Search results for "Metalloproteinase 9"

showing 10 items of 74 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
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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
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The immunoexpression of matrix metalloproteinase MMP2 and MMP9 as prognostic significance in cutaneous metastases of breast carcinoma

2004

Aim. Many types of cutaneous metastasis occur in carcinoma of the breast. Cutaneous metastasis has been reported as having a poor prognosis. A fundamental prerequisite for carcinoma cells to metastatize is the ability of the tumour cells to dissociate from the primary tumour and to breach matrix proteins. Degradation and remodelling of matrix proteins can be affected by a variety of enzymatic activities including the matrix metalloproteinases (MMPs). We have analysed the sensitivity, specificity and predictive value of immunohistochemical staining with monoclonal antibodies directed against gelatinase A (MMP-2) and B (MMP-9) in cutaneous metastatic breast carcinoma. Methods. Twenty-two pati…

Gelatinase ABreast neoplasmMetalloproteinase 9Gelatinase BSkin neoplasmsMetalloproteinase 2
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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
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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
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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
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Nandrolone decanoate interferes with testosterone biosynthesis altering blood-testis barrier components

2017

Abstract The aim of this study was to investigate whether nandrolone decanoate (ND) use affects testosterone production and testicular morphology in a model of trained and sedentary mice. A group of mice underwent endurance training while another set led a sedentary lifestyle and were freely mobile within cages. All experimental groups were treated with either ND or peanut oil at different doses for 6 weeks. Testosterone serum levels were measured via liquid chromatography–mass spectrometry. Western blot analysis and quantitative real‐time PCR were utilized to determine gene and protein expression levels of the primary enzymes implicated in testosterone biosynthesis and gene expression leve…

Male0301 basic medicinemedicine.medical_specialtyNandrolone decanoateStimulationEndogenyMUC1BiologyMale infertilityMice03 medical and health sciencesAnabolic AgentsWestern blotPhysical Conditioning AnimalInternal medicineTestisGene expressionmedicineAnimalsNandroloneBlood-testis barrier; MMP-2; MMP-9; MUC1; Nandrolone decanoate; Testosterone; TJP1; Molecular Medicine; Cell Biologyblood–testis barrierInducerTestosteroneTJP1TestosteroneBlood-testis barrierBlood–testis barrierMMP‐9medicine.diagnostic_testMMP-2Mucin-1Tissue Inhibitor of MetalloproteinasesOriginal ArticlesCell Biologymedicine.diseaseProtein Transport030104 developmental biologyEndocrinologyGene Expression RegulationMatrix Metalloproteinase 9Zonula Occludens-1 ProteinMatrix Metalloproteinase 2Molecular MedicineOriginal ArticleMMP‐2Sedentary BehaviorMMP-9Signal Transduction
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Roles of p53, NF-κB and the androgen receptor in controlling NGAL expression in prostate cancer cell lines

2018

Neutrophil gelatinase-associated lipocalin (NGAL a.k.a lipocalin 2, lnc2) is a secreted protein which can form a complex with matrix metalloproteinase-9 (MMP9). This MMP9/NGAL complex has been associated with metastasis. MMP9 and NGAL are detected in the urine of patients afflicted with many different types of cancer, including prostate cancer. The effects of p53, NF-κB and the androgen receptor (AR) on the expression of NGAL was examined in four prostate cancer cell lines. Prostate cancer cell lines that are AR negative and expressed either mutant or no p53 (DU145 and PC3) displayed higher levels of NGAL expression compared to the prostate cancer cell lines (LNCaP and 22Rv-1) which are AR …

Male0301 basic medicinep53Cancer ResearchLipocalinMMP9Metastasis03 medical and health sciencesProstate cancerDU145GeneticCell Line Tumorandrogen receptorLNCaPGeneticsmedicineHumansNF-kappaBNGALMolecular BiologyChemistryNF-kappa BProstatic Neoplasmsmedicine.diseaseprostate cancerGene Expression Regulation NeoplasticAndrogen receptor030104 developmental biologyMatrix Metalloproteinase 9Receptors AndrogenCell cultureCancer researchMolecular MedicineTumor Suppressor Protein p53
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BRAF(V600E) MUTATION AND THE BIOLOGY OF PAPILLARY THYROID CANCER

2008

BRAF((V600E)) mutation is the most frequent genetic alteration in papillary thyroid carcinomas (PTCs) that are 80-90% of all thyroid cancers. We evaluated the relationship between BRAF((V600E)) and tumor, host, and environmental factors in PTCs from all geographical areas of Sicily. By PCR, BRAF((V600E)) was investigated in a series of 323 PTCs diagnosed in 2002-2005. The correlation between clinicopathological tumor, host, and environmental characteristics and the presence of BRAF((V600E)) were evaluated by both univariate and multivariate analyses. BRAF((V600E)) was found in 38.6% PTCs, with a 52% frequency in the classical PTCs and 26.4% in the tall cell variant. Univariate analysis indi…

MaleCancer Researchendocrine system diseasesEndocrinology Diabetes and Metabolismmedicine.disease_causethyroidPapillary thyroid cancerSettore MED/13 - EndocrinologiaImmunoenzyme TechniquesEndocrinologythyroid cancerskin and connective tissue diseasesSicilyMicrodissectionBRAF(V600E)Univariate analysisMutationGeographyReverse Transcriptase Polymerase Chain ReactionThyroidBRAF V600; Papillary Thyroid CancerMiddle Agedhumanitiesmedicine.anatomical_structureMatrix Metalloproteinase 9OncologyLymphatic MetastasisDisease ProgressionFemaleMicrodissectionProto-Oncogene Proteins B-rafPapillary thyroid cancer BRAF(V600E) thyroid thyroid cancerBRAF V600BiologyThyroid carcinomamedicineCarcinomaHumansNeoplasm InvasivenessRNA MessengerThyroid NeoplasmsneoplasmsDNA PrimersLasersPapillary thyroid cancer BRAFmedicine.diseaseCarcinoma Papillarydigestive system diseasesMutationCancer researchV600EFollow-Up StudiesPapillary Thyroid Cancer
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Heterogeneous activation of MMP-9 due to prostate cancer-bone interaction.

2007

OBJECTIVES To determine whether matrix metalloproteinase (MMP)-9 activation resulting from prostate cancer cell-bone interaction is dependent on the tumor cell type and/or the nature of the bone microenvironment. METHODS In vitro co-cultures of human prostate cancer cells (PC3 and C4-2B) and mouse, human fetal, or human adult tissues were performed. In vivo the tumor cells were intratibially injected in SCID mice or intraosseously inoculated into fetal or adult bone xenografts in SCID mice. MMP-2 and MMP-9 expression and activation were determined by gelatin zymography in conditioned media obtained in vitro and in lysates derived from the in vivo studies at different time points. RESULTS Ac…

MaleFetusPathologymedicine.medical_specialtybusiness.industryUrologyBone metastasisProstatic NeoplasmsMice SCIDMatrix metalloproteinaseBone tissuemedicine.diseaseIn vitroBone and BonesProstate cancerMicemedicine.anatomical_structureMatrix Metalloproteinase 9In vivoCancer cellMedicineAnimalsHumansbusinessCells CulturedUrology
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