Galectins: matricellular glycan-binding proteins linking cell adhesion, migration, and survival

ELOLA, MT; WOLFENSTEIN-TODEL, C; TRONCOSO, MF; VASTA, GR; RABINOVICH, GA

CELLULAR AND MOLECULAR LIFE SCIENCES

Springer

Año: 2007 vol. 64 p. 1679 - 1700

1420-682X

Galectins are a taxonomically widespread family of glycan-binding proteins, defined by at least one conserved carbohydrate-recognition domain with a canonical amino acid sequence and affinity for b-galactosides. Because of their anti-adhesive as well as adhesive extracellular functions, galectins should be considered as a novel class of adhesion-modulating proteins collectively known as “matricellular proteins” (which include SPARC, thrombospondin, tenascin, hevin and disintegrins). Accordingly, galectins sometimes have de-adhesive effects when presented as soluble proteins to cells in a strong adhesive state. In this context the de-adhesive properties of galectins should be considered as physiologically relevant as the pro-adhesive effects of these glycan-binding proteins. This article focuses on the roles of mammalian galectins in cell adhesion, spreading, and migration, and the cross-regulation of these functions. Although careful attention should be paid when examining individual galectin functions due to overlapping distributions, these intriguing glycan-binding proteins offer promising possibilities for the treatment and intervention of a wide variety of pathological processes including cancer, inflammation, and autoimmunity.