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Human MMP2 Protein expressed in Human Cells - ABIN2002031
Brooks, Silletti, von Schalscha, Friedlander, Cheresh: Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity. in Cell 1998
Show all 7 Pubmed References
Human MMP2 Protein expressed in Escherichia coli (E. coli) - ABIN1080273
Zheng, Hu, Huang, Xu, Yang, Li: In vivo bioengineered ovarian tumors based on collagen, matrigel, alginate and agarose hydrogels: a comparative study. in Biomedical materials (Bristol, England) 2015
study demonstrated that matrix metalloproteinase 1 (show MMP1 Proteins) and 2 might be fundamental for events related to equine tissue remodeling, which occurs during follicular development
Data indicate that matrix metalloproteinases mmp1 (show MMP1 Proteins) and mmp2 mutants have distinct heart phenotypes.
We also show that follicular OA-Oamb signaling induces Mmp2 enzymatic activation but not Mmp2 protein expression, likely via intracellular Ca2 (show CA2 Proteins)+ as the second messenger.
Finally, matrix metalloproteinase 2 (Mmp2), a type of protease thought to facilitate mammalian ovulation, is expressed in mature follicle and corpus luteum cells.
As a Wnt (show WNT4 Proteins) signaling antagonist, MMP2 cleaves the glypican (show GPC1 Proteins), reducing the ability of Dlp (show DMD Proteins) to interact with the Wnt (show WNT4 Proteins) ligand and promote its distribution.
Matrix metalloproteinase 2 is required for fat-body remodeling in Drosophila
Drosophila MMP2 regulates the matrix molecule faulty attraction (Frac) to promote motor axon targeting in Drosophila.
Dendrite reshaping of adult Drosophila sensory neurons requires matrix metalloproteinase MMP2-mediated modification of the basement membranes
Mmp2 expression in the developing air sac (show ADCY10 Proteins) is controlled by the Drosophila FGF homolog Branchless and then participates in a negative feedback and lateral inhibition mechanism that defines the precise pattern of FGF signaling.
findings demonstrate a critical role for Mmp2 in tubulogenesis post-induction, and implicate Mmp2 in regulating dynamic and essential changes to the extracellular matrix
Dexamethasone and hydrocortisone alter expression and activity of MMP-2 and MMP-9 (show MMP9 Proteins) in the embryonic zebrafish.
developed a novel selective radiolabeled MMP2/9 inhibitor, suitable for single photon emission computed tomography (SPECT) imaging that effectively targets atherosclerotic lesions in mice
MMP-2 and MMP-9 (show MMP9 Proteins) have roles in early stages of experimental autoimmune encephalomyelitis induction; MMP-9 (show MMP9 Proteins) from an immune cell source is required in EAE for initial infiltration of leukocytes into the central nervous system
This study illustrated that tumour-derived MMP2 has at least two roles in tumour malignancy; to enhance tumour invasiveness by degrading the extracellular matrix and to enhance tumour growth by promoting vessel maturation and function.
MMP-2 and -9 expression were suppressed significantly by treatment with SB-3CT. The data demonstrated, for the first time, that SB-3CT strongly reduced corneal lymphangiogenesis and macrophage infiltration during inflammation.
animals were submitted to the evaluation of Blood-Brain Barrier permeability and MMP-2 and MMP-9 (show MMP9 Proteins) in striatum, hippocampus and cerebral cortex
High MMP2 expression is associated with abdominal aortic aneurysm.
Low MMP2 expression is associated with liver fibrosis.
Cleavage of beta-DG still occurred when both MMP-2 and MMP-9 (show MMP9 Proteins) 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.
NH2-terminal truncated MMP-2 "primes" the kidney to enhanced susceptibility to I-R injury via induction of mitochondrial dysfunction.
Study demonstrated evidence of beta-dystroglycan cleavage by matrix metalloproteinase-2/-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.
The expression of RECK (show RECK Proteins) in human healthy and diseased gingiva may contribute to periodontal physiological and pathological processes; low RECK (show RECK Proteins) expression may be associated with the enhanced MMP-2 and MMP-9 (show MMP9 Proteins) production in inflamed gingiva.
Results continue to establish ANG (show ANG Proteins) as an oncoprotein and further reveal that ANG (show ANG Proteins) contributes to oncogenesis by the activation of MMP2 through modulation of DNMT3b (show DNMT3B Proteins) functions.
This study demonstrated that MMP2 higher expression in glioblastoma
GABRA3 (show GABRA3 Proteins) induced MMP-2 and MMP-9 (show MMP9 Proteins) expression through activation of the JNK (show MAPK8 Proteins)/AP-1 (show FOSB Proteins) signaling pathway, promoting lymphatic metastasis in lung adenocarcinoma.
Kinase activation led to increased MMP-2 and MT1-MMP (show MMP14 Proteins) 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
MMP2/9 are elevated in epicardial adipose tissue from patients with coronary artery disease.
TSP-2 (show THBS2 Proteins) enhances the migration of PCa (show FLVCR1 Proteins) cells by increasing MMP-2 expression through down-regulation of miR (show MLXIP Proteins)-376c expression.
Concentrations of MMP-2 and MMP-9 (show MMP9 Proteins) in serum in humans measured after acute stroke are potentially influenced by extraneous covariates rather than being directly associated with characteristics of the underlying stroke.
There were no differences in activities of MMP-2, proMMP-9, and MMP-9 (show MMP9 Proteins)/NGAL (neutrophil gelatinase associated lipocalin (show LCN2 Proteins)) complex (gelatin substrate) in men with detected prostate cancer, although the latter two were somewhat diminished.
Data indicate that the matrix metallopeptidases MMP-2/MMP-9 (show MMP9 Proteins) ratio provided better compromise between specificity and sensitivity in distinguishing PE from normal pregnancies, than either of the two MMPs alone.
this study shows that differential FFAR1 signaling is associated with gene expression or gelatinase granule release in bovine neutrophils
NADPH oxidase (show NOX1 Proteins) plays an important role in proMMP-2 expression and activation and MMP-2 mediated SMC (show DYM Proteins) proliferation occurs through the involvement of Spm (show NPC1 Proteins)-Cer (show CBLN1 Proteins)-S1P (show MBTPS1 Proteins) signaling axis under ANG II (show AGT Proteins) stimulation of PASMCs
The expression patterns of MMP1 (show MMP1 Proteins), MMP2, and MMP8 (show MMP8 Proteins) were explored during fetal and postnatal development of longissimus dorsi muscle in cattle, and the relationships of MMP1 (show MMP1 Proteins), MMP2, and MMP8 (show MMP8 Proteins) expression levels with meat quality traits were analyzed in cattle. The expression of MMP1 (show MMP1 Proteins), MMP2, and MMP8 (show MMP8 Proteins) were also tested in four kinds of fat tissues and three kinds of skeletal muscle tissues.
The results showed that a decrease in MMP-1 (show MMP1 Proteins) and MMP-2 gene expression is accompanied with a decrease in NO concentrations in infertile cows affected with ovarian cysts.
Activation of cytosolic MMP-9 (show MMP9 Proteins) and MMP-2 was investigated in the retinal endothelial cells incubated in high glucose for 6-96 h, and correlated with their mitochondrial accumulation and mitochondrial damage.
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 (show MMP14 Proteins)-dependent and -independent pathway.
Data suggest that EMMPRIN derived from endometrial epithelial cells regulates expression of matrix metalloproteinases (MMP-2; MMP-14 (show MMP14 Proteins)) in endometrial stromal cells; expression of stromal MMPs is significantly higher in coculture with epithelial cells.
Adding pure bovine MMP-2 to the smooth muscle membrane suspension causes an increase in Ca(2+)-ATPase activity, but the pretreatment with TIMP-2 (show TIMP2 Proteins) inhibits the increase in the enzyme activity
A differential pattern of matrix metalloproteinase-2 and Tissue inhibitor metalloproteinase-2 was observed in cow uteri with adenomyosis.
MMP-14 (show MMP14 Proteins), MMP-2 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.
we demonstrated the presence of high molecular weight (HMW) complexes (130, 170, and 220 kDa) containing MMP9 (show MMP9 Proteins), TIMP1 (show TIMP1 Proteins), and NGAL (show LCN2 Proteins) (also MMP2 in 220 kDa complex) without proteolytic activity.
Data demonstrate for the first time that MMP2 and MMP9 (show MMP9 Proteins) are expressed in swine ovarian follicle both in theca and granulosa layers.
FiO2 used for resuscitation affects matrix metalloproteinases MMP-9 (show MMP9 Proteins) and MMP-2, caspase-3 (show CASP3 Proteins) and BDNF (show BDNF Proteins)
MMP-2 may play an important role in regulating MLC1 turnover in the heart under normal physiological conditions
Oxygen for newborn resuscitation increases MMP-2/-9 activity resulting in tissue damage and influencing remodeling processes.
PI3K-dependent regulation of MT1-MMP (show MMP14 Proteins) protein synthesis and subsequent activation of latent MMP-2 as critical events in neointimal hyperplasia after vascular injury.
MMP-2 processes dental sialophosphoprotein into smaller subunits in the dentin matrix during odontogenesis
contribution of MMPs to the inflammatory breakdown of the blood-CSF (show CSF2 Proteins) barrier in vitro
The levels of matrix metalloproteinase-2 and matrix metalloproteinase-9 (show MMP9 Proteins) in the corpus luteum of swine during luteolysis are reported.
Hemodialysis graft placement leads to early increases in wall shear stress, VEGF-A (show VEGFA Proteins), pro-MMP-9 (show MMP9 Proteins), MMP-2, VEGFR-1 (show FLT1 Proteins), VEGFR-2 (show KDR Proteins), and TIMP-1 (show TIMP1 Proteins), which may contribute to the development of venous stenosis.
Inflammatory factors such as TNF-alpha (show TNF Proteins) can stimulate MMP-2/9 activity in corneal epithelium cells. This may be a potential manipulating mechanism of MMP expression in the pathogenesis of corneal diseases
Results provide evidence that MMP-2 bears the potentiality to cleave alpha-DG enriched from rabbit skeletal muscle indicating that this degradation indeed might also occur in vivo.
In conclusion, MMP-2 could be responsible for the proteolysis of dystrophin (show DMD Proteins).
Castor oil polymer induces bone formation with high matrix metalloproteinase-2 expression.
MMP2 spinal cord expression is increased in cervical spondylotic myelopathy.
Ulinastatin (show AMBP Proteins) effectively inhibited the increased expression of MMP-2, MMP-3 (show MMP3 Proteins), and iNOS (show NOS2 Proteins) in degenerated NP cells induced by IL-1beta (show IL1B Proteins) in vitro.
Hemoperfusion could obviously reduce oxidative stress and the expression levels of MMP-2, MMP-9 (show MMP9 Proteins) and TIMP-1 (show TIMP1 Proteins) in rabbits with acute paraquat poisoning.
The RNA interference targeting COX-2 can effectively inhibit the expression of COX-2 and MMP-2 in IL-1alpha stimulated rabbit corneal stromal cells in vitro.
Our results strongly suggest that ischaemic postconditioning may exert part of its cardioprotective effects through the inhibition of MMP-2 activity.
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. This gene encodes an enzyme which degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. Mutations in this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms have been found for this gene.
, matrix metalloprotease 2
, matrix metalloproteinase
, matrix metalloproteinase 2
, 72 kDa type IV collagenase
, Gelatinase A
, matrix metalloproteinase-2
, 72 kDa gelatinase
, gelatinase A
, 72kD gelatinase
, 72kD type IV collagenase
, 72kDa gelatinase
, 72kDa type IV collagenase
, collagenase type IV-A
, matrix metalloproteinase-II
, neutrophil gelatinase
, matrix metalloproteinase 2 (72 KDa type IV collagenase)
, matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)