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malfunction
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hsa-miR-222 regulates UM1 cancer cell invasion, at least in part, by indirectly regulating MMP1 expression through targeting superoxide dismutase SOD2 mRNA, overview
malfunction
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hypoxia and specifically HIF-1a increase CXCR4 and MMP1 expression in JJ cell line and chondrosarcoma invasion in vitro
malfunction
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inflammatory tissue destruction is central to pathology in cerebral tuberculosis with microglial-derived matrix metalloproteinases playing a key role in driving such damage
malfunction
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MMP-1 is downregulated 4fold during trophoblast differentiation, reduced MMP-1 expression in pre-eclampsia and fetal growth restriction
malfunction
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MMP-1 is involved in photoaging of the skin
malfunction
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MMP-1A is strongly expressed in tumor and arthritis specimens
malfunction
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periodontal disease is characterized by increased expression and activity of matrix metalloproteinases and insufficient expression/activity of their inhibitors, tissue inhibitors of matrix metalloproteinases, TIMPs. This altered MMP-TIMP balance results in progressive destruction of gingival and periodontal extracellular matrix
malfunction
the catalytically domain of MMP-1 (MMP-1 CAT) alone does not cleave collagen
malfunction
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MMP-1A is strongly expressed in tumor and arthritis specimens
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metabolism
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altering the binding of at least two transcription factors, c-Jun and SP1, proteasome inhibition results in increased production of MMP-1 and decreases synthesis of type I collagen in human dermal fibroblasts. Differential effects of proteasome inhibition and TGF-beta on MMP-1 and MMP-2, overview
metabolism
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effects of baicalin on the total protein amount and collagen I mRNA expression in periodontal ligament cells, and the regulatory effects on MMP-1/TIMP-1 expression, overview
metabolism
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interleukin-6 and high glucose synergistically upregulate MMP-1 expression by U-937 cell mononuclear phagocytes via ERK1/2 and JNK pathways and c-Jun, MMP-1 regulation, overview
metabolism
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matrix metalloproteinase-1 is regulated in tuberculosis by a p38 MAPK-dependent, p-aminosalicylic acid-sensitive signaling cascade. The p38 MAPK pathway regulates the divergence between MMPs and TIMP-1, overview
metabolism
astragaloside IV controls collagen reduction in photoaging skin by improving transforming growth factor-beta/Smad signaling suppression and inhibiting matrix metalloproteinase-1. Transforming growth factor beta type II protein and COL1 mRNA decreased but MMP-1 and Smad7 levels increased in the photoaging model group, which is reversed by topical application of AST. AST prevents collagen reduction from UV irradiation in photoaging skin
metabolism
matrix metalloproteinase 1 and collagens play a key role in platelet-derived growth factor (PDGF) and stromal cell-derived factor-1 (SDF-1) promotion of the skin wound repairing effect of bone mesenchymal stem cells. Bone marrow mesenchymal stem cells (BMSCs) are applied to treatment of skin wounds. PDGF treatment recruits BSMCs to injured sites and strengthens the effect of BMSCs on skin wound by suppressing activity of MMP-1. SDF-1 treatment increases the treating effect of BMSCs on skin injury through the deposition of collagen I and collagen III. Phenotypes, overview
metabolism
methotrexate (MTX) significantly reduces collagen type I production in different strains of fibroblasts derived from neonatal, adult, and hypertrophic scar tissues, while under the same experimental conditions, it increases the expression of MMP-1. Possible involvement of MTX-induced extracellular signal-regulated kinase 1/2 (ERK1/2) pathway in MMP-1 production. Activation of ERK1/2 pathway plays an important role in MTX-induced MMP-1 expression in primary human dermal fibroblasts
metabolism
the expression profiles of multiple and possibly redundant matrix-remodeling proteases (e.g., collagenases) differ strongly in health, disease, and development. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes
metabolism
the expression profiles of multiple and possibly redundant matrix-remodeling proteases (e.g., collagenases) differ strongly in health, disease, and development. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes
metabolism
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matrix metalloproteinase 1 and collagens play a key role in platelet-derived growth factor (PDGF) and stromal cell-derived factor-1 (SDF-1) promotion of the skin wound repairing effect of bone mesenchymal stem cells. Bone marrow mesenchymal stem cells (BMSCs) are applied to treatment of skin wounds. PDGF treatment recruits BSMCs to injured sites and strengthens the effect of BMSCs on skin wound by suppressing activity of MMP-1. SDF-1 treatment increases the treating effect of BMSCs on skin injury through the deposition of collagen I and collagen III. Phenotypes, overview
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physiological function
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both plasma and mucosal levels of MMP-1 and TIMP-1 are independently correlated with ulcerative colitis, overview
physiological function
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increased expression of MMPs by toll-like receptor activation may be involved in infection-associated inflammation, cell migration and tissue remodelling in human skin
physiological function
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lithium-induced MMP-1 may participate in the reinforcement of endothelial cell senescence revealing a novel mechanism for lithium-induced tissue remodeling
physiological function
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lithium-induced MMP-1 may participate in the reinforcement of endothelial cell senescence revealing a novel mechanism for lithium-induced tissue remodeling
physiological function
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matrix metalloproteinase-1 degrades the extracellular matrix and is implicated in tuberculosis-driven tissue destruction, signaling pathways regulating macrophage MMP-1 in human pulmonary tuberculosis, overview
physiological function
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matrix metalloproteinases and the tissue inhibitors of MMPs, TIMPs, play a pivotal role in matrix remodeling following myocardial infarction, the MMPs/TIMP-1 balance is perturbed after myocardial infarction. Oral valsartan, but not PD123319 limits infarct size, normalized MMPs/TIMP-1 balance and restores FN level
physiological function
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matrix metalloproteinases play a pivotal role in tissue remodeling and destruction in inflammation-associated diseases such as cardiovascular disease and periodontal disease
physiological function
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MMP-1 is a zinc-dependent endopeptidase capable of degrading all components of the extracellular matrix
physiological function
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MMP-1 is implicated in the degradation of human skin matrix proteins such as collagen and other components of extracellular matrix
physiological function
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MMP-1 is increased in inflammatory conditions leading to destruction of extracellular matrix
physiological function
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MMP-1 is involved in in inflammatory atherosclerotic lesions and is known to be implicated in the vascular remodeling events preceding plaque rupture, the most common cause of acute myocardial infarction
physiological function
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MMP-1 is involved in spontaneous resorption of disc herniation after sciatica, overview. MMP-3 appears to play a greater role than MMP-1 in disc herniation resorption
physiological function
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MMP-1 or interstitial collagenase unwinds native type I collagen and initiate its degradation
physiological function
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MMP-1 promotes osteoclastic bone resorption and bone metastases, the breast cancer cell produced MMP-1 is involved in the activation of the epidermal growth factor ligands that activate NF-kappaB ligand RANKL, via its central osteoclastogenic pathway receptor activator, to promote breast cancer osteolysis, molecular mechanism, overview
physiological function
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proteasome inhibition, e.g. by inhibitor bortezomib, in vitro decreases type I collagen and enhances MMP-1 production by human fibroblasts, thus favoring an antifibrotic fibroblast phenotype. These effects are dominant over the pro-fibrotic phenotype induced by transforming growth factor-beta
physiological function
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role for MMP-1 in the TGF-beta- and EGF-stimulated collagen remodeling process
physiological function
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throughout the process of invading and remodelling spiral arteries, extracellular matrix must be broken down and matrix metalloproteinases are major participants in this disintegration
physiological function
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transfection of a plasmid expression of MMP-1 into myocard after infarction increases myocyte shortening and reduces Na+-Ca2+ exchange current, it decreases myocardial fibrosis and improves cardiac remodeling and function
physiological function
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MT1-MMP is identified as the dominant and direct-acting protease responsible for the type I collagenolytic activity mediated by both mouse and human pulmonary fibroblasts. MT1-MMP is shown to be essential for pulmonary fibroblast migration within three-dimensional (3-D) hydrogels of cross-linked type I collagen that recapitulate ECM barriers encountered in the in vivo environment
physiological function
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MT1-MMP is identified as the dominant and direct-acting protease responsible for the type I collagenolytic activity mediated by both mouse and human pulmonary fibroblasts. MT1-MMP is shown to be essential for pulmonary fibroblast migration within three-dimensional (3-D) hydrogels of cross-linked type I collagen that recapitulate ECM barriers encountered in the in vivo environment
physiological function
MMP-1 is one of the key regulators of the overall quantity of type I procollagen deposited by fibroblasts during scar formation. It increases collagen degradation in the extracellular matrix (ECM)
physiological function
the protease drives morphological, biochemical, and viscoelastic changes in the extracellular matrix (ECM) leading to unique ECM-cell crosstalk, complexity and selectivity of collagenase-associated degradation mechanisms during tissue remodeling. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes. Specific influences of the highly abundant collagenases on fibroblast-ECM crosstalk, overview
physiological function
the protease drives morphological, biochemical, and viscoelastic changes in the extracellular matrix (ECM) leading to unique ECM-cell crosstalk, complexity and selectivity of collagenase-associated degradation mechanisms during tissue remodeling. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes. Specific influences of the highly abundant collagenases on fibroblast-ECM crosstalk, overview
additional information
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c-Jun is a key subunit of AP-1 known to be essential for MMP-1 transcription
additional information
genetic variants of a common functional polymorphism in the matrix metalloproteinase-1 gene promoter do not account for the itchy skin phenotype in epidermolysis bullosa
additional information
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Rac1 signaling results in accumulation of type I collagen due to decreased collagenase activity, overview
additional information
ability of MMP-1 to unwind triple-helical collagen, collagenolytic matrix metalloproteinase structure-function relationships, molecular dynamics studies, overview. Conformational selection mechanism for collagenolysis with full-length MMPs. Dynamic crosscorrelation analysis of MMP-1 with THP, modelling. Molecular dynamics simulations are utilized to dock MMP-1 with the cleavage site region in type III collagen
additional information
although collagenolytic matrix metalloproteinases (MMPs) possess common domain organizations, there are subtle differences in their processing of collagenous triple-helical substrates
additional information
detection of collagen deposition and MMP-1 secretion in rat-1 fibroblasts, macrorheological properties and morphologies of natural and MMP-degraded ECMs