Dataset Information

MUSCLE-DERIVED GALECTIN 3 IS A NEW MEDIATOR OF MUSCLE TO BONE CROSSTALK

ABSTRACT: Galectin-3 is a pleiotropic lectin that regulates multiple cellular processes in a multitude of tissue types. In bone, depending on its cellular localization, Galectin 3 has a dual and opposite role, as if on the one hand intracellular Galectin 3 promotes bone formation, on the other circulating Galectin 3 antagonizes osteoblast differentiation and increases osteoclast activity. In the present study, we demonstrate that Gal-3 is released in the extracellular environment from muscle cultured cells, and reveal the role of Gal-3 in muscle to bone crosstalk, as a factor able to impair bone homeostasis during muscle differentiation and following muscular activity

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Cell Culture

SUBMITTER: Manuela Piazzi

LAB HEAD: Jessika Bertacchini

PROVIDER: PXD040187 | Pride | 2025-05-06

REPOSITORIES: Pride

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			Action	DRS
	2-black_HyperG-1002119_g90-20-Top7_05.raw	Raw
	2-black_HyperG-1002119_g90-20-Top7_08.raw	Raw
	2-black_HyperG-1002119_g90-20-Top7_13.raw	Raw
	3-black_HyperG-1002119_g90-20-Top7_06.raw	Raw
	3-black_HyperG-1002119_g90-20-Top7_10.raw	Raw

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Publications

Myoblast-Derived Galectin 3 Impairs the Early Phases of Osteogenesis Affecting Notch and Akt Activity.

Amore Emanuela E Cenni Vittoria V Piazzi Manuela M Signore Michele M Orlandi Giulia G Neri Simona S Biressi Stefano S Barone Rosario R Di Felice Valentina V Follo Matilde Y MY Bertacchini Jessika J Palumbo Carla C

Biomolecules 20240930 10

Galectin-3 (Gal-3) is a pleiotropic lectin produced by most cell types, which regulates multiple cellular processes in various tissues. In bone, depending on its cellular localization, Gal-3 has a dual and opposite role. If, on the one hand, intracellular Gal-3 promotes bone formation, on the other, its circulating form affects bone remodeling, antagonizing osteoblast differentiation and increasing osteoclast activity. From an analysis of the secretome of cultured differentiating myoblasts, we i ...[more]

PMID: 39456175

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Project description:Identification of interactors is a major attempt in cell biology. Not only protein-protein but also protein-carbohydrate interactions are of high relevance for signal transduction in biological systems. Here we aim to identify novel interacting binding partners for the β-galactoside-binding proteins Galectin-1 (Gal-1) and Galectin-3 (Gal-3) in context of the eye disease proliferative vitreoretinopathy (PVR). PVR is one of the most common failures after retinal detachment surgeries and is characterized by the migration, adhesion and epithelial-to-mesenchymal transition (EMT) of retinal pigment epithelial cells (RPE) and the subsequent formation of sub- and epiretinal fibrocellular membranes. Gal-1 and Gal-3 bind in a dose- and carbohydrate-dependent manner to mesenchymal RPE cells and inhibit cellular processes like attachment and spreading. Yet knowledge about glycan-dependent interactors of Gal-1 and Gal-3 on RPE cells is very limited, although this is a prerequisite to unravel the influence of galectins on distinct cellular processes in RPE cells. In this approach, we identified by galectin pull-down experiments and quantitative proteomic screening 131 Galectin-3 and 15 Galectin-1 interactors. They mainly play a role in multiple binding processes and are mostly membrane proteins. Here we focused on two novel identified interactors of Gal-1 and Gal-3 in the context of PVR: the low-density lipoprotein receptor LRP1 and the platelet-derived growth factor receptor beta PDGFRB. We observed crosslinking and lattice formation of exogenous Gal-1 and Gal-3 with LRP1/PDGFRB and ITGB1 on the cell surface of human RPE cells. Weaker binding of Gal-1 and Gal-3 on these interactors and no lattice formation on the cell surface was seen, when complex-type-N-glycosylation was inhibited by treatment of the cells with Kifunensine. In conclusion, the identified specific glycoprotein ligands for Gal-1 and Gal-3 give us new insights in the highly specific binding of galectins to dedifferentiated RPE cells and the resulting prevention of PVR-associated cellular events.