4 edition of Differential regulation of matrix metalloproteinase-2 (MMP-2) by phorbol myrisate acetate, and by DL-[alpha]-difluoromethylornithine, in cell lines of varying tumorigenic and metastatic potential found in the catalog.
Differential regulation of matrix metalloproteinase-2 (MMP-2) by phorbol myrisate acetate, and by DL-[alpha]-difluoromethylornithine, in cell lines of varying tumorigenic and metastatic potential
Thesis (M.Sc.) -- University of Toronto, 1999.
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Vascular matrix metalloproteinase (MMP)-2 activity was higher, but MMP-1 levels were significantly reduced in GK rats, and MMP levels were restored to control levels by ETA receptor antagonism. We conclude that ET-1 promotes cerebrovascular remodeling in type 2 diabetes through differential regulation of by: Matrix metallopeptidases (MMPs), also known as matrix metalloproteinases or matrixins, are metalloproteinases that are calcium-dependent zinc-containing endopeptidases; other family members are adamalysins, serralysins, and MMPs belong to a larger family of proteases known as the metzincin ro: IPR
Hepatic fibrosis is the result of an imbalance between enhanced matrix synthesis and diminished breakdown of connective tissue proteins, the net result of which is increased deposition of extracellular matrix. In this concept, MMPs play an important role because their activity is largely responsible for matrix breakdown (9,10). Differential effects of tumor necrosis factor- on matrix metalloproteinase-2 expression in human myometrial and uterine leiomyoma smooth muscle cells.
Differential Regulation of Matrix Metalloproteinase-2 and -9 Expression and Activity in Adult Rat Cardiac Fibroblasts in Response to Interleukin-1β 21 July | Journal of Biological Chemistry, Vol. , No. 38Cited by: Upregulation of MMP-2 and MMP-9 in diabetes leads to disruption of extracellular matrix and thus causes complications of diabetes. Matrix metalloproteinase 2 and 9 can be potential targets to treat cardiovascular complications of : Lokesh Kumar Bhatt, Veeranjaneyulu Addepalli.
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Differential regulation of matrix metalloproteinase-2 and -9 expression and activity in adult rat cardiac fibroblasts in response to interleukin-1beta. Xie Z(1), Singh M, Singh K.
Author information: (1)Department of Physiology, James H Quillen College of Medicine, James H Quillen Veterans Affairs Medical Center, East Tennessee State University Cited by: The differential regulation of MMP‐2 and MMP‐9, therefore, may be a useful therapeutic target in the treatment of RA.
Activated protein C (APC) is a natural anticoagulant derived from its vitamin K–dependent plasma precursor protein C. Activation of protein C occurs on the endothelial cell surface and is triggered by a complex formed between thrombin and Cited by: The differential effects of PKC isoforms on the regulation of MAPK activity in different cell types may reflect differences in activation of different isoforms of PKC and their downstream coupling.
Of note, IL-1β has been shown to activate ERK1/2, JNKs, and p38 kinase via PKC-independent pathways in intestinal myofibroblasts (40).Cited by: Differential regulation of matrix metalloproteinase 2 and matrix metalloproteinase 9 by activated protein C: Relevance to inflammation in rheumatoid arthritis.
Differential Regulation of Matrix Metalloproteinase-2 and -9 Expression and Activity in Adult Rat Cardiac Fibroblasts in Response to Interleukin-1 October. Differential regulation of matrix metalloproteinase-2 activation in human breast cancer cell lines Erik W. () Differential regulation of matrix metalloproteinase-2 activation in human breast cancer cell lines.
Annals of the New York Academy of Sciences,pp. View at publisher Impact and interest: 0 citations in Scopus. 6 Cited by: 6. Read "Differential regulation of matrix metalloproteinase 2 and matrix metalloproteinase 9 by activated protein C: Relevance to inflammation in rheumatoid arthritis, Arthritis & Rheumatology" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
Differential regulation of matrix metalloproteinase-2 and -9 expression and activity in adult rat cardiac fibroblasts in response to interleukin-1beta. (PMID) PMIDCited by: Matrix metalloproteinases (MMPs) are a group of proteinases that degrade components of the extracellular matrix (ECM).
There is increasing evidence for a link between the activation of MMPs and Alzheimer's disease (AD) pathogenesis, in which both beneficial and detrimental actions of MMPs have been by: Regulation of matrix metalloproteinase 2 by oligomeric amyloid β protein Article in Brain research March with 34 Reads How we measure 'reads'.
Matrix metalloproteinases (MMPs) are a major group of enzymes that regulate cell-matrix composition. MMP genes show a highly conserved modular structure.
Ample evidence exists on the role of MMPs in normal and pathological processes, including embryogenesis, wound healing, inflammation, arthritis, cardiovascular diseases, pulmonary diseases and by: Fig 1.
Effect of doxycycline on matrix metalloproteinase-2 (MMP-2) production from cultured aortic smooth muscle cells (SMCs). Aortic SMCs cultured in either serum-free M (Control) or macrophage or lymphocyte co-culture medium (Stimulated) were treated with doxycycline at indicated concentrations for 24 by: Matrix metalloproteinase-2 (MMP-2), previously named 72 kDa type IV collagenase or gelatinase A, belongs to the MMP family of calcium and zinc-dependent endopeptidases.
MMPs were originally considered to be secreted proteases which play a major role in degrading extracellular matrix (ECM) proteins. Differential regulation of matrix metalloproteinase-2 activation in human breast cancer cell lines. MMP-2 activity increased 71% (n = 5, P β-galactosidase activity showed a fold (n = 8, P MMP-2 transcription at day 3 and day 8, by: 72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the MMP2 gene.
The MMP2 gene is located on chromosome 16 at position The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory s: MMP2, CLG4, CLG4A, MMP-2, MMP-II. Up-regulation of matrix metalloproteinase-2 (MMP-2) expression and down-regulation of extracellular signal-regulated kinase (ERK) activity in human uterine leiomyoma.
Protein and mRNA were extracted from human myometrium (HM) and matched uterine leiomyoma (HL) tissues for western blot and real-time qPCR (RT–qPCR) by: Background and Aims. Matrix metalloproteinase-2 (MMP-2), a type IV collagenase secreted by activated hepatic stellate cells (HSCs), is upregulated in chronic liver disease and is considered a profibrotic mediator due to its proliferative effect on cultured HSCs and ability to degrade normal liver by: Differential regulation of gelatinase A and B and TIMP-1 and -2 by TNFα and HIV virions in astrocytes especially through the production of matrix metalloproteinase-2 A.
Pagenstecher, A.K. Stalder, C.L. Kincaid, S.D. Shapiro, I.L. CampbellDifferential expression of matrix metalloproteinase and tissue inhibitor of matrix Cited by: Differential regulation of platelet aggregation by matrix metalloproteinases-9 and Fernandez-Patron C(1), Martinez-Cuesta MA, Salas E, Sawicki G, Wozniak M, Radomski MW, Davidge ST.
Author information: (1)Perinatal Research Centre, Department of Obstetrics/Gynaecology, University of Alberta, Edmonton, by:.
Expression of Matrix Metalloproteinase-2 and -9 and Their Inhibitors in Peripheral Blood Cells of Patients with Chronic Hepatitis C Article (PDF Available) in Clinical Chemistry 46(2)Ensembl ENSG ENSMUSG UniProt P P RefSeq (mRNA) NM_ NM_ RefSeq (protein) NP_ n/a Location (UCSC) Chr – Mb Chr – Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Tissue inhibitor of metalloproteinases 2 (TIMP2) is a gene and a Aliases: TIMP2, CSCK, DDC8, TIMP .Introduction.
Alteration in the expression of extracellular matrix metalloproteinase inducer (EMMPRIN), matrix metalloproteinase-2 (MMP-2), tissue inhibitors of matrix metalloproteinases (TIMP-2) and platelet derived growth factor (PDGF-AA) Cited by: