GALECTIN-8: A MATRICELLULAR LECTIN WITH KEY ROLES IN ANGIOGENESIS

MARIA F TRONCOSO; FATIMA FERRAGUT; MARÍA L BACIGALUPO; VÍCTOR M CARDENAS DELGADO; LORENA G NUGNES; LUCAS GENTILINI; DIEGO LADERACH; CARLOTA WOLFENSTEIN-TODEL; DANIEL COMPAGNO; GABRIEL ADRIAN RABINOVICH; ELOLA MARIA TERESA

GLYCOBIOLOGY

OXFORD UNIV PRESS INC

Lugar: Oxford; Año: 2014 vol. 24 p. 907 - 914

0959-6658

Galectin-8 (gal-8) is a "tandem-repeat"-type galectin, containing two carbohydrate recognition domains connected by a linker peptide. gal-8 is expressed both in the cytoplasm and nucleus in vascular endothelial cells (ECs) from normal and tumor-associated blood vessels, and in lymphatic endothelial cells. Herein, we describe a novel role for gal-8 in the regulation of vascular and lymphatic angiogenesis and provide evidence of its critical implications in tumor biology. Functional assays revealed central roles for gal-8 in the control of capillary-tube formation, EC migration and in vivo angiogenesis. So far, two endothelial ligands have been described for gal-8, namely podoplanin in lymphatic vessels and CD166 (ALCAM, activated leukocyte cell adhesion molecule) in vascular ECs. Other related gal-8 functions are also summarized here, including cell adhesion and migration, which collectively demonstrate the multi-functionality of this complex lectin. Thus, gal-8 is an important component of the angiogenesis network, and an essential molecule in the extracellular matrix by providing molecular anchoring to this surrounding matrix. The implications of gal-8 in tumor angiogenesis remain to be further explored, but it is exciting to speculate that modulating gal-8-glycan interactions could be used to block lymphatic-vascular connections vital for metastasis.