ArticleInternational journal of molecular sciences2026
Extracellular Galectin-3/Carbohydrate Interactions Modulate Cancer Cellular Migration.
Article in International journal of molecular sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Galectin-3-mediated processes are important during many aspects of cancer progression, but they are not well understood. Galectin-3 is present extracellularly, and because of its carbohydrate recognition domain (CRD) and unstructured N-terminal domain (NTD), galectin-3 undergoes multimerization, which influences events such as carbohydrate-controlled cell-cell interactions. Investigations reported herein using an in vitro wound-healing assay show that exogenous galectin-3 inhibits cancer cellular migration. Since the addition of the galectin-3 CRD without the NTD does not arrest cellular migration, we attribute the effect of full-length galectin-3 on migration to the extracellular interactions between multimeric, full-length galectin-3 and extracellular receptors. In this publication, lactose-functionalized dendrimers serve as multivalent binding partners for galectin-3 and are used to mitigate extracellular multivalent galectin/carbohydrate interactions. The addition of lactose-functionalized dendrimers provides significant restoration of cellular migration in the presence of exogenous galectin-3 without increasing cellular viability. Thus, although galectin-3/protein interactions within the cell are known to increase both cellular migration and viability, cell surface galectin-3/carbohydrate interactions have the opposite impact and decrease cellular migration.
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