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  MMPs and TIMPs in Tumors

BioLegend offers a variety of reagents for MMP and TIMP research. Matrix metalloproteinases (MMPs) are calcium-dependent zinc endopeptidases, which degrade the extracellular matrix and remodel tissues. The catalytic activity of MMPs is tightly controlled at the level of gene expression and can be inhibited by specific inhibitors such as tissue inhibitors of matrix metalloproteinases (TIMPs). Valacca et al. examined the interaction between MMP-14 and TIMP-2 and conditions influencing tumor cell apoptosis or survival.

TIMP-2 binds to MMP-14 and, depending on the environment of the tumor cell, can lead to different responses. In the presence of collagen-I, TIMP-2 binds to MMP-14 and activates AKT, causing tumor cells to be protected by serum starvation-induced apoptosis. In the presence of collagen, TIMP-2 can induce apoptosis by blocking MMP-14s activity. Growth in the collagen environment simulates exposure of tumor cells to a pro-apoptotic extracellular matrix, while the collagen-free setting imitates epithelial cells adhering to their basement membrane. TIMP-2 and its interaction with MMP-14 can cause either pro- or anti-apoptotic signals depending on the environment.
Adapted from Valacca C, et al. 2015. PLoS One.  

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