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Human MMP 9 Protein expressed in Human Cells - ABIN2002581
Opdenakker, Van den Steen, Dubois, Nelissen, Van Coillie, Masure, Proost, Van Damme: Gelatinase B functions as regulator and effector in leukocyte biology. in Journal of leukocyte biology 2001
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Rat (Rattus) MMP 9 Protein expressed in Human Cells - ABIN3218785
Belotti, Paganoni, Manenti, Garofalo, Marchini, Taraboletti, Giavazzi: Matrix metalloproteinases (MMP9 and MMP2) induce the release of vascular endothelial growth factor (VEGF) by ovarian carcinoma cells: implications for ascites formation. in Cancer research 2003
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Our findings indicate that overexpression of MMP-9 rescued insulin (zeige INS Proteine) survival signaling in vitro and in early stages in the 5XFAD model of AD.
Review/Meta-analysis: Matrix metalloproteinase-9 has high predictive value for hemorrhagic transformation after acute ischemic stroke.
In dilation cardiomyopathy, expression of MMP-2 (zeige MMP2 Proteine), MMP-9, and TIMP-1 (zeige TIMP1 Proteine) and their ratios in autopsy material and in cultures was elevated by 1.5-9 times.
The expression of MMP-9 is associated with clinical outcome in chondrosarcoma.
OSM (zeige OSM Proteine) [oncostatin M (zeige OSM Proteine)]might be involved in the invasiveness of extravillous trophoblasts under hypoxia conditions via increasing MMP-2 (zeige MMP2 Proteine) and MMP-9 enzymatic activities through STAT3 (zeige STAT3 Proteine) signaling. Increased MMP-9 activity by OSM (zeige OSM Proteine) seems to be more important in primary trophoblasts.
MMP-9 levels in the tumor tissue extracts had also increased significantly
MMP-9 -1562 C/T polymorphism might be related to the digestive cancer susceptibility [meta-analysis]
MMP-9 protein overexpression was found in prostate cancers, low expression in any of the normal tissues or in benign prostatic tissue
Hypoxia promotes retinoblastoma cell line HXO-RB44 invasion by activating HIF-1alpha (zeige HIF1A Proteine)/MMP9 signaling pathway.
There was no difference found in MMP-2 (zeige MMP2 Proteine), MMP-9 or TLR-4 (zeige TLR4 Proteine) levels between non-thrombocytopenic and thrombocytopenic septic donors. PLA formation was increased in thrombocytopenic patients.
In the initial periods of AP progression, an increased expression of MMP9 in the TLR2 KO and MyD88 (zeige MYD88 Proteine) KO mice was observed. In the final periods of AP progression, a reduction of MMP2 (zeige MMP2 Proteine) expression and an increase of MMP9 expression in the TLR2 KO mice were observed. MMP2 (zeige MMP2 Proteine) and MMP9 production was modulated for TLR2 and MyD88 (zeige MYD88 Proteine) during apical periodontitis progression
Our data suggest that MMP-9 deficiency does not result in major abnormalities in the development of any conventionally selected or agonist selected subsets and does not interfere with thymocyte apoptosis and clearance, and that MMP-9 expression is not induced in immature T cells at any stage of their thymic development.
analysis of Foxn1 (zeige FOXN2 Proteine) and Mmp-9 expression in the intact and postinjured skin of young, adult, and old C57BL/6J and transgenic Foxn1 (zeige FOXN2 Proteine)::Egfp mice
Diet and exercise affect atheromatous MMP2/9 activity by modulating the systemic inflammatory milieu, with sVCAM-1, resistin, and adiponectin closely interacting with each other and with visceral fat.
Myocardial MMP-9 inhibition prevents ventricular arrhythmia through pleiotropic effects, including the modulation of calcium homeostasis and reduced calcium leakage.
results first identified the role of SNX10 (zeige SNX10 Proteine) in MMP9 trafficking and secretion, and provided an evidence for SNX10 (zeige SNX10 Proteine) as a possible therapeutic target for bone destructing disease.
Thus, the light reintroduction-induced increase in MMP-9 removes constraints on structural and functional plasticity in the mature cortex.
the ZnT3 (zeige Slc30a3 Proteine) null state removed synaptic zinc, it rather increased free zinc in the cytosol of brain cells, which appeared to increase MMP-9 activity and BDNF (zeige BDNF Proteine) levels. The present results suggest that zinc dyshomeostasis during the critical period of brain development may be a possible contributing mechanism for ASD (zeige GUSB Proteine).
MMP-9 activation by hypoxia requires LRP1 (zeige LRP1 Proteine) and Pyk2 (zeige PTK2B Proteine) phosphorylation in fibroblasts.
Aneurysmal-prone factors induced HIF-1alpha (zeige HIF1A Proteine) can cause overexpression of MMP-2 (zeige MMP2 Proteine) and MMP-9 and promote aneurysmal progression.
Results provide evidence for the utility of MMP9 and TIMP1 (zeige TIMP1 Proteine) as markers of age- and lactocrine-sensitive porcine female reproductive tract development.
Increased MMP-9 expression is associated with carotid atherosclerotic plaque.
Increased expression of MMP-9 is associated with intraplaque hemorrhage in a swine model of vulnerable carotid atherosclerosis
we demonstrated the presence of high molecular weight (HMW) complexes (130, 170, and 220 kDa) containing MMP9, TIMP1 (zeige TIMP1 Proteine), and NGAL (zeige LCN2 Proteine) (also MMP2 (zeige MMP2 Proteine) in 220 kDa complex) without proteolytic activity.
Data demonstrate for the first time that MMP2 (zeige MMP2 Proteine) and MMP9 are expressed in swine ovarian follicle both in theca and granulosa layers.
FiO2 used for resuscitation affects matrix metalloproteinases MMP-9 and MMP-2 (zeige MMP2 Proteine), caspase-3 (zeige CASP3 Proteine) and BDNF (zeige BDNF Proteine)
Oxygen for newborn resuscitation increases MMP-2 (zeige MMP2 Proteine)/-9 activity resulting in tissue damage and influencing remodeling processes.
contribution of MMPs to the inflammatory breakdown of the blood-CSF (zeige CSF2 Proteine) barrier in vitro
The levels of matrix metalloproteinase-2 (zeige MMP2 Proteine) and matrix metalloproteinase-9 (MMP-9)in the corpus luteum of swine during luteolysis are reported.
Our data define pericyte interactions as a main inducer of endothelial MMP secretion and propose a new role for pericyte-endothelial cell crosstalk at the BBB in vitro
In diabetic retinopathy transcription of MMP-9 is regulated by AP-1 binding at both, proximal and distal sites of its promoter, and acetylation of c-Jun and c-Fos subunits is important in its regulation.
These data demonstrate that serum neutrophil haptoglobin (zeige HP Proteine)-MMP 9 complexes appear sooner and decline more rapidly than other acute phase proteins.
Activation of cytosolic MMP-9 and MMP-2 (zeige MMP2 Proteine) was investigated in the retinal endothelial cells incubated in high glucose for 6-96 h, and correlated with their mitochondrial accumulation and mitochondrial damage.
Role of TGF-beta1 (zeige TGFB1 Proteine) and TNF-alpha (zeige TNF Proteine) in IL-1beta (zeige IL1B Proteine) mediated activation of proMMP-9 in pulmonary artery smooth muscle cells: involvement of an aprotinin sensitive protease.
Decreased MMP-9 and increased TIMP-1 (zeige TIMP1 Proteine) expression were found in peripheral blood cells from Mycobacterium avium subsp. paratuberculosis (Map)-infected cattle after stimulation with Map lysate and Map purified protein derivative than in control cattle.
We used a trophoblast cell line (F3) derived from bovine placentomes to examine the influence of EGF (zeige EGF Proteine) on MMP-9 and TIMP-1 (zeige TIMP1 Proteine) expression by semiquantitative RT-PCR and MMP activity by zymography.
results suggest a significant role of matrix metalloproteinase-2 (zeige MMP2 Proteine) and-9 in growth and development of bovine follicle
Cells constitutively produced proMMP-9 and proMMP-2, and treatment with TNFalpha (zeige TNF Proteine), hepatocyte growth factor (zeige HGF Proteine), and 12-O-tetradecanoylphorbol 13-acetate resulted in significant increase in level of proMMP-9 but not in level of proMMP-2.
MMP-2 and MMP-9 production in blastocysts attached to the endometrial cells is regulated by TNF-alpha and TNF-beta
Results suggest that MMP-2 (zeige MMP2 Proteine), MMP-9, and TIMP-2 (zeige TIMP2 Proteine) mRNAs are expressed in bovine placentomes during the gestational and postpartum periods and that these enzymes, in conjunction with steroidogenic enzymes, mediate fetal membrane detachment after parturition.
Mmp9 is dispensable for Hematopoietic stem cells budding, and is required for proper colonization of secondary niches.
The findings of this study suggest that Mmp-9 is a protective molecule against infection by Listeria monocytogenes by engaging in migration of zebrafish macrophages to the site of infection via a non-proteolytic role.
elevated beta-oxidation-fuelled mitochondria-derived reactive oxygen species within epidermal cells helps guide matrix metalloproteinase-driven leukocyte recruitment.
Mmp9 regulates both acute and chronic tissue damage and plays an essential role in collagen reorganization during wound repair.
MeHg impairs tail development at least partially by activation of the tissue remodeling proteases Mmp9 and Mmp13 (zeige MMP13 Proteine).
study identified mechanism by which mycobacteria induce granulomas: ESAT-6 induced MMP9 in epithelial cells neighboring infected macrophages; MMP9 enhanced recruitment of macrophages, which contributed to nascent granuloma maturation & bacterial growth
From 24h post fertilization, mmp9 expression was detected in a population of circulating white blood cells.
expression and activity of MMP-2 (zeige MMP2 Proteine) and MMP-9 in the embryonic zebrafish.
The MMP-9 gene was duplicated and differentiated into two genes, one was specialized in a common ancestor of X. laevis and X. tropicalis expressed in degenerating and remodeling organs in response to thyroid hormone (zeige PTH Proteine) during metamorphosis.
MMP-9TH is responsible in the larval epithelial apoptosis through degrading ECM (zeige MMRN1 Proteine) components in the basal lamina, whereas MMP-9 is involved in the removal of dying epithelial cells during amphibian intestinal remodeling
metamorphic tail and intestine RNA levels of TIMP-2 (zeige TIMP2 Proteine), MT1-MMP (zeige MMP14 Proteine) and Gel-A, but not MT3-MMP (zeige MMP24 Proteine) or TIMP-3 (zeige TIMP3 Proteine), are elevated during periods of cell death and proliferation
Expression of MMP-9 increased after cerebral aneurysm induction, peaking at week 3, leading to reduced smooth muscle cell number, damaged endothelial cells, and damage to the aneurysm wall elastic layer.
Inflammatory factors such as TNF-alpha (zeige TNF Proteine) can stimulate MMP-2 (zeige MMP2 Proteine)/9 activity in corneal epithelium cells. This may be a potential manipulating mechanism of MMP expression in the pathogenesis of corneal diseases
Therefore, it was reasonable to speculate that the increased expression of VEGF (zeige VEGFA Proteine) and MMP-9 in residual hepatic tumor cells and tumor angiogenesis post-embolization would be responsible for the increased metastatic potentiality and invasiveness.
Performing minimally invasive surgical procedures in the early stages of intracerebral hemorrhage significantly decreases MMP-9.
Increased expression of MMP-9 in spinal cord follows cervical spondylotic myelopathy.
Hemoperfusion could obviously reduce oxidative stress and the expression levels of MMP-2 (zeige MMP2 Proteine), MMP-9 and TIMP-1 (zeige TIMP1 Proteine) in rabbits with acute paraquat poisoning.
In experimental syringomyelia, MMP-9 plays an important role in causing edema in the presyrinx state.
Tongxinluo can inhibit the expression of MMP-3 (zeige MMP3 Proteine) and 9 and increase the expression of PPARgamma (zeige PPARG Proteine) in atherosclerotic rabbits.
TGF-beta (zeige TGFB1 Proteine) mediated MMP-9 induction may be regulated by the NF-kappaB (zeige NFKB1 Proteine), Smad3 (zeige SMAD3 Proteine), and JNK (zeige MAPK8 Proteine) pathways, whereas the IL-1beta (zeige IL1B Proteine) mediated induction may be regulated by the NF-kappaB (zeige NFKB1 Proteine) and p38 (zeige MAPK14 Proteine) pathways.
The results showed that MMP-2 (zeige MMP2 Proteine), MMP-9, and StAR were significantly expressed in the granulosa and thecal cells of the ovarian atretic follicles during proestrus, and were strongly expressed in the corpus luteum during metestrus.
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. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.
92 kDa gelatinase
, 92 kDa type IV collagenase
, macrophage gelatinase
, matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
, matrix metalloproteinase-9
, type V collagenase
, 92kD gelatinase
, 92kD type IV collagenase
, 92kDa gelatinase
, 92kDa type IV collagenase
, Gel B
, collagenase type IVB
, gelatinase B
, matrix metalloproteinase 9
, 92-kDa type IV collagenase
, matrix metalloproteinase 9 (gelatinase B 92-kDa type IV collagenase)
, matrix metalloproteinase 9 (gelatinase B, 92-kDa type IV collagenase)
, type IV collagenase MMP-9
, Matrix metalloproteinase-9
, matrix metalloproteinase 9 (gelatinase B, 92kDa matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
, 75 kDa gelatinase