New Aspects of Galectin Functionality in Nuclei of Cultured Bone Marrow Stromal and Epidermal Cells: Biotinylated Galectins as a Tool to Detect Specific Binding Sites

The study explored the nuclear presence and functionality of galectins, particularly galectin-1, in cultured bone marrow stromal cells and keratinocytes. Researchers used biotinylated galectins as a tool to detect specific nuclear binding sites, finding that galectin-1, but not galectins-3, -5, or -7, showed reactivity in these cells. The binding of galectin-1 was linked to the carbohydrate recognition domain and was observed in nuclear speckles, colocalizing with the SC35 splicing factor. This binding was sensitive to RNase treatment, indicating a role in RNA processing. Additionally, cells with galectin-1 binding sites expressed ΔNp63, a stem cell marker, and were identified as basal cells based on cytokeratin expression. The study concluded that labeled galectins could effectively localize binding sites, enhancing the understanding of galectin functionality in the nucleus.