info:eu-repo/semantics/article
Galectin-8: a matricellular lectin with key roles in angiogenesis
Fecha
2014-10Registro en:
Troncoso, María Fernanda; Ferragut, Fátima; Bacigalupo, Maria Lorena; Cardenas Delgado, Victor Manuel; Nugnes, Lorena Gisela; et al.; Galectin-8: a matricellular lectin with key roles in angiogenesis; Oxford University Press; Glycobiology; 24; 10; 10-2014; 907-914
0959-6658
CONICET Digital
CONICET
Autor
Troncoso, María Fernanda
Ferragut, Fátima
Bacigalupo, Maria Lorena
Cardenas Delgado, Victor Manuel
Nugnes, Lorena Gisela
Gentilini, Lucas Daniel
Laderach, Diego Jose
Wolfenstein, Carlota Elisa
Compagno, Daniel Georges
Rabinovich, Gabriel Adrian
Elola, Maria Teresa
Resumen
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.