Abstract
Matrix metalloproteinases (MMPs) play a key role in matrix remodelling and thus invasion and metastasis. Extracellular galectin-3 has been shown to induce MMP9 secretion. Here, we demonstrate that galectin-3 induces MMP9 at transcript level and it is dependent on the surface levels of poly-N-acetyllactosamine (polyLacNAc). By employing signalling pathway inhibitors, MMP9 expression was shown to be induced via p38 MAP-kinase pathway. Using clones of melanoma cells expressing shRNAs to lysosome-associated membrane protein-1 (LAMP1), a major carrier of polyLacNAc, surface LAMP1 was demonstrated to serve as one of the key mediators of galectin-3-induced MMP9 expression via p38 MAPK pathway.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cell Line, Tumor
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Galectin 3 / biosynthesis*
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Galectin 3 / genetics
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Gene Expression Regulation, Neoplastic
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Humans
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Lysosomal-Associated Membrane Protein 1 / biosynthesis*
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Lysosomal-Associated Membrane Protein 1 / genetics
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MAP Kinase Signaling System / genetics
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Matrix Metalloproteinase 9 / biosynthesis*
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Matrix Metalloproteinase 9 / genetics
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Melanoma, Experimental / genetics
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Melanoma, Experimental / pathology
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Mice
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p38 Mitogen-Activated Protein Kinases / biosynthesis*
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p38 Mitogen-Activated Protein Kinases / genetics
Substances
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Galectin 3
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Lysosomal-Associated Membrane Protein 1
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p38 Mitogen-Activated Protein Kinases
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MMP9 protein, human
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Matrix Metalloproteinase 9