Effect of tumor-associated mutant E-cadherin variants with defects in exons 8 or 9 on matrix metalloproteinase 3

Journal of Cellular Physiology
Margit FuchsBirgit Luber

Abstract

Tumor progression is characterized by loss of cell adhesion and increase of invasion and metastasis. The cell adhesion molecule E-cadherin is frequently down-regulated or mutated in tumors. In addition to down-regulation of cell adhesion, degradation of the extracellular matrix by matrix metalloproteinases is necessary for tumor cell spread. To investigate a possible link between E-cadherin and matrix metalloproteinase 3 (MMP-3), we examined expression of MMP-3 in human MDA-MB-435S cells transfected with wild-type (wt) or three different tumor-associated mutant E-cadherin variants with alterations in exons 8 or 9, originally identified in gastric carcinoma patients. In the presence of wt E-cadherin, the MMP-3 protein level was decreased in cellular lysates and in the supernatant where a secreted form of the protein is detectable. Down-regulation of MMP-3 was not found in MDA-MB-435S transfectants expressing mutant E-cadherin variants which indicates that E-cadherin mutations interfere with the MMP-3 suppressing function of E-cadherin. The mechanism of regulation of MMP-3 by E-cadherin is presently not clear. We have previously found that cell motility is enhanced by expression of the mutant E-cadherin variants used in this stud...Continue Reading

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Citations

Oct 26, 2007·Experimental Cell Research·Margit FuchsBirgit Luber
Aug 7, 2012·Journal of Neurochemistry·Inge Van HoveLieve Moons
Dec 9, 2008·American Journal of Physiology. Lung Cellular and Molecular Physiology·Alexander MargulisMarion T Kasaian
Sep 1, 2017·Biomedicine & Pharmacotherapy = Biomédecine & Pharmacothérapie·BaoChun WangNing Liu

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