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The current data support MT1-MMP as an additional ILK (show ILK Proteins) substrate and show that modulation of ILK (show ILK Proteins) expression and activity inhibit MT1-MMP-related pro-metastatic behaviors of ovarian cancer cells.
Kinase activation led to increased MMP-2 (show MMP2 Proteins) and MT1-MMP expression and melanoma cell migration induced by hHK-1 (show HOOK1 Proteins). Thus, hHK-1 (show HOOK1 Proteins) and the NK1 receptor (show TACR1 Proteins) are critical to melanoma cell migration and each may be a promising chemotherapeutic target
Endoplasmic reticulum (ER) glycosylation of MMP14 is required for ECM (show MMRN1 Proteins) degradation and tumor growth.
Authors demonstrate that CAIX (show CA9 Proteins) associates with MMP14 through potential phosphorylation residues within its intracellular domain, and that CAIX (show CA9 Proteins) enhances MMP14-mediated collagen degradation by directly contributing hydrogen ions required for MMP14 catalytic activity.
developed a GNP-based, near-infrared fluorescent contrast agent that is highly specific for MMP-14 detection in breast tumor cell lines.
ERO1alpha plays a crucial role in HSC (show FUT1 Proteins) proliferation via posttranslational modification of collagen and MT1-MMP
MT1-MMP-expressing cells induced co-cultured non-MT1-MMP-expressing cells.
The mechanism of transition from nondifferentiated to differentiated states in HepaRG cells was studied by proteomics. Two key factors (MMP-14 and OCLN (show OCLN Proteins)) were validated by qRT-PCR and Western blot. Blockade of MMP-14 further demonstrated its important function during tumor cell migration.
Data suggest that phosphorylation of Thr567 in cytoplasmic tail of MT1-MMP (MMP14) influences behavior of both individual ovarian cancer cells and multicellular aggregates; tumor cells expressing MT1-MMP-T567E phosphomimetic mutant exhibit enhanced cell migration and enhanced cell adhesion to peritoneum and other biological surfaces.
MMP-14 Is a novel substrate for matriptase (show ST14 Proteins), which regulates the levels of MMP-14 on the cell surface. High levels of matriptase (show ST14 Proteins) in alpha-1 antitrypsin (show SERPINA1 Proteins) deficiency may contribute to increased extracellular matrix degradation by alveolar macrophages both directly and through MMP-14 activation.
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.
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 (show MMP15 Proteins) in regulating mammary gland adipocyte differentiation. Whereas MMP14 promotes the generation of white fat depots crucial for energy storage, MMP15 (show MMP15 Proteins) differentially controls the formation of thermogenic brown fat.
The authors identified the membrane-tethered matrix metalloprotease (show ADAMTS7 Proteins) 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 (show LYVE1 Proteins) on lymphatic endothelial cells to inhibit LYVE-1 (show LYVE1 Proteins)-mediated lymphangiogenic responses and restrains the production of VEGF-C (show VEGFC Proteins).
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 (show HPSE Proteins) and MMP14, a membrane-bound MMP, shedding light on how branching occurs within developing mammary glands.
results suggest that ET-1 (show EDN1 Proteins)-induced activation of proMMP-2 is mediated via cross-talk between NADPH oxidase (show NOX1 Proteins)-PKCalpha (show PKCa Proteins)-p(38)MAPK (show MAPK1 Proteins) and NFkappaB-MT1MMP signaling pathways along with a marked decrease in TIMP-2 (show TIMP2 Proteins) expression in the cells
Data indicate the involvement of PKC-alpha (show PKCa Proteins) in proMMP-2 activation and inhibition of TIMP-2 (show TIMP2 Proteins) expression by NF-kappaB (show NFKB1 Proteins)-MT1-MMP-dependent and -independent pathway.
Data suggest that EMMPRIN derived from endometrial epithelial cells regulates expression of matrix metalloproteinases (MMP-2 (show MMP2 Proteins); MMP-14) in endometrial stromal cells; expression of stromal MMPs is significantly higher in coculture with epithelial cells.
MMP-14, MMP-2 (show MMP2 Proteins) and TIMP-2 (show TIMP2 Proteins) 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 (show MMP2 Proteins), MMP14, and the metallopeptidase (show ECEL1 Proteins) inhibitor TIMP2 (show TIMP2 Proteins) between different phases of the estrous cycle indicating an endocrine regulation.
EMMPRIN from the luminal epithelium may regulate the expression of stromal MMP-2 (show MMP2 Proteins) 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 (show AGER Proteins)-activated NADPH oxidase (show NOX1 Proteins)-dependent signaling pathways.
MMP-1 (show MMP1 Proteins) 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 (show MMP2 Proteins) as critical events in neointimal hyperplasia after vascular injury.
Induction of endogenous MMP-14 gene and coexpression of SAF-1 (show MAZ Proteins) & MMP-14 in the macrophages present in the atherosclerotic plaque implicate SAF-1 (show MAZ Proteins) 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