Galectin-8: a matricellular lectin with key roles in angiogenesis

TRONCOSO MF; FERRAGUT F; BACIGALUPO ML; CARDENAS DELGADO VM; NUGNES LG; GENTILINI L; LADERACH D; WOLFENSTEIN DE TODEL C; COMPAGNO D; RABINOVICH GA; ELOLA MT

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 carbohydraterecognition domains connected by a linker peptide. gal-8 is expressed both in the cytoplasmand nucleus in vascular endothelial cells from normal and tumor-associated blood vessels, andin lymphatic endothelial cells. Herein we describe a novel role for gal-8 in the regulation ofvascular and lymphatic angiogenesis and provide evidence of its critical implications in tumorbiology. Functional assays revealed central roles for gal-8 in the control of capillary-tubeformation, endothelial cell migration, and in vivo angiogenesis. So far, two endothelial ligandshave been described for gal-8, namely podoplanin in lymphatic vessels and CD166 (ALCAM,activated leukocyte cell adhesion molecule) in vascular endothelial cells. Other related gal-8functions are also summarized here including cell adhesion and migration, which collectivelydemonstrate the multi-functionality of this complex lectin. Thus, gal-8 is an importantcomponent of the angiogenesis network, and an essential molecule in the extracellular matrixby providing molecular anchoring to this surrounding matrix. The implications of gal-8 intumor angiogenesis remain to be further explored, but it is exciting to speculate thatmodulating gal-8-glycan interactions could be used to block lymphatic-vascular connectionsvital for metastasis.