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Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Additionally we are shipping MMP8 Antibodies (201) and MMP8 Kits (115) and many more products for this protein.
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Suggest that Ang-(1 (show ANGPT1 Proteins)-7) plays an important role in protecting against atherosclerosis via counter-regulation of Ang II (show AGT Proteins)-induced MMP-8.
MMP8 plays an important role in intestinal I/R injury through mechanisms involving increased inflammation and loss of claudin-3 (show CLDN3 Proteins)
These results suggest that some of the anti-inflammatory effects of Dexamethasone are mediated through increased MMP-8 expression.
These results suggest a novel pathogenetic role of MMP8 and implicate modulation of its activity as a tractable strategy for therapies against cerebral ischemia.
Fusion peptide inhibitors of MMP-8/-9 prevent endotoxic shock if administered within a strict time window.
the loss of MMP-8 likely has pleiotropic effects on innate immunity and angiogenesis that are reflected in changes in the protease web.
A previously unknown role of MMP8 in M2-macrophage polarization by cleaving fibromodulin (show FMOD Proteins) and therefore increasing the bioavailability of TGF-beta (show TGFB1 Proteins).
MMP-8-deficient mice had significantly lower serum triglyceride (TG) levels (P = 0.003) and larger HDL (show HSD11B1 Proteins) particles compared with wild-type (WT) mice. However, no differences were observed in the apoA-I (show APOA1 Proteins) levels.
These results demonstrate that MMP-8 critically mediates microglial activation by modulating TNF-alpha (show TNF Proteins) activity, which may explain neuroinflammation in septic mouse brain.
MMP-13 (show MMP13 Proteins) prevails over MMP-8 in collagen degradation in atheromata.
Data show that polymorphism in the promoter region of matrix metallopeptidase 8 (MMP-8) (-799C/T) and two non-synonymous polymorphisms (Val436Ala and Lys460Thr) were not significantly associated with risk of pterygium.pterygium.
Persistent oral human papillomavirus infection was associated with a low salivary MMP-8 concentration indicating eventually a failure in oral anti-inflammatory defence.
Reduced expression of types I and III collagen and TIMP-1 (show TIMP1 Proteins) as well as the increased expression of MMP-1 (show MMP1 Proteins) and MMP-8 in the anterior vaginal wall tissues play important roles in the onset of pelvic organ prolapse.
Genetic polymorphism in S100A9 (show S100A9 Proteins)-S100A12 (show S100A12 Proteins)-S100A8 (show S100A8 Proteins) locus affects serum and plasma MMP-8 and shows a suggestive association with the risk of cardiovascular diseases.
Our study demonstrated that the MMP-8 C-799T is associated with the risk of developing severe preeclampsia during pregnancy. However, the MMP-8 C + 17G polymorphism might not be a risk factor for susceptibility to preeclampsia.
Our findings suggest that the polymorphisms at MMP-8 -799C/T, Val436Ala and Lys460Thr may not play a major role in determining the personal susceptibility to childhood acute lymphoblastic leukemia in Taiwan.
Reduction in serum levels of MMP8 predicted complete remission in type 2 diabetes mellitus patients following bariatric surgery.
MMP8 -799C/T, Val436Ala and Lys460Thr polymorphisms may only play an indirect role in determining personal cancer susceptibility to breast cancer in Taiwan.
Our findings suggest that the polymorphisms at MMP-8 C-799T or Val436Ala may not play a major role in mediating personal risk of oral cancer; however, the detailed mechanisms require further investigation.
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage. Its function is degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
matrix metallopeptidase 8 (neutrophil collagenase)
, matrix metalloproteinase 8
, collagenase 2
, matrix metalloproteinase-8
, neutrophil collagenase
, neutrophil collagenease
, PMNL collagenase
, matrix metalloproteinase 8 (neutrophil collagenase)