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• W4304128531 endingPage "1451" @default.
• W4304128531 startingPage "1451" @default.
• W4304128531 abstract "Melanoma cell adhesion molecule (MCAM, CD146, MUC18) is a heavily glycosylated transmembrane protein and a marker of melanoma metastasis. It is expressed in advanced primary melanoma and metastasis but rarely in benign naevi or normal melanocytes. More and more evidence has shown that activation of the MCAM on cell surface plays a vital role in melanoma progression and metastasis. However, the natural MCAM binding ligand that initiates MCAM activation in melanoma so far remains elusive. This study revealed that galectin-3, a galactoside-binding protein that is commonly overexpressed in many cancers including melanoma, is naturally associated with MCAM on the surface of both skin and uveal melanoma cells. Binding of galectin-3 to MCAM, via O-linked glycans on the MCAM, induces MCAM dimerization and clustering on cell surface and subsequent activation of downstream AKT signalling. This leads to the increases of a number of important steps in melanoma progression of cell proliferation, adhesion, migration, and invasion. Thus, galectin-3 is a natural binding ligand of MCAM in melanoma, and their interaction activates MCAM and promotes MCAM-mediated melanoma progression. Targeting the galectin-3–MCAM interaction may potentially be a useful therapeutic strategy for melanoma treatment." @default.
• W4304128531 created "2022-10-11" @default.
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• W4304128531 date "2022-10-10" @default.
• W4304128531 modified "2023-10-18" @default.
• W4304128531 title "Galectin-3 Is a Natural Binding Ligand of MCAM (CD146, MUC18) in Melanoma Cells and Their Interaction Promotes Melanoma Progression" @default.
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• W4304128531 doi "https://doi.org/10.3390/biom12101451" @default.
• W4304128531 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36291660" @default.
• W4304128531 hasPublicationYear "2022" @default.
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