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. 2020 May 31;12(6):1421. doi: 10.3390/cancers12061421

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Gal-3 is involved in cell adhesion regulation, migration, invasion, angiogenesis, and metastasis. The specific extracellular Gal-3 function depends on the polymerization of Gal-3 into pentameric complexes. The action of Galectin 3 depends on glycan binding partners. These complexes link to glycans of high complexity (e.g., N-glycosylation lactosamine tetra-antennary forms and the Thomsen–Fredenreich antigen on O-glycans, especially in cancer. Through carbohydrate binding and polymerization to pentamers, Gal-3 forms a lattice and regulates the position of growth factor receptors, including EGFR, integrins and proteins like MUC16.