Sandbox 985
From Proteopedia
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'''Matrix metalloproteinase 9''' | '''Matrix metalloproteinase 9''' | ||
| - | 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. | + | 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. <ref> </Yabluchanskiy, A., Y. Ma, R. P. Iyer, M. E. Hall, and M. L. Lindsey. "Matrix Metalloproteinase-9: Many Shades of Function in Cardiovascular Disease." Physiology 28.6 (2013): 391-403. Web. 4 May 2015.> |
<StructureSection load='1l6j' size='340' side='right' caption='Human matrix metalloproteinase MMP9 (gelatinase B),1l6j' scene=''> | <StructureSection load='1l6j' size='340' side='right' caption='Human matrix metalloproteinase MMP9 (gelatinase B),1l6j' scene=''> | ||
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MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. | MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. | ||
| - | Emerging evidences suggest that membrane-anchored proteases play important roles during growth, morphogenesis, tissue repair, and pathogenesis. It has been proposed that, by concentrating at or near the cell surface, the proteolytic activities of these enzymes can be effective even in the presence of high concentrations of (diffusable) inhibitors.<ref></Takahashi, C. "Regulation of Matrix Metalloproteinase-9 and Inhibition of Tumor Invasion by the Membrane-anchored Glycoprotein RECK." Proceedings of the National Academy of Sciences 95.22 (1998): 13221-3226. Web. 4 May 2015.> | + | Emerging evidences suggest that membrane-anchored proteases play important roles during growth, morphogenesis, tissue repair, and pathogenesis. It has been proposed that, by concentrating at or near the cell surface, the proteolytic activities of these enzymes can be effective even in the presence of high concentrations of (diffusable) inhibitors.<ref> </Takahashi, C. "Regulation of Matrix Metalloproteinase-9 and Inhibition of Tumor Invasion by the Membrane-anchored Glycoprotein RECK." Proceedings of the National Academy of Sciences 95.22 (1998): 13221-3226. Web. 4 May 2015.> |
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MMP-9 is absent from most normal adult tissues, including the intestinal epithelial cells. We and several others have shown that MMP-9 is highly expressed during intestinal inflammation in different animal models and human IBD. In addition to its role in inflammation, recent studies from our laboratory have shown that MMP-9 plays a role in epithelial cell differentiation. | MMP-9 is absent from most normal adult tissues, including the intestinal epithelial cells. We and several others have shown that MMP-9 is highly expressed during intestinal inflammation in different animal models and human IBD. In addition to its role in inflammation, recent studies from our laboratory have shown that MMP-9 plays a role in epithelial cell differentiation. | ||
Revision as of 17:18, 4 May 2015
Matrix metalloproteinase 9
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. [1]
