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

被引：35

作者：

Dange, Manohar C. ^{[1
]}

Agarwal, Akhil Kumar ^{[1
]}

Kalraiya, Rajiv D. ^{[1
]}

机构：

[1] Tata Mem Hosp, ACTREC, Kalraiya Lab, Navi Mumbai 410210, India

来源：

MOLECULAR AND CELLULAR BIOCHEMISTRY | 2015年 / 404卷 / 1-2期

关键词：

Galectin-3; PolyLacNAc; MMP9; p38; MAPK; LAMP1; TUMOR-CELLS; MELANOMA-CELLS; MATRIX METALLOPROTEINASES; CANCER PROGRESSION; GENE-EXPRESSION; METASTASIS; GLYCOSYLATION; ADHESION; OLIGOSACCHARIDES; GLYCOPROTEINS;

D O I：

10.1007/s11010-015-2367-5

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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.

引用

页码：79 / 86

页数：8

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