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Exploring the In situ pairing of human galectins toward synthetic O-mannosylated core M1 glycopeptides of α-dystroglycan

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Title: Exploring the In situ pairing of human galectins toward synthetic O-mannosylated core M1 glycopeptides of α-dystroglycan
Authors: Villones, Lareno L. Browse this author
Ludwig, Anna-Kristin Browse this author
Kumeta, Hiroyuki Browse this author
Kikuchi, Seiya Browse this author
Ochi, Rika Browse this author
Aizawa, Tomoyasu Browse this author
Nishimura, Shin-Ichiro Browse this author
Gabius, Hans-Joachim Browse this author
Hinou, Hiroshi Browse this author →KAKEN DB
Issue Date: 23-Oct-2022
Publisher: Nature Portfolio
Journal Title: Scientific reports
Volume: 12
Issue: 1
Start Page: 17800
Publisher DOI: 10.1038/s41598-022-22758-0
Abstract: Dystroglycan (DG), which constitutes a part of the dystrophin-glycoprotein complex, connects the extracellular matrix to the cytoskeleton. The matriglycans presented by the extracellular alpha-DG serve as a contact point with extracellular matrix proteins (ECM) containing laminin G-like domains, providing cellular stability. However, it remains unknown whether core M1 (GlcNAc beta 1-2Man) structures can serve as ligands among the various O-Mannosylated glycans. Therefore, based on the presence of N-acetylLactosamine (LacNAc) in this glycan following the core extension, the binding interactions with adhesion/growth-regulatory galectins were explored. To elucidate this process, the interaction between galectin (Gal)-1, -3, -4 and -9 with alpha-DG fragment (372)TRGAIIQTPTLGPIQPTRV(390) core M1-based glycopeptide library were profiled, using glycan microarray and nuclear magnetic resonance studies. The binding of galectins was revealed irrespective of its modular architecture, adding galectins to the list of possible binding partners of alpha-DG core M1 glycoconjugates by cis-binding (via peptide- and carbohydrate-protein interactions), which can be abrogated by alpha 2,3-sialylation of the LacNAc units. The LacNAc-terminated alpha-DG glycopeptide interact simultaneously with both the S- and F-faces of Gal-1, thereby inducing oligomerization. Furthermore, Gal-1 can trans-bridge alpha-DG core M1 structures and laminins, which proposed a possible mechanism by which Gal-1 ameliorates muscular dystrophies; however, this proposal warrants further investigation.
Type: article
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

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