Modulation of endothelial cell migration and angiogenesis by Galectin-8

VÍCTOR MANUEL CÁRDENAS DELGADO; LUCAS COLOMBO; MARÍA FERNANDA TRONCOSO; LORENA NUGNES; ISABEL FRAHM; DIEGO CROCI; GABRIEL ADRIÁN RABINOVICH; CARLOTA WOLFENSTEIN-TODEL; MARÍA TERESA ELOLA

School of Pharmacy and Biochemistry, University of Buenos Aires

Simposio; IMBS Symposium.2 The Kohler-Milstein Conference; 2009

University of Freiburg (Germany), University of Buenos Aires (Argentina)

Galectins are a family of glycan-binding proteins with affinity for â-galactosides and a conserved sequence motif. They have the ability to decipher glycan-containing information and mediate cell-cell communication. Galectin-8 (Gal-8), member of this family, is a bivalent ‘tandem-repeat’ type galectin which possesses two CRDs connected by a linker peptide. It has been described the expression of galectin-1, -3, -8 and -9 in the endothelium. Moreover, galectin-1 and -3 have been directly implicated in angiogenic processes. In this report we provide compelling evidence of the angiogenesis-stimulating effect of gal-8 on in vitro assays. Furthermore, Gal-8 subcellular localization and immunohistochemical expression in vascular ECs of normal and tumor vessels are also analyzed.