抗Human MMP14 抗体:
抗Mouse (Murine) MMP14 抗体:
抗Rat (Rattus) MMP14 抗体:
Human Polyclonal MMP14 Primary Antibody for WB - ABIN3043408
Jin, Jiang, Yang, Zhang, Yang, Zhang, Li, Yang, Ma: Acipimox attenuates atherosclerosis and enhances plaque stability in ApoE-deficient mice fed a palmitate-rich diet. in Biochemical and biophysical research communications 2012
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Human Polyclonal MMP14 Primary Antibody for IHC (p), WB - ABIN3044302
Jiang, Jin, Li, Zhang, Yang, Yang, Li, Yang, Ma: Intermittent hypobaric hypoxia promotes atherosclerotic plaque instability in ApoE-deficient mice. in High altitude medicine & biology 2013
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Human Monoclonal MMP14 Primary Antibody for CyTOF, FACS - ABIN4899219
Mierke, Bretz, Altevogt: Contractile forces contribute to increased glycosylphosphatidylinositol-anchored receptor CD24-facilitated cancer cell invasion. in The Journal of biological chemistry 2011
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Human Monoclonal MMP14 Primary Antibody for FACS - ABIN4895756
Loskutov, Kozyulina, Kozyreva, Ice, Jones, Roston, Smolkin, Ivanov, Wysolmerski, Pugacheva: NEDD9/Arf6-dependent endocytic trafficking of matrix metalloproteinase 14: a novel mechanism for blocking mesenchymal cell invasion and metastasis of breast cancer. in Oncogene 2015
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Human Polyclonal MMP14 Primary Antibody for CyTOF, FACS - ABIN4900817
Gkantidis, Blumer, Katsaros, Graf, Chiquet: Site-specific expression of gelatinolytic activity during morphogenesis of the secondary palate in the mouse embryo. in PLoS ONE 2012
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Human Polyclonal MMP14 Primary Antibody for IHC - ABIN6711837
Xu, Wang: miR‑133a suppresses cell proliferation, migration and invasion in human lung cancer by targeting MMP‑14. in Oncology reports 2014
Human Monoclonal MMP14 Primary Antibody for FACS - ABIN4895758
Sathyamoorthy, Tezera, Walker, Brilha, Saraiva, Mauri, Wilkinson, Friedland, Elkington: Membrane Type 1 Matrix Metalloproteinase Regulates Monocyte Migration and Collagen Destruction in Tuberculosis. in Journal of immunology (Baltimore, Md. : 1950) 2015
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.
MMP-14 aggravated the onset of severe preeclampsia by mediating sEng release.
Data show that MT1-MMP regulates an outside-in DNA Damage Response (DDR) through the modulation of integrinbeta1.
Pancreatic tumor cell metastasis is restricted by MT1-MMP binding protein MTCBP-1.
PROX1 is a transcriptional regulator of MMP14
This MMP14 biosensor promises to serve as a tool for the advancement of a broad range of investigations targeting MMP14 activity during cell migration in health and disease
down-regulation of KIF2A can inhibit gastric cancer cell invasion by suppressing MT1-MMP
MT1MMP was overexpressed in gastric carcinoma cells, and silencing of MT1MMP inhibited the proliferation and invasion of cells via regulating the expression of vimentin and Ecadherin.
it was demonstrated recently that lumican interacts directly with the catalytic domain of MMP-14 and inhibits its activity. The aim of this review was to summarize the interactions between SLRPs and MMPs with a special interest to lumican.
irected receptor recycling is used by cancer cells to achieve invasive migration. Accordingly, abrogating HRS- and actin-dependent MT1-MMP recycling results in defective matrix degradation and invasion of triple-negative breast cancer cells.
miR5845p also inhibited the expression of MMP4 and Slug, which are involved in tumor invasion and metastasis. Taken together, these results indicated that the miR5845p/MMP14 axis may serve as an anticancer target in the treatment of nonsmallcell lung cancer patients.
that MMP-14 enhances the invasive ability of SW982 cells by inducing epithelial-to-mesenchymal transition
This study indicates for the first time that high serum soluble MMP-14 levels in gastric cancer serves as a marker for a poor prognosis, possibly indicating the presence of distant metastases.
SNPs (rs2236302) exhibit a significant association with increased risk of steroid-induced femur head osteonecrosis in the population of northern China.
These data demonstrate that miR-584-3p directly targets the MMP-14 promoter to repress YY1-facilitated MMP-14 expression and inhibits the progression of gastric cancer.
Functional analysis demonstrated that this mutation, in contrast to previously reported human and murine MMP14 mutations, does not affect MMP14's transport to the cell membrane. Instead, it partially impairs MMP14's proteolytic activity. This residual activity likely accounts for the mitigated phenotype observed in our patients
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.
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
cells other than osteoclasts can cause focal bone destruction in inflammatory bone disease and suggest that MMP14 is a key mediator conferring pathological bone-resorbing capacity on c-Fos-deficient Sh3bp2(knock in (KI)/KI) macrophages.
High MMP14 expression is associated with melanoma metastasis and invasion.
MMP-14 is active in late stage tumors and is predominantly associated with stromal cell populations that have been activated by specific signaling molecules (e.g., TGFbeta) produced by tumor 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.
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.
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.
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.
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.
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.
Based on our observations as well as previously published data, we hypothesize that MMP14's catalytic activity is the prime determinant of disease severity. Given the limitations of our in vitro assays in addressing the consequences of MMP14 dysfunction, we generated a novel mmp14a/b knockout zebrafish model
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