Search results for "Matrix Metalloproteinase"

showing 10 items of 212 documents

MMP-10 Is Required for Efficient Muscle Regeneration in Mouse Models of Injury and Muscular Dystrophy

2013

Abstract Matrix metalloproteinases (MMPs), a family of endopeptidases that are involved in the degradation of extracellular matrix components, have been implicated in skeletal muscle regeneration. Among the MMPs, MMP-2 and MMP-9 are upregulated in Duchenne muscular dystrophy (DMD), a fatal X-linked muscle disorder. However, inhibition or overexpression of specific MMPs in a mouse model of DMD (mdx) has yielded mixed results regarding disease progression, depending on the MMP studied. Here, we have examined the role of MMP-10 in muscle regeneration during injury and muscular dystrophy. We found that skeletal muscle increases MMP-10 protein expression in response to damage (notexin) or diseas…

Duchenne muscular dystrophyMatrix metalloproteinaseBiologyMuscle disorderMuscular DystrophiesExtracellular matrixMiceMatrix Metalloproteinase 10medicineAnimalsHumansRegenerationMuscular dystrophyMuscle SkeletalRegeneration (biology)Skeletal muscleCell BiologyAnatomymedicine.diseaseCell biologyDisease Models Animalmedicine.anatomical_structureMatrix Metalloproteinase 9Mice Inbred mdxMatrix Metalloproteinase 2Molecular MedicineITGA7Developmental BiologyStem Cells
researchProduct

E-selectin modulates the malignant properties of T84 colon carcinoma cells.

2002

The extravasation of metastatic cells is regulated by molecular events involving the initial adhesion of tumor cells to the endothelium and subsequently the migration of cells in the host connective tissue. E-selectin on endothelial cells and sialyl Lewis X carbohydrate component on tumor cells are mainly involved in the adhesion of colon carcinoma cells to the endothelium of target organ. Interaction of T84 colon cancer cells to purified E-selectin in vitro caused an increase in the tyrosine phosphorylation of a number of proteins as well as the modulation of cellular properties correlated to the metastatic phenotype. Specifically, E-selectin-stimulated actin reorganization, increased coll…

EndotheliumLactams MacrocyclicBiophysicsOligosaccharidesBiologyBiochemistryCell–cell interactionCancer stem cellCell MovementE-selectinmedicineBenzoquinonesCell AdhesionTumor Cells CulturedHumansEnzyme InhibitorsNeoplasm MetastasisPhosphorylationCell adhesionPhosphotyrosineSialyl Lewis X AntigenMolecular BiologyCells CulturedCarcinomaSoluble cell adhesion moleculesQuinonesCell migrationCell BiologyProtein-Tyrosine KinasesPhosphoproteinsCoculture TechniquesCell biologymedicine.anatomical_structureRifabutinCancer cellColonic NeoplasmsCancer researchbiology.proteinMatrix Metalloproteinase 2Endothelium VascularE-SelectinBiochemical and biophysical research communications
researchProduct

Extracellular Hsp70 Enhances Mesoangioblast Migration via an Autocrine Signaling Pathway

2016

Mouse mesoangioblasts are vessel-associated progenitor stem cells endowed with the ability of multipotent mesoderm differentiation. Therefore, they represent a promising tool in the regeneration of injured tissues. Several studies have demonstrated that homing of mesoangioblasts into blood and injured tissues are mainly controlled by cytokines/chemokines and other inflammatory factors. However, little is known about the molecular mechanisms regulating their ability to traverse the extracellular matrix (ECM). Here, we demonstrate that membrane vesicles released by mesoangioblasts contain Hsp70, and that the released Hsp70 is able to interact by an autocrine mechanism with Toll-like receptor …

Extracellular VesicleNF-kappa BEndothelial CellsModels BiologicalHsp70Toll-Like Receptor 4Autocrine CommunicationMicePhosphatidylinositol 3-KinasesMembrane MicrodomainsMatrix Metalloproteinase 9NF-KappaB Inhibitor alphaCell MovementMesoangioblast Stem CellAnimalsMatrix Metalloproteinase 2HSP70 Heat-Shock ProteinsExtracellular SpaceMatrix MetalloproteinaseProto-Oncogene Proteins c-aktLow Density Lipoprotein Receptor-Related Protein-1MigrationProtein BindingSignal Transduction
researchProduct

Urokinase Plasminogen Activator and Gelatinases Are Associated with Membrane Vesicles Shed by Human HT1080 Fibrosarcoma Cells

1997

Membrane vesicles are shed by tumor cells both in vivo and in vitro. Although their functions are not well understood, it has been proposed that they may play multiple roles in tumor progression. We characterized membrane vesicles from human HT1080 fibrosarcoma cell cultures for the presence of proteinases involved in tumor invasion. By gelatin zymography and Western blotting, these vesicles showed major bands corresponding to the zymogen and active forms of gelatinase B (MMP-9) and gelatinase A (MMP-2) and to the MMP-9. tissue inhibitor of metalloproteinase 1 complex. Both gelatinases appeared to be associated with the vesicle membrane. HT1080 cell vesicles also showed a strong, plasminoge…

GelatinasesMacromolecular SubstancesFibrosarcomaBlotting WesternCellGelatinase ABiologyBiochemistryTumor Cells CulturedmedicineHumansCollagenasesFibrinolysinMolecular BiologyGlycoproteinsUrokinaseEnzyme PrecursorsVesicleMetalloendopeptidasesTissue Inhibitor of MetalloproteinasesCell BiologyTissue inhibitor of metalloproteinaseUrokinase-Type Plasminogen ActivatorMolecular biologyExtracellular MatrixUrokinase receptorBloodmedicine.anatomical_structureMatrix Metalloproteinase 9GelatinasesMatrix Metalloproteinase 2HT1080medicine.drugJournal of Biological Chemistry
researchProduct

Liver-specific overexpression of matrix metalloproteinase 9 (MMP-9) in transgenic mice accelerates development of hepatocellular carcinoma.

2010

Matrix metalloproteinase-9 (MMP-9) plays a central role in tumor invasion and development of metastases. Expression of MMP-9 had been shown in human hepatocellular carcinomas (HCCs). However, it remained unclear whether MMP-9 could influence development of HCC. In order to address this issue, we generated transgenic mice overexpressing MMP-9 in the liver. In order to avoid embryonic lethality a Cre-lox system was utilized for conditional overexpression of MMP-9 under control of an albumin enhancer and promoter. Induction of MMP-9 overexpression in transgenic mice was achieved by i.v. injection of an adenovirus coding for the Cre recombinase. Initiation of liver carcinogenesis was achieved b…

Genetically modified mouseCancer ResearchLiver tumorTransgeneGenetic VectorsCre recombinaseGene ExpressionMice TransgenicBiologymedicine.disease_causeMiceLiver Neoplasms ExperimentalIn vivoGene OrdermedicineAnimalsHomeostasisHumansHomologous RecombinationMolecular BiologyIntegrasesHCCSmedicine.diseaseMolecular biologyCell Transformation NeoplasticPhenotypeLiverMatrix Metalloproteinase 9Organ SpecificityHepatocellular carcinomaCarcinogenesisMolecular carcinogenesis
researchProduct

Redox regulation of genome stability by effects on gene expression, epigenetic pathways and DNA damage/repair

2015

Reactive oxygen and nitrogen species (e.g. H2O2, nitric oxide) confer redox regulation of essential cellular signaling pathways such as cell differentiation, proliferation, migration and apoptosis. In addition, classical regulation of gene expression or activity, including gene transcription to RNA followed by translation to the protein level, by transcription factors (e.g. NF-κB, HIF-1α) and mRNA binding proteins (e.g. GAPDH, HuR) is subject to redox regulation. This review will give an update of recent discoveries in this field, and specifically highlight the impact of reactive oxygen and nitrogen species on DNA repair systems that contribute to genomic stability. Emphasis will be placed …

Genome instabilityRedox signalingRNA UntranslatedEpigenetic regulation of neurogenesisDNA RepairHuR mRNA-binding protein in the 3′-untranslated regionClinical BiochemistryHDAC histone deacetylaseReview ArticleAP-1 activator protein 1BiochemistryApe-1 apurinic/apyrimidinic endonuclease 1GPx-1 glutathione peroxidase-1Epigenesis GeneticHistonesTrx thioredoxinPHD prolylhydroxylaseBER base excision repairlcsh:QH301-705.5HO-1 heme oxygenase-1EpigenomicsGeneticsRegulation of gene expressionNox member of the NADPH oxidase familylcsh:R5-920JmjC Jumonji C domain-containing histone demethylasesHIF-1α hypoxia inducible factor-1α5-hmC 5-hydroxymethylcytosineddc:Cell biologyMMP matrix metalloproteinaseGrx glutaredoxinGAPDH glyceraldehyde-3-phosphate dehydrogenaseNrf2 nuclear factor erythroid related factor 2DNA methylationEpigeneticslcsh:Medicine (General)Oxidation-ReductionSignal Transduction5-mC 5-methylcytosineDNA repairDNA damageNF-κB nuclear factor-κBBiologyGenomic InstabilityRNS reactive nitrogen speciesROS reactive oxygen speciesNER nucleotide excision repairSOD superoxide dismutaseOxyR transcription factor (hydrogen peroxide-inducible genes activator)HumansEpigeneticsOrganic ChemistryPETN pentaerithrityl tetranitrateGene regulationOxidative StressDNMT DNA methyltransferaseGene Expression Regulationlcsh:Biology (General)AREs AU-rich elementsHAT histone acetyltransferaseKeap1 kelch-like ECH-associated protein 1BiomarkersCOPD chronic obstructive pulmonary disorderDNA DamageRedox Biology
researchProduct

Role of the Netrin-like Domain of Procollagen C-Proteinase Enhancer-1 in the Control of Metalloproteinase Activity

2010

The netrin-like (NTR) domain is a feature of several extracellular proteins, most notably the N-terminal domain of tissue inhibitors of metalloproteinases (TIMPs), where it functions as a strong inhibitor of matrix metalloproteinases and some other members of the metzincin superfamily. The presence of a C-terminal NTR domain in procollagen C-proteinase enhancers (PCPEs), proteins that stimulate the activity of astacin-like tolloid proteinases, raises the possibility that this might also have inhibitory activity. Here we show that both long and short forms of the PCPE-1 NTR domain, the latter beginning at the N-terminal cysteine known to be critical for TIMP activity, show no inhibition, at …

Glycobiology and Extracellular MatricesMatrix metalloproteinaseBiochemistryBONE MORPHOGENETIC PROTEIN-1AdamalysinFIBRILLAR PROCOLLAGENSTolloid ProteinaseExtracellular Matrix Proteins0303 health sciencesADAMTSFRIZZLED-RELATED PROTEINS030302 biochemistry & molecular biologyTissue Inhibitor of Metalloproteinases11 Medical And Health SciencesALPHA-CONVERTING-ENZYMEI PROCOLLAGENADAM ProteinsExtracellular MatrixPLASMINOGEN ACTIVATIONBiochemistryCollagen03 Chemical SciencesLife Sciences & BiomedicineProcollagenBiochemistry & Molecular BiologyTERMINAL DOMAINTolloid-Like MetalloproteinasesADAMTSBiologyBone morphogenetic protein 1Cell Line03 medical and health sciencesDisintegrinHumansHUMAN TISSUE INHIBITORMatrix MetalloproteinaseMolecular BiologyGlycoproteins030304 developmental biologyThrombospondinScience & TechnologyHeparinADAMCell Biology06 Biological SciencesMATRIX-METALLOPROTEINASESProtein Structure TertiaryADAM ProteinsProcollagen peptidaseSULFATED GLYCOSAMINOGLYCANSEnzymologybiology.proteinJournal of Biological Chemistry
researchProduct

Mutant p53 gain of function can be at the root of dedifferentiation of human osteosarcoma MG63 cells into 3AB-OS cancer stem cells

2014

Osteosarcoma is a highly metastatic tumor affecting adolescents, for which there is no second-line chemotherapy. As suggested for most tumors, its capability to overgrow is probably driven by cancer stem cells (CSCs), and finding new targets to kill CSCs may be critical for improving patient survival. TP53 is the most frequently mutated tumor suppressor gene in cancers and mutant p53 protein (mutp53) can acquire gain of function (GOF) strongly contributing to malignancy. Studies thus far have not shown p53-GOF in osteosarcoma. Here, we investigated TP53 gene status/role in 3AB-OS cells-a highly aggressive CSC line previously selected from human osteosarcoma MG63 cells-to evaluate its involv…

HistologyTumor suppressor genePhysiologyEndocrinology Diabetes and MetabolismApoptosisIn situ hybridizationBiologyTNF-Related Apoptosis-Inducing LigandCell MovementCancer stem cellCell Line TumorSettore BIO/10 - BiochimicaBiomarkers TumormedicineHumansNeoplasm Invasiveness3AB-OS cells CSCs Cancer cell dedifferentiation Cancer stem cells FISH Fluorescent in situ hybridization GOF Gain of function Human osteosarcoma MMPs Matrix metalloproteinases Mutant p53 Mutant p53 gain of function Mutp53 OS OsteosarcomaClonogenic assayTumor Stem Cell AssayCell ProliferationMembrane Potential MitochondrialOsteosarcomaCancerReceptors Death DomainCell DedifferentiationCell cyclemedicine.diseaseMolecular biologyAmino Acid SubstitutionProto-Oncogene Proteins c-bcl-2Gene Knockdown TechniquesMutationNeoplastic Stem CellsCancer researchOsteosarcomaEctopic expressionTumor Suppressor Protein p53Bone
researchProduct

Immunohistochemical expression of apoptotic factors, cytokeratins, and metalloproteinase-9 in periapical and epithelialized gingival lesions

2012

Bellmann K, 2010, CELL STRESS CHAPERON, V15, P101, DOI 10.1007-s12192-009-0126-9; Cappello Francesco, 2011, Front Biosci (Schol Ed), V3, P341, DOI 10.2741-s155; Cappello F, 2006, CANCER, V107, P2417, DOI 10.1002-cncr.22265; Cappello F, 2002, EUR J HISTOCHEM, V46, P199; Carneiro E, 2009, ORAL SURG ORAL MED O, V107, P127, DOI 10.1016-j.tripleo.2008.07.030; Chandra D, 2007, J BIOL CHEM, V282, P31289, DOI 10.1074-jbc.M702777200; Fujita Y, 2011, ODONTOLOGY, V100, P215; Garcia Celia Carrillo, 2007, Med Oral Patol Oral Cir Bucal, V12, pE585; Garcia CC, 2009, ORAL SURG ORAL MED O, V107, pE43, DOI 10.1016-j.tripleo.2008.12.002; Gregory CD, 2011, J PATHOL, V223, P177, DOI 10.1002-path.2792; Gupta S, …

Histologybusiness.industryCaspase 3GingivaApoptosisGeneral MedicineMolecular biologyImmunohistochemistryCaspase 9EpitheliumPathology and Forensic MedicineCell stressMatrix Metalloproteinase 9cytokeratins MMP-9 caspase-3 caspase-9 perapical lesions epithelial gingival lesions apoptosisIHC PCNA TUNELProliferating Cell Nuclear AntigenMedicineHumansKeratinsbusinessApoptosis Regulatory ProteinsPeriapical Granuloma
researchProduct

Intramuscular Extracellular Matrix: Complex Environment of Muscle Cells

2002

KOVANEN, V. Intramuscular extracellular matrix: Complex environment of muscle cells. Exerc. Sport Sci. Rev., Vol. 30, No. 1, pp 20–25, 2002. Different collagen types among other extracellular matrix molecules, remodeling of the extracellular matrix with the aid of matrix metalloproteinases, and inte

IntegrinsChemistryFibrillar CollagensPhysical Therapy Sports Therapy and RehabilitationNon-Fibrillar CollagensExtracellular matrix moleculesMatrix metalloproteinaseBasement MembraneMatrix MetalloproteinasesExtracellular MatrixCell biologyExtracellular matrixHumansMyocyteOrthopedics and Sports MedicineMuscle SkeletalExercise and Sport Sciences Reviews
researchProduct