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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 Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) Antibodies (450) and Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) Kits (162) and many more products for this protein.
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MMP3 contributes to the pathogenesis of ARDS by affecting the pulmonary inflammatory response in female mice in relevant models of lung injury.
endogenously secreted chemerin (show RARRES2 Proteins) plays an autocrine/paracrine role in white adipose tissue, identifying chemerin (show RARRES2 Proteins) as a therapeutic target to modulate adipose remodelling.
Overexpression of Mmp3 in 3T3-L1 preadipocytes inhibited differentiation. High fat diet-induced obesity downregulates adipocyte MMP3 expression to trigger adipogenesis, and adipocyte TIMP4 (show TIMP4 Proteins) may modulate this process to regulate hyperplastic vs. hypertrophic adipose tissue expansion, fat distribution, and metabolic health in a sex- and depot-dependent manner.
Matrix metalloprotease (show ADAMTS7 Proteins) 3 (MMP3), an endogenous neuronal activator of microglia, increased cytokine release from YAC128 microglia compared to wildtype microglia. We found elevated MMP levels in Huntington's Disease (HD) CSF (show CSF2 Proteins), and MMP levels correlate with disease severity in HD. These data support a novel role for MMPs and microglial activation in HD pathogenesis.
These results indicate that periodic induction, via use of an eye drop, of AAV-mediated secretion of MMP-3 into aqueous humour could have therapeutic potential for those cases of glaucoma that are sub-optimally responsive to conventional pressure-reducing medications.
Data show that loss of loss of matrix metalloproteinase-3 (MMP-3) repressed the upregulation of the chemokines monocyte chemoattractant protein (MCP)-1 (show CPT1B Proteins) and (C-X-C motif) ligand 1 (CXCL1 (show CXCL1 Proteins)).
Mmp3-knockout mice maintained higher arterial oxygenation compared to wild-type mice in a model of acute lung injury.
NMP4 (show ZNF384 Proteins) deficiency suppressed the arthritis-induced increase in bone resorption, expression of RANKL (show TNFSF11 Proteins) and MMP-3 mRNA.
MMP-3 produced in blood vessel endothelial cells after spinal cord injury serves as an endogenous molecule for microglial activation followed by p38MAPK (show MAPK14 Proteins) activation and proNGF production
genetic inactivation of MMP-3 has profound effects on the structural integrity and plasticity response of the visual cortex of adult mice
2G allele of MMP-1 (show MMP1 Proteins), C allele of MMP-2 (show MMP2 Proteins) and 5A/6A genotype of MMP-3 are associated with susceptibility and disease progression of type 2 diabetic nephropathy
MMP-1 (show MMP1 Proteins) genotype may accelerate the development of HIV-associated neurocognitive disorder (HAND) whereas MMP3 -1612 5A5A genotype may reduce the risk of pathogenesis of HAND.
Preliminary studies indicate that baseline MMP3 and TIMP3 (show TIMP3 Proteins) concentrations are associated with patient survival and disease-free time
MMP-3 (Lys45Glu) polymorphisms associate with obesity risk and its severity.
Data suggest that serum matrix metalloproteinase-3 (MMP-3) and the 7-joint ultrasound score (US7) scores could both effectively reflect disease activity and therapeutic responses in patients with moderate to severe rheumatoid arthritis (RA).
results demonstrated that measurement of MMP-3 could become a marker of disease activity in rheumatoid arthritis patients
The results indicated that the 5A allele of the MMP3 gene-promoter region could be associated with oral submucous fibrosis risk factor, but not oral squamous cell carcinoma, in an Indian population
C/EBPbeta (show CEBPB Proteins) upregulation promoted tumor cell invasion in an MMP3-dependent manner in vitro and was associated with metastatic status in colorectal cancer
MMP3 (and MMP-1 (show MMP1 Proteins) and MMP-2 (show MMP2 Proteins)) are independently associated with markers of arterial stiffening in patients with type 1 diabetes.
A significant increase in the frequency of the MMP3-1171dupA (rs3025058) polymorphism genotype among patients with unstable angina was detected.
The present study was aimed to determine the association between metalloproteinase 3 (MMP3), transforming growth factor beta 1 (TGFbeta1 (show TGFB1 Proteins)) and collagen type X alpha I (COL10A1 (show COL10A1 Proteins)) gene polymorphisms with traits related to leg weakness in pigs.
the identification of MMP1 (show MMP1 Proteins) and MMP10 (show MMP10 Proteins) genes in swine is reported.
contribution of MMPs to the inflammatory breakdown of the blood-CSF (show CSF2 Proteins) barrier in vitro
Results indicate that leukemia inhibitory factor (LIF (show LIF Proteins)) and Oncostatin M (show OSM Proteins) increase the expression of MMP-1 (show MMP1 Proteins), MMP-3, and TIMP-1 (show TIMP1 Proteins) several fold, and that their expression is reduced to basal levels in the presence of the LIF (show LIF Proteins) antagonist MH35-BD.
Compromised autophagy may be related to the osteoarthritis progression; JNK (show MAPK8 Proteins) and p38 (show MAPK14 Proteins) MAPKs up-regulate MMP3 and down-regulate autophagy.
chitosan-pDNA nanoparticles encoding shRNA targeting MMP-3 and -13 had great potential in silencing the dedifferentiation-related genes for regenerating prolonged and endurable cartilage.
Ulinastatin (show AMBP Proteins) effectively inhibited the increased expression of MMP-2 (show MMP2 Proteins), MMP-3, and iNOS (show NOS2 Proteins) in degenerated NP cells induced by IL-1beta (show IL1B Proteins) in vitro.
Tongxinluo can inhibit the expression of MMP-3 and 9 and increase the expression of PPARgamma (show PPARG Proteins) in atherosclerotic rabbits.
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. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
, matrix metalloproteinase 3
, matrix metalloproteinase-3
, stromelysin 1
, PTR1 protein
, matrix metalloproteinase 3 (stromelysin 1, progelatinase)
, metalloproteinase 3 receptor
, matrix metallopeptidase 3 (stromelysin 1, progelatinase)
, matrix metalloproteinase 10 (stromelysin 2)