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

TRONCOSO, MARÍA F.; FERRAGUT, FÁTIMA; BACIGALUPO, MARÍA L.; CÁRDERAS DELGADO, VICTOR M.; NUGNES, LORENA G.; GENTILINI, LUCAS; LADERACH, DIEGO; WOLFENSTEIN-TODEL, CARLOTA; COMPAGNO, DANIEL; RABINOVICH, GABRIEL A.; ELOLA, MARÍA T.

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 from normal and tumor blood vessels, and in lymphatic endothelial cells. The number of newly discovered genes and proteins contributing to angiogenesis is growing too fast. Herein, an essential new role for Gal-8 in the regulation of vascular and lymphatic angiogenesis is described, which might have critical implications in tumor biology. Functional assays revealed Gal-8 roles in the control of capillary-tube formation, endothelial cell migration, and in vivo angiogenesis. So far, two endothelial ligands have been described for Gal-8, that is podoplanin in lymphatic and CD166 (ALCAM, activated leukocyte cell adhesion molecule) in vascular endothelial cells. Other related Gal-8 functions are also explored such as cell adhesion and migration, which demonstrate the multi-functionality of this complex lectin. Taken together, we conclude that Gal-8 is another player in the angiogenesis network, and an essential molecule in the extracellular matrix by providing molecular anchoring to this surrounding matrix. The potential functions of Gal-8 in tumor angiogenesis still remain to be studied, but it is exciting to speculate that interfering with Gal-8 expression might be used to block lymphatic-vascular connections vital for metastasis.