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Galectin-3 binding protein (Gal-3BP), coronary artery disease and cardiovascular mortality – insights from the LURIC study

ABSTRACT: Gal-3BP effects on human monocyte-derived macrophages were assessed in vitro. Macrophages were treated with recombinant human Gal-3BP or control buffer and gene expression was measured using Illumina Sentrix-8 gene arrays. Gene array data were analyzed with the Local pooled error (LPE). There was significant regulation of 217 probe sets corresponding to 200 genes (115 up, 85 down). Analysis of the significantly upregulated genes identified “inflammatory/immune response” as one of the most strongly regulated gene ontologies. Our finding that Gal-3BP induces genes and proteins involved in immune and inflammatory response in human monocyte-derived macrophages is in line with previously published data on the role of human Gal-3BP.

ORGANISM(S): Homo sapiens

PROVIDER: GSE97244 | GEO | 2017/04/01

SECONDARY ACCESSION(S): PRJNA381062

REPOSITORIES: GEO

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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.

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Galectin-3 binding protein (Gal-3BP), coronary artery disease and cardiovascular mortality – insights from the LURIC study

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