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Metalloproteinases and Their Inhibitors: Potential for the Development of New Therapeutics

Overview
Journal Cells
Publisher MDPI
Date 2020 May 30
PMID 32466129
Citations 108
Authors
Affiliations
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Abstract

The metalloproteinase (MP) family of zinc-dependent proteases, including matrix metalloproteinases (MMPs), a disintegrin and metalloproteases (ADAMs), and a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTSs) plays a crucial role in the extracellular matrix (ECM) remodeling and degradation activities. A wide range of substrates of the MP family includes ECM components, chemokines, cell receptors, and growth factors. Metalloproteinases activities are tightly regulated by proteolytic activation and inhibition via their natural inhibitors, tissue inhibitors of metalloproteinases (TIMPs), and the imbalance of the activation and inhibition is responsible in progression or inhibition of several diseases, e.g., cancer, neurological disorders, and cardiovascular diseases. We provide an overview of the structure, function, and the multifaceted role of MMPs, ADAMs, and TIMPs in several diseases via their cellular functions such as proteolysis of other cell signaling factors, degradation and remodeling of the ECM, and other essential protease-independent interactions in the ECM. The significance of MP inhibitors targeting specific MMP or ADAMs with high selectivity is also discussed. Recent advances and techniques used in developing novel MP inhibitors and MP responsive drug delivery tools are also reviewed.

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References
1.
Arkadash V, Yosef G, Shirian J, Cohen I, Horev Y, Grossman M . Development of High Affinity and High Specificity Inhibitors of Matrix Metalloproteinase 14 through Computational Design and Directed Evolution. J Biol Chem. 2017; 292(8):3481-3495. PMC: 5336179. DOI: 10.1074/jbc.M116.756718. View

2.
Deryugina E, Ratnikov B, Strongin A . Prinomastat, a hydroxamate inhibitor of matrix metalloproteinases, has a complex effect on migration of breast carcinoma cells. Int J Cancer. 2003; 104(5):533-41. DOI: 10.1002/ijc.10977. View

3.
Li Y, Xu X, Chen X, Wei G, He B, Wang J . The nuclear factor-κB pathway is involved in matrix metalloproteinase-9 expression in RU486-induced endometrium breakdown in mice. Hum Reprod. 2012; 27(7):2096-106. DOI: 10.1093/humrep/des110. View

4.
Loechel F, Fox J, Murphy G, Albrechtsen R, Wewer U . ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3. Biochem Biophys Res Commun. 2000; 278(3):511-5. DOI: 10.1006/bbrc.2000.3835. View

5.
Masciantonio M, Lee C, Arpino V, Mehta S, Gill S . The Balance Between Metalloproteinases and TIMPs: Critical Regulator of Microvascular Endothelial Cell Function in Health and Disease. Prog Mol Biol Transl Sci. 2017; 147:101-131. DOI: 10.1016/bs.pmbts.2017.01.001. View