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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
Show all 5 Pubmed References
A MMP-9-cleaved OPN fragment, OPN-32kDa, was responsible for inducing expansion of myeloid-derived suppressor cells, which may contribute to 3LL tumor's evasion of the immune response.
animals were submitted to the evaluation of Blood-Brain Barrier permeability and MMP-2 (show MMP2 Proteins) and MMP-9 in striatum, hippocampus and cerebral cortex
p63alpha protein up-regulates heat shock protein 70 (show HSP70 Proteins) expression via E2F1 transcription factor (show E2F1 Proteins) 1 (show HNF1A Proteins), promoting Wasf3/Wave3 (show WASF3 Proteins)/MMP9 signaling and bladder cancer invasion
IL-33 (show IL33 Proteins)-induced MMP-9 expression in the mouse monocyte/macrophage line RAW264.7.
Cleavage of beta-DG still occurred when both MMP-2 (show MMP2 Proteins) and MMP-9 were knocked out in gamma - sarcoglycan (show SGCG Proteins)-deficient mice. The study found that up-regulation of MMP-14 (show MMP14 Proteins) is capable of cleaving beta-DG, and it may be involved in the pathogenesis of sarcoglycanopathy.
MMP-9's contribution to development of atherosclerotic lesions may be a direct stimulation of endothelial cells, and that PAR-1 (show MARK2 Proteins) may serve as a receptor for MMP-9.
Results show that ablation of systemic MMP-9 initiated fatal communication between maintenance of physiological functions of MMP-9 in the bone marrow and invasive growth of pancreatic ductal adenocarcinoma via the deregulation of IL6 (show IL6 Proteins).
MMP-9 mediates IL-17 (show IL17A Proteins)'s capacity to inhibit myoblast differentiation during inflammatory diseases
The MURC/Cavin-4 (show MURC Proteins) in vascular smooth muscle cells modulates abdominal aortic aneurysm (AAA (show AAAS Proteins)) progression at the early stage via the activation of JNK (show MAPK8 Proteins) and MMP-9. MURC/Cavin-4 (show MURC Proteins) is a potential therapeutic target against AAA (show AAAS Proteins) progression.
Study demonstrated evidence of beta-dystroglycan cleavage by matrix metalloproteinase-2 (show MMP2 Proteins)/-9 in permanent middle cerebral artery occlusion mouse brains; this cleavage was implicated in aquaporin-4 (show AQP4 Proteins) redistribution and brain edema in cerebral ischemia.
High mmp9 expression is associated with breast Cancer.
results suggest that MMP1 (show MMP1 Proteins)-1607 1G/2G, MMP3 (show MMP3 Proteins)-1171 5A/6A and MMP9-1562 C/T gene polymorphisms have synergistic effect on breast cancer. The interactions of MMPs clinical risk factors such as lymph node involvement has shown a strong correlation and might influence the 5-years survival rate, suggesting their potential role in the breast carcinogenesis
Ureaplasma spp. carry the protease necessary for PGP release, and PGP and MMP-9 are increased in amniotic fluid during Ureaplasma infection, suggesting Ureaplasma spp. induced collagen fragmentation contributes to preterm rupture of membranes and neutrophil influx causing chorioamnionitis.
Discovery of a highly selective chemical inhibitor of matrix metalloproteinase-9 (MMP-9) that allosterically inhibits zymogen activation
MMP-9 was shown to be useful in the diagnosis of cervical cancer, but only in the combined analysis with CA 125 (show MUC16 Proteins), as a new diagnostic panel.
Oxidatively modified low-density lipoproteins (oxLDL) alter the function of the endoplasmic reticulum, inducing ER stress (ERS), which activates inflammatory pathways in macrophages. MMP-9 is the main protease acting on the degradation of the extracellular matrix and the ensuing destabilization of the atherosclerotic plaque. oxLDL stimulate MMP-9 expression and secretion in macrophages by mechanisms involving ERS.
The results indicated that MMP-2 (show MMP2 Proteins) -1306C/T and MMP-9 -1562C/T polymorphisms might be associated with an increased risk of T-Cell acute lymphoblastic leukemia in a Chinese population.
Taken together, our data suggest that eupatilin inhibits TNFalpha (show TNF Proteins)-induced MMP-2 (show MMP2 Proteins)/-9 expression by suppressing NF-kappaB (show NFKB1 Proteins) and MAPKAP-1 (show MAPKAP1 Proteins) pathways via PPARalpha (show PPARA Proteins). Our findings suggest the usefulness of eupatilin for preventing skin aging.
Levels of miR106a are modulated during cellular migration, causing a change in the levels of SIRT-1 (show SIRT1 Proteins) mRNA by affecting its stability and the levels of SIRT-1 (show SIRT1 Proteins) in turn can regulate the levels of MMP9.
These results suggest that the phosphorylation of STAT3 (show STAT3 Proteins) regulates MMP-9 production in ovarian cancer, which might be responsible for its invasiveness and metastasis.
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 (show TIMP1 Proteins), and NGAL (show LCN2 Proteins) (also MMP2 (show MMP2 Proteins) in 220 kDa complex) without proteolytic activity.
Data demonstrate for the first time that MMP2 (show MMP2 Proteins) 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 (show MMP2 Proteins), caspase-3 (show CASP3 Proteins) and BDNF (show BDNF Proteins)
Oxygen for newborn resuscitation increases MMP-2 (show MMP2 Proteins)/-9 activity resulting in tissue damage and influencing remodeling processes.
contribution of MMPs to the inflammatory breakdown of the blood-CSF (show CSF2 Proteins) barrier in vitro
The levels of matrix metalloproteinase-2 (show MMP2 Proteins) 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
Variable gene expression (eg, matrix metalloproteinase-9, CCL2 (show CCL2 Proteins) and Lp-PLA(2 (show Lp-PLA2 Proteins)) mRNAs), both in regard to the arterial bed and duration of disease, was associated with variable plaque development and progression.
The results showed that MMP-2 (show MMP2 Proteins), 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.
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 (show PTH Proteins) during metamorphosis.
MMP-9TH is responsible in the larval epithelial apoptosis through degrading ECM (show MMRN1 Proteins) 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 (show TIMP2 Proteins), MT1-MMP (show MMP14 Proteins) and Gel-A, but not MT3-MMP (show MMP24 Proteins) or TIMP-3 (show TIMP3 Proteins), are elevated during periods of cell death and proliferation
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 (show HP Proteins)-MMP 9 complexes appear sooner and decline more rapidly than other acute phase proteins.
Activation of cytosolic MMP-9 and MMP-2 (show MMP2 Proteins) 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 (show TGFB1 Proteins) and TNF-alpha (show TNF Proteins) in IL-1beta (show IL1B Proteins) mediated activation of proMMP-9 in pulmonary artery smooth muscle cells: involvement of an aprotinin sensitive protease.
Decreased MMP-9 and increased TIMP-1 (show TIMP1 Proteins) 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 (show EGF Proteins) on MMP-9 and TIMP-1 (show TIMP1 Proteins) expression by semiquantitative RT-PCR and MMP activity by zymography.
results suggest a significant role of matrix metalloproteinase-2 (show MMP2 Proteins) and-9 in growth and development of bovine follicle
Cells constitutively produced proMMP-9 and proMMP-2, and treatment with TNFalpha (show TNF Proteins), hepatocyte growth factor (show HGF Proteins), 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 (show MMP2 Proteins), MMP-9, and TIMP-2 (show TIMP2 Proteins) 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.
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 (show TNF Proteins) can stimulate MMP-2 (show MMP2 Proteins)/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 (show VEGFA Proteins) 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 (show MMP2 Proteins), MMP-9 and TIMP-1 (show TIMP1 Proteins) 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 (show MMP3 Proteins) and 9 and increase the expression of PPARgamma (show PPARG Proteins) in atherosclerotic rabbits.
TGF-beta (show TGFB1 Proteins) mediated MMP-9 induction may be regulated by the NF-kappaB (show NFKB1 Proteins), Smad3 (show SMAD3 Proteins), and JNK (show MAPK8 Proteins) pathways, whereas the IL-1beta (show IL1B Proteins) mediated induction may be regulated by the NF-kappaB (show NFKB1 Proteins) and p38 (show MAPK14 Proteins) pathways.
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 (show MMP13 Proteins).
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 (show MMP2 Proteins) and MMP-9 in the embryonic zebrafish.
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