital Clínic de Barcelona, 08036 Barcelona, Spain.
  • 3. Department of Dermatology, UC Davis School of Medicine, Sacramento, CA 95816, United States.
  • 4. From Institut d'Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), Centre Esther Koplowitz, 08036 Barcelona, Spain; Servei d'Immunologia, Centre de Diagnòstic Biomèdic, Hospital Clínic de Barcelona, 08036 Barcelona, Spain; Departament de Biologia Cel lular, Immunologia i Neurociències, Facultat de Medicina Universitat de Barcelona, 08036 Barcelona, Spain. Electronic address: [email protected].
PMID: 24945728 DOI: 10.1016/j.febslet.2014.05.064
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
ALCAM/CD166; Apoptosis; CD6; Cell adhesion; Galectin; T-cell activation.