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Review
. 2014 Oct;24(10):907-14.
doi: 10.1093/glycob/cwu054. Epub 2014 Jun 16.

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

María F Troncoso  1 , Fátima Ferragut  1 , María L Bacigalupo  1 , Víctor M Cárdenas Delgado  1 , Lorena G Nugnes  1 , Lucas Gentilini  2 , Diego Laderach  2 , Carlota Wolfenstein-Todel  1 , Daniel Compagno  2 , Gabriel A Rabinovich  3 , María T Elola  4
Affiliations
Review

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

María F Troncoso et al. Glycobiology. 2014 Oct.

Abstract

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.

Keywords: CD166; angiogenesis; endothelium; galectin-8.

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