Extracellular galectin-3 induces MMP9 expression by activating p38 MAPK pathway via lysosome-associated membrane protein-1 (LAMP1)
Extracellular galectin-3 induces MMP9 expression by activating p38 MAPK pathway via lysosome-associated membrane protein-1 (LAMP1)
复制标题
DOI：
10.1007/s11010-015-2367-5
复制
发表时间：
2015-06-01
影响因子：
4.3
通讯作者：
Kalraiya, Rajiv D.
中科院分区：
文献类型：
--
作者：
Dange, Manohar C.;Agarwal, Akhil Kumar;Kalraiya, Rajiv D.
基质金属蛋白酶(MMPs)在基质重塑和侵袭转移中起关键作用。细胞外Galectin-3被证明能诱导MMP9的分泌。在这里，我们证明了Galectin-3在转录水平上诱导MMP9，并且它依赖于聚N-乙酰乳糖胺(PolyLacNAc)的表面水平。通过使用信号通路抑制剂，MMP9的表达被证明是通过p38 MAP-K途径诱导的。利用多聚LacNAc的主要载体溶酶体相关膜蛋白1(LAMP1)表达shRNA的黑色素瘤细胞克隆，表面LAMP1被证明是Galectin-3通过p38MAPK途径诱导MMP9表达的关键介质之一。
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.