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Study suggest that the downregulation of miR1505p and the overexpression of MMP14 may be deeply involved in the pathogenesis of lung squamous cell carcinoma.
the expression of three cytokines for the pathogenesis of osteoarthritis (OA). which include IL-1beta (zeige IL1B Proteine), MMP14 and GRP78 (zeige HSPA5 Proteine) was decreased by the various concentrations of icariin. These preliminary results imply that icariin might be an effective compound for the treatment of OA disease.
Overexpression of MMP-14 in familial amyloidotic polyneuropathy might be associated with the inflammatory process and can also contribute to further remodeling of the ECM (zeige MMRN1 Proteine).
MMP14 rs1042703 was associated with nominally shorter time to progression in malignant mesothelioma patients.
analysis of MT1-MMP structure and proteolytic activity
In squamous cell carcinoma of the cervix (SCCC), higher levels of MMP-14 expression were established in tumor cells, as evidenced by IHC (+3) and RT-PCR.Furin activity in the tumor was much higher than that in normal tissues. The expression of TIMP-2 (zeige TIMP2 Proteine) mRNA was sufficiently obvious in both the tumor and normal tissues to the bottom of the uterine cavity.
MMP-14 is regulated by a cascade of IL-6 (zeige IL6 Proteine) and p53 (zeige TP53 Proteine), demonstrating that the tumor microenvironment directly stimulates molecular changes in cancer cells to drive an invasive phenotype
cytomembrane MMP14 was induced by IL-6 (zeige IL6 Proteine) secreted from astrocytes, thereby enhancing the migration and invasion of glioma cells through activation of MMP2 (zeige MMP2 Proteine)
MMP-14 levels decrease in lungs from endotoxemic mice and serum from septic patients. * Mmp14 (-/-) mice show increased lung injury and mortality following endotoxemia. * Absence of Mmp14 decreases activated MMP-2 (zeige MMP2 Proteine) and increases S100A9 (zeige S100A9 Proteine) levels in lung tissue. * MMP-14 ameliorates inflammation by promoting S100A9 (zeige S100A9 Proteine) cleavage by activated MMP-2 (zeige MMP2 Proteine).
In turn, LIMK1 (zeige LIMK1 Proteine) and LIMK2 (zeige LIMK2 Proteine) are required for MT1-MMP-dependent matrix degradation and cell invasion in a three-dimensional type I collagen environment.
MT1-MMP expressed by vascular smooth muscle cells plays a key role in limiting the progression of atherosclerosis in APOE (zeige APOE Proteine)-null mice by regulating proliferative responses and inhibiting the deterioration of VSMC function in atherogenic vascular walls.
Study documents that MT1-MMP is widely expressed in the tooth and surrounding connective tissues during development and postnatal growth. Consistent with this expression, loss of MT1-MMP in mice impairs tooth root formation and eruption in association with multiple defects in dentoalveolar tissues.
Authors demonstrate that CAIX (zeige CA9 Proteine) associates with MMP14 through potential phosphorylation residues within its intracellular domain, and that CAIX (zeige CA9 Proteine) enhances MMP14-mediated collagen degradation by directly contributing hydrogen ions required for MMP14 catalytic activity.
High mmp14 expression is associated with Lung Metastasis of Breast Cancer.
Although neither proteinase is required for branching morphogenesis, transcriptome profiling reveals a key role for MMP14 and MMP15 (zeige MMP15 Proteine) in regulating mammary gland adipocyte differentiation. Whereas MMP14 promotes the generation of white fat depots crucial for energy storage, MMP15 (zeige MMP15 Proteine) differentially controls the formation of thermogenic brown fat.
The authors identified the membrane-tethered matrix metalloprotease (zeige ADAMTS7 Proteine) MT1-MMP as a prominent host-extracellular matrix-remodeling collagenase in influenza infection.
MMP-14 expression in fibroblasts plays a crucial role in collagen remodeling in adult skin and largely contributes to dermal homeostasis underlying its pathogenic role in fibrotic skin disease in a mouse model
MT1-MMP directly cleaves LYVE-1 (zeige LYVE1 Proteine) on lymphatic endothelial cells to inhibit LYVE-1 (zeige LYVE1 Proteine)-mediated lymphangiogenic responses and restrains the production of VEGF-C (zeige VEGFC Proteine).
results suggest that ET-1 (zeige EDN1 Proteine)-induced activation of proMMP-2 is mediated via cross-talk between NADPH oxidase (zeige NOX1 Proteine)-PKCalpha (zeige PKCa Proteine)-p(38)MAPK (zeige MAPK1 Proteine) and NFkappaB-MT1MMP signaling pathways along with a marked decrease in TIMP-2 (zeige TIMP2 Proteine) expression in the cells
Data indicate the involvement of PKC-alpha (zeige PKCa Proteine) in proMMP-2 activation and inhibition of TIMP-2 (zeige TIMP2 Proteine) expression by NF-kappaB (zeige NFKB1 Proteine)-MT1-MMP-dependent and -independent pathway.
Data suggest that EMMPRIN derived from endometrial epithelial cells regulates expression of matrix metalloproteinases (MMP-2 (zeige MMP2 Proteine); MMP-14) in endometrial stromal cells; expression of stromal MMPs is significantly higher in coculture with epithelial cells.
MMP-14, MMP-2 (zeige MMP2 Proteine) and TIMP-2 (zeige TIMP2 Proteine) are co-localized in the fetal compartment and therefore could influence the timely release of fetal membranes in cattle.
Results describe distinct changes in expression of MMP2 (zeige MMP2 Proteine), MMP14, and the metallopeptidase (zeige ECEL1 Proteine) inhibitor TIMP2 (zeige TIMP2 Proteine) between different phases of the estrous cycle indicating an endocrine regulation.
EMMPRIN from the luminal epithelium may regulate the expression of stromal MMP-2 (zeige MMP2 Proteine) and MMP-14 suggesting a role in adhesion and fusion of embryo to luminal epithelium.
MT1-MMP seems to act by inducing tissue remodeling in cartilage
sphingosine 1-phosphate is the predominant serum factor essential for MT1-MMP-dependent migration and morphogenic differentiation of vascular endothelial cells
MT1-MMP plays a crucial role in RAGE (zeige AGER Proteine)-activated NADPH oxidase (zeige NOX1 Proteine)-dependent signaling pathways.
MMP-1 (zeige MMP1 Proteine) was involved in osteoarthritis development in rabbit ACLT model and the amount of its expression was related with the degree of cartilage degradation.
Modulation of MT1-MMP activity and microRNA-133a exportation into the myocardial interstitium occurred in the setting of acute myocardial ischemia-reperfusion.
A heterogeneous response in MT1-MMP activity likely contributes to regional dysfunction with ischemia-reperfusion. Subsequent I/R activates a proteolytic cascade within the MI region, contributing to continued adverse remodeling.
PI3K-dependent regulation of MT1-MMP protein synthesis and subsequent activation of latent MMP-2 (zeige MMP2 Proteine) as critical events in neointimal hyperplasia after vascular injury.
Induction of endogenous MMP-14 gene and coexpression of SAF-1 (zeige MAZ Proteine) & MMP-14 in the macrophages present in the atherosclerotic plaque implicate SAF-1 (zeige MAZ Proteine) as a key regulator of MMP-14 gene induction in macrophage cells.
In an isolated left ventricular myocyte ischemia/reperfusion model, hypoxia induced a >70% increase in MT1-MMP abundance in myocytes. Confocal microscopy revealed MT1-MMP internalization during this time & reemergence to the membrane with reperfusion.
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 protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily\; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 protein, and this activity may be involved in tumor invasion.
matric metalloproteinase 14
, matrix metalloproteinase-14
, membrane type 1 metalloprotease
, membrane-type-1 matrix metalloproteinase
, MT-MMP 1
, Membrane type 1-MMP
, matrix metalloproteinase 14 (membrane-inserted)
, membrane-type matrix metalloproteinase 1
, type 1 matrix metalloprotease 14
, matrix metalloproteinase 14 membrane-inserted
, matrix metalloproteinase 14, membrane-inserted
, membrane type 1-matrix metalloproteinase
, matrix metalloproteinase 14 preproprotein
, matrix metallopeptidase 1 (interstitial collagenase)
, matrix metalloproteinase 14
, membrane type 1 metalloproteinase
, membrane-type 1 matrix metalloproteinase
, membrane type-1 metalloproteinase