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MT1-MMP plays a crucial role in RAGE-activated NADPH oxidase-dependent signaling pathways.
MMP-1 was involved in osteoarthritis development in rabbit ACLT model and the amount of its expression was related with the degree of cartilage degradation.
Converting a broad matrix metalloproteinase family inhibitor into a specific inhibitor of MMP-9 and MMP-14.
High expression of MMP14 is associated with Colorectal Cancer.
Study shows that modulation of matrix pore size or of lamin A expression known to modulate nuclear stiffness directly impinges on levels of MT1-MMP-mediated pericellular collagenolysis by cancer cells. This response requires an intact connection between the nucleus and the centrosome via the linker of nucleoskeleton and cytoskeleton (LINC) complex protein nesprin-2 and dynein adaptor Lis1.
Melatonin disturbs SUMOylation-mediated crosstalk between c-Myc and nestin via MT1 activation and promotes the sensitivity of paclitaxel in brain cancer stem cells
The results suggest that MMP-14 is involved in proliferative diabetic retinopathy angiogenesis.
MMP14 down-regulated the expression of TNF-alpha to inhibit extracellular matrix and MMP14 down-regulation was found to impair the proliferation and invasion ability of cervical cancer cells.
High expression of mmp14 is associated with preeclampsia.
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, MMP14 and GRP78 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.
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 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 and p53, demonstrating that the tumor microenvironment directly stimulates molecular changes in cancer cells to drive an invasive phenotype
cytomembrane MMP14 was induced by IL-6 secreted from astrocytes, thereby enhancing the migration and invasion of glioma cells through activation of MMP2
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 and increases S100A9 levels in lung tissue. * MMP-14 ameliorates inflammation by promoting S100A9 cleavage by activated MMP-2.
In turn, LIMK1 and LIMK2 are required for MT1-MMP-dependent matrix degradation and cell invasion in a three-dimensional type I collagen environment.
miR-337-3p directly binds to the MMP-14 promoter to repress MZF1-facilitatd MMP-14 expression, thus suppressing the progression of gastric cancer
CCN3 (Nov) and CCN5 (WISP2) are novel substrates of MMP14.
The current data support MT1-MMP as an additional ILK substrate and show that modulation of ILK expression and activity inhibit MT1-MMP-related pro-metastatic behaviors of ovarian cancer cells.
results suggest that ET-1-induced activation of proMMP-2 is mediated via cross-talk between NADPH oxidase-PKCalpha-p(38)MAPK and NFkappaB-MT1MMP signaling pathways along with a marked decrease in TIMP-2 expression in the cells
Data indicate the involvement of PKC-alpha in proMMP-2 activation and inhibition of TIMP-2 expression by NF-kappaB-MT1-MMP-dependent and -independent pathway.
Data suggest that EMMPRIN derived from endometrial epithelial cells regulates expression of matrix metalloproteinases (MMP-2; MMP-14) in endometrial stromal cells; expression of stromal MMPs is significantly higher in coculture with epithelial cells.
MMP-14, MMP-2 and TIMP-2 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, MMP14, and the metallopeptidase inhibitor TIMP2 between different phases of the estrous cycle indicating an endocrine regulation.
EMMPRIN from the luminal epithelium may regulate the expression of stromal MMP-2 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
MMP14 is a new member of the intricate gene network activated in osteocytes by PTH1R signaling that can be targeted to adjust the skeletal responses to PTH in favor of bone preservation.
MT1-MMP expressed by vascular smooth muscle cells plays a key role in limiting the progression of atherosclerosis in APOE-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 associates with MMP14 through potential phosphorylation residues within its intracellular domain, and that CAIX 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 in regulating mammary gland adipocyte differentiation. Whereas MMP14 promotes the generation of white fat depots crucial for energy storage, MMP15 differentially controls the formation of thermogenic brown fat.
The authors identified the membrane-tethered matrix metalloprotease 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 on lymphatic endothelial cells to inhibit LYVE-1-mediated lymphangiogenic responses and restrains the production of VEGF-C.
The authors propose a model for cell-regulated collagen fibril assembly during tendon development in which MMP14 cleaves a molecular bridge tethering collagen fibrils to the plasma membrane of fibripositors.
We demonstrate that MMP-14-mediated signaling in fetal hepatic progenitor cells promotes biliary luminal formation around the portal vein and negatively controls the maturation of hepatocytes.
Results show a reciprocal association between levels of heparanase and MMP14, a membrane-bound MMP, shedding light on how branching occurs within developing mammary glands.
MT1-MMP proteolytic activity is required for maintaining cell integrity, loss of MT1-MMP causes cell senescence and nuclear defects.
of the transcripts of tissue inhibitors of matrix metalloproteinases (TIMPs) showed that expression of both TIMP1 and TIMP2 correlates negatively with the invasive potential of cells.
Angiotensin II suppresses RECK, but induces matrix metalloproteinases both in vivo and in vitro.
Active MT1-MMP promotes Notch1 cleavage independently of ADAM10 or -17.
LV mass was similar among WT, MT1-MMP overexpression, and MT1-MMP reduced expression after PO, significant differences in LV function.
In the kidneys of Sirt1(endo-/-) mice, impaired angiogenesis, reduced matrilytic activity, and retention of the profibrotic cleavage substrates tissue transglutaminase and endoglin accompanied MMP-14 suppression.
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 as critical events in neointimal hyperplasia after vascular injury.
Induction of endogenous MMP-14 gene and coexpression of SAF-1 & MMP-14 in the macrophages present in the atherosclerotic plaque implicate SAF-1 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.
Data indicate Mmp14a-dependent retinal defects lead to microphthalmia; Mmp14b, on the contrary, does not appear to alter retinal neurogenesis.
VANGL2 regulates the endocytosis and cell-surface availability of MMP14 in a manner that is dependent on focal adhesion kinase.
Data suggest that the MT1-MMP-PTK7 axis plays an important role in normal embryogenesis.
MT-MMPalpha and beta were expressed through at least the first 72 h of development and this expression was targeted to the cell surface
Data show that Mmp14 is required for proper cell polarity underlying the directed migration of mesodermal cells during gastrulation, and identify a genetic interaction between mmp14 and non-canonical Wnt signaling.
MMP-14, located in the cytoplasm of normal lamellar basal cells, disappears during laminitis development; pathology of laminitis is associated with increased and lowered transcription of MMP-14 and TIMP-2, respectively
MMP14 is critical for neural crest EMT and migration, partially through regulating the levels of cadherins.
results suggest that MT1-MMP & gelatinase A function together in the ECM degradation or remodeling associated with metamorphosis & that MT1-MMP has additional gelatinase A-independent roles in the development of adult longitudinal muscle in the intestine.
coexpression of wild type MT1-MMP and GelA leads to a cooperative effect on embryonic development and this cooperative effect is abolished when the catalytic activity of either MMP is eliminated through a point mutation in the catalytic domain
metamorphic tail and intestine RNA levels of TIMP-2, MT1-MMP and Gel-A, but not MT3-MMP or TIMP-3, are elevated during periods of cell death and proliferation
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.
, MT-MMP 1
, matrix metallopeptidase 1 (interstitial collagenase)
, matrix metalloproteinase 14
, matrix metalloproteinase-14
, membrane type 1 metalloproteinase
, membrane-type matrix metalloproteinase 1
, membrane-type-1 matrix metalloproteinase
, membrane type 1 metalloprotease
, matrix metalloproteinase 14 (membrane-inserted)
, matrix metalloproteinase 14 preproprotein
, membrane type-1 metalloproteinase
, matric metalloproteinase 14
, Membrane type 1-MMP
, type 1 matrix metalloprotease 14
, matrix metalloproteinase 14 membrane-inserted
, matrix metalloproteinase 14, membrane-inserted
, membrane type 1-matrix metalloproteinase
, membrane-type 1 matrix metalloproteinase
, matrix metalloproteinase 14 (membrane-inserted) alpha
, matrix metalloproteinase 14a (membrane-inserted)
, matrix metallopeptidase 14 (membrane-inserted)
, matrix metallopeptidase 14 L homeolog
, membrane type-1 matrix metalloproteinase 14