Abstract
Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases capable of degrading essentially all components of extracellular matrix (ECM). MMPs play a role in normal remodeling processes, e.g. fetal development, tissue repair, and angiogenesis, as well as in pathologic conditions, including rheumatoid arthritis, periodontitis, autoimmune blistering disorders of skin, tumor cell invasion, and metastasis (1).The activity of MMPs is specifically inhibited by tissue inhibitors of metalloproteinases (TIMPs), which bind to active MMPs in 1:1 molar stoichiometry (1,2). The TIMP gene family consists of four members, TIMP-1, -2, -3 and -4, which share common features in their genomic organization and tertiary structure (2). In contrast to other TIMPs, which are secreted in soluble form, TIMP-3 is associated with ECM (3).
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Abbreviations
- MMP:
-
matrix metalloproteinase
- TIMP:
-
tissue inhibitor of metalloproteinases
References
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© 1998 Springer Science+Business Media New York
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Ahonen, M., Baker, A.H., Kähäri, VM. (1998). High Level Expression of Tissue Inhibitors of Metalloproteinases-1,-2 and -3 in Melanoma Cells Achieved by Adenovirus Mediated Gene Transfer. In: Walden, P., Trefzer, U., Sterry, W., Farzaneh, F., Zambon, P. (eds) Gene Therapy of Cancer. Advances in Experimental Medicine and Biology, vol 451. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5357-1_11
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DOI: https://doi.org/10.1007/978-1-4615-5357-1_11
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