Sandbox 985
From Proteopedia
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== Disease == | == Disease == | ||
| - | Matrix metalloproteinase (MMP)-9, one of the most widely investigated MMPs, regulates pathological remodeling processes that involve inflammation and fibrosis in cardiovascular disease. MMP-9 directly degrades extracellular matrix (ECM) proteins and activates cytokines and chemokines to regulate tissue remodeling. MMP-9 deletion or inhibition has proven overall beneficial in multiple animal models of cardiovascular disease. | + | === Cardiovascular === |
| + | Matrix metalloproteinase (MMP)-9, one of the most widely investigated MMPs, regulates pathological remodeling processes that involve inflammation and fibrosis in cardiovascular disease. MMP-9 directly degrades extracellular matrix (ECM) proteins and activates cytokines and chemokines to regulate tissue remodeling. MMP-9 deletion or inhibition has proven overall beneficial in multiple animal models of cardiovascular disease. | ||
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| + | === Hypertension === | ||
| + | MMP-9 activity is induced very early with the development of hypertension, contributing to collagen breakdown and arterial distensibility. An increase in fibrillar collagen in the compensated stage of hypertension is associated with increased MMP-9 activity. An increased arterial pressure and altered remodeling in the blood vessels lead to a pressure overload of the heart. Under these conditions, both vascular and cardiac tissues undergo additional compensatory remodeling. MMP-9 activity is increased in arteries with high pressure compared with vessels under normal pressure. | ||
== Relevance == | == Relevance == | ||
Revision as of 14:33, 4 May 2015
MMP family members share similar fundamental structural characteristics and are classified according to their substrate specificity. By this classification, MMP-9 belongs to the gelatinase subgroup and is known as gelatinase B due to its ability to degrade gelatin. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. The zinc binding motif HEXXHXXGXXH in the catalytic domain, and the “cysteine switch” motif PRCGXPD in the propeptide are common structural signatures, where three histidines in the zinc binding motif coordinate and the cysteine in the propetide coordinate with the catalytic zinc ion. MMP9 is produced by the several cell types, normal alveolar macrophages and granulocytes.
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
