Extracellular galectin-3 induces MMP9 expression by activating p38 MAPK pathway via lysosome-associated membrane protein-1 (LAMP1)

Molecular and Cellular Biochemistry
Manohar C DangeRajiv D Kalraiya

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.

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Citations

May 16, 2018·Endocrine Connections·Eva Olga MelinMagnus Hillman
Jun 24, 2020·Molecular Genetics & Genomic Medicine·Yu-Huang LiaoYu-Lin Ko
Sep 28, 2018·Frontiers in Cellular Neuroscience·Laura Thomas, Laura Andrea Pasquini
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