Matrix metalloproteinases stimulate epithelial-mesenchymal transition during tumor development - PubMed (original) (raw)
Review
Matrix metalloproteinases stimulate epithelial-mesenchymal transition during tumor development
Lidiya S Orlichenko et al. Clin Exp Metastasis. 2008.
Abstract
Matrix metalloproteinases (MMPs) are a family of more than 28 enzymes that were initially identified on the basis of their ability to cleave most elements of the extracellular matrix (ECM) but have subsequently been found to be upregulated in nearly every tumor type. As digestion of the ECM is essential for tumor invasion and metastasis, MMPs have been studied for their role in these later stages of tumor development. More recently, exposure to these enzymes has been found to impact cellular signaling pathways that stimulate cell growth at early stages of tumor progression. MMPs have also been found to cleave intracellular targets and so inducing mitotic abnormalities and genomic instability. Emerging evidence indicates that tumor-associated MMPs can also stimulate processes associated with epithelial-mesenchymal transition (EMT), a developmental process that is activated in tumor cells during cell invasion and metastasis. Investigations of potential therapeutic MMP inhibitors aimed at blocking the protumorigenic tissue alterations induced by MMPs have been complicated by the side effects associated with nonspecific inhibition of normal physiological processes; recent investigations have shown how delineation of the extracellular targets and intracellular signaling pathways by which MMP action on cancer cells can induce EMT provides insight into novel therapeutic targets. Here, we provide an overview of recent findings of MMP action in tumors and the mechanisms by which MMPs induce both phenotypic and genotypic alterations that facilitate tumor progression.
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References
- J Immunol. 2004 Jun 1;172(11):7060-8 - PubMed
- Int J Oncol. 2006 Jan;28(1):33-42 - PubMed
- Oncogene. 1999 Nov 18;18(48):6835-9 - PubMed
- Oncogene. 2000 Mar 16;19(12):1605-12 - PubMed
- J Cell Biol. 1997 Dec 29;139(7):1861-72 - PubMed
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