Abstract
Matrix metalloproteinases (MMPs), also known as matrixins, belong to a group of zinc-dependent proteins, which are thought to play a central role in the breakdown of extracellular matrix. Collagen, elastin, gelatin and casein are major components cleaved by MMPs. The breakdown of these components is essential for many physiological processes such as embryonic development, morphogenesis, reproduction, and tissue resorption and remodelling. MMPs also participate in pathological processes such as arthritis, cancer, cardiovascular and neurological diseases. This review summarizes current knowledge regarding these proteins, their participation in physiological and pathophysiological roles, their involvement in activation and inhibition, and their interactions with other metal-binding proteins including metallothioneins.
Keywords: Matrix metalloproteinases, collagen, tissue inhibitors of matrix metalloproteinases, cysteine switch, zinc, metallothionein, tumour disease, morphogenesis, tissue resorption, neurological diseases, metal-binding proteins, metalloproteinase, interstitial collagenase, pre-synthetic region, nu-clear magnetic resonance (NMR), N-Terminal Propeptide, C-Terminal Domain, Stromelysin-1, Matrilysin, Collagenase-3, Enamelysin, Epilysin, Catalytic Domain, Stromelysins, Macrophage Elastase, inflammatory tissue, INHIBITION OF MMPs, Gene Expression, Regulation of MMP Activity, Tissues Inhibitors, ZINC-CONTAINING PROTEINS, zinc-binding proteins, non-extracellular ma-trix, atherosclerosis, gastritis ulcer disease, central nervous system, disease, metastasis, Tumour Growth, Tumour Protection, Apoptosis, Angiogenesis, hereditary disorders
Current Medicinal Chemistry
Title: Matrix Metalloproteinases
Volume: 17 Issue: 31
Author(s): O. Zitka, J. Kukacka, S. Krizkova, D. Huska, V. Adam, M. Masarik, R. Prusa and R. Kizek
Affiliation:
Keywords: Matrix metalloproteinases, collagen, tissue inhibitors of matrix metalloproteinases, cysteine switch, zinc, metallothionein, tumour disease, morphogenesis, tissue resorption, neurological diseases, metal-binding proteins, metalloproteinase, interstitial collagenase, pre-synthetic region, nu-clear magnetic resonance (NMR), N-Terminal Propeptide, C-Terminal Domain, Stromelysin-1, Matrilysin, Collagenase-3, Enamelysin, Epilysin, Catalytic Domain, Stromelysins, Macrophage Elastase, inflammatory tissue, INHIBITION OF MMPs, Gene Expression, Regulation of MMP Activity, Tissues Inhibitors, ZINC-CONTAINING PROTEINS, zinc-binding proteins, non-extracellular ma-trix, atherosclerosis, gastritis ulcer disease, central nervous system, disease, metastasis, Tumour Growth, Tumour Protection, Apoptosis, Angiogenesis, hereditary disorders
Abstract: Matrix metalloproteinases (MMPs), also known as matrixins, belong to a group of zinc-dependent proteins, which are thought to play a central role in the breakdown of extracellular matrix. Collagen, elastin, gelatin and casein are major components cleaved by MMPs. The breakdown of these components is essential for many physiological processes such as embryonic development, morphogenesis, reproduction, and tissue resorption and remodelling. MMPs also participate in pathological processes such as arthritis, cancer, cardiovascular and neurological diseases. This review summarizes current knowledge regarding these proteins, their participation in physiological and pathophysiological roles, their involvement in activation and inhibition, and their interactions with other metal-binding proteins including metallothioneins.
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Cite this article as:
Zitka O., Kukacka J., Krizkova S., Huska D., Adam V., Masarik M., Prusa R. and Kizek R., Matrix Metalloproteinases, Current Medicinal Chemistry 2010; 17 (31) . https://dx.doi.org/10.2174/092986710793213724
DOI https://dx.doi.org/10.2174/092986710793213724 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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