HOW DO PROTEIN-GLYCAN INTERACTIONS REGULATE T-CELL PHYSIOLOGY?

MARTA A. TOSCANO; JUAN M. ILARREGUI; GERMAN A. BIANCO; NATALIA RUBINSTEIN; GABRIEL A. RABINOVICH

MEDICINA (BUENOS AIRES)

Fundación Revista Medicina (Buenos Aires)

Lugar: Buenos Aires; Año: 2006 vol. 66 p. 357 - 362

0025-7680

Recent evidence indicates that protein-glycan interactions play a critical role in different events associated with the physiology of T-cell responses including thymocyte maturation, T-cell activation, lymphocyte migration and T-cell apoptosis. Glycans decorating T-cell surface glycoproteins can modulate T-cell physiology by specifically interacting with endogenous lectins including selectins and galectins. These endogenous lectins are capable of recognizing sugar structures localized on T-cell surface glycoproteins and trigger different signal transduction pathways leading to differentiation, proliferation, cell cycle regulation or apoptosis. Protein-carbohydrate interactions may be controlled at different levels, including regulated expression of lectins during T-cell maturation and differentiation and the spatio-temporal regulation of glycosyltransferases and glycosidases, which create and modify sugar structures present in T-cell surface glycoproteins. This article briefly reviews the mechanisms by which protein-carbohydrate interactions modulate immunological processes such as T-cell activation, migration and apoptosis.