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Exploring the role of sialidases in Galectin-1-associated resistance to cancer therapies.

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Biochimica et biophysica acta. General subjects 📖 저널 OA 3.1% 2026 Vol.1870(6) p. 130931 cited 1 Galectins and Cancer Biology
TL;DR Findings indicate that glycosyltransferases, particularly MGAT5, GCNT1, and ST6GAL1, coordinately shape the GAL1-specific glycome in settings of therapeutic resistance, whereas glycan remodeling by endogenous sialidases does not play a major role.
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PubMed DOI OpenAlex Semantic 마지막 보강 2026-04-28
OpenAlex 토픽 · Galectins and Cancer Biology Glycosylation and Glycoproteins Research Signaling Pathways in Disease

Scheidegger MA, Merlo JP, Villarreal SN, Schattner M, Croci DO, Dalotto-Moreno T, Mariño KV, Rabinovich GA

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Findings indicate that glycosyltransferases, particularly MGAT5, GCNT1, and ST6GAL1, coordinately shape the GAL1-specific glycome in settings of therapeutic resistance, whereas glycan remodeling by en

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APA Marco A Scheidegger, Joaquín P. Merlo, et al. (2026). Exploring the role of sialidases in Galectin-1-associated resistance to cancer therapies.. Biochimica et biophysica acta. General subjects, 1870(6), 130931. https://doi.org/10.1016/j.bbagen.2026.130931
MLA Marco A Scheidegger, et al.. "Exploring the role of sialidases in Galectin-1-associated resistance to cancer therapies.." Biochimica et biophysica acta. General subjects, vol. 1870, no. 6, 2026, pp. 130931.
PMID 41831659

Abstract

The diverse repertoire of cell surface glycans, generated by the coordinated activity of glycosyltransferases and glycosidases, encodes critical biological information that is interpreted by glycan-binding proteins including galectins. Galectin-1 (GAL1), a member of this family, plays key roles across multiple hallmarks of cancer, including angiogenesis and immune evasion, driving resistance to anti-angiogenic and immunotherapeutic strategies through glycosylation-dependent mechanisms. Here, we first review the contribution of GAL1-glycan interactions to therapeutic resistance in cancer, with a particular focus on anti-angiogenic therapies and immunotherapy, and discuss the central role of glycosyltransferases in shaping these responses. While the biosynthesis of 'GAL1-permissive' glycans has been extensively characterized, the contribution of post-synthetic glycan remodeling to GAL1-driven therapeutic resistance remains uncertain. To explore mechanisms underlying GAL1-mediated resistance, we investigated whether tumor- or stromal-derived sialidases (NEU1 or NEU3) modulate sensitivity to vascular endothelial growth factor (VEGF)-targeted therapies by unmasking GAL1-binding glyco-epitopes. In the second part of the study, we present original in vivo experiments using gain- and loss-of-function approaches, demonstrating that, at least in our experimental settings, sialidases do not contribute to resistance to anti-VEGF treatment. Finally, bioinformatic analyses of patient datasets revealed differential regulation of GAL1, as well as specific glycosyltransferases, in patients responding or not to anti-VEGF or anti-PD-1 therapies. Collectively, these findings indicate that glycosyltransferases, particularly MGAT5, GCNT1, and ST6GAL1, coordinately shape the GAL1-specific glycome in settings of therapeutic resistance, whereas glycan remodeling by endogenous sialidases does not play a major role. Whether sialidases influence GAL1-dependent functions in other contexts remains to be explored.

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