Search results for "Matrix Metalloproteinase 2"

showing 10 items of 49 documents

Lipid Peroxidation, Protein Oxidation, Gelatinases, and Their Inhibitors in a Group of Adults with Obesity

2019

AbstractThe association between obesity and cardiovascular diseases has a multifactorial pathogenesis, including the synthesis of inflammatory molecules, the increase in oxidative stress and the dysregulation of the matrix metalloprotease (MMP) concentration and activity. In a group of adults with obesity, divided in 2 subgroups according to the body mass index (BMI), we examined lipid peroxidation, expressed as thiobarbituric acid-reactive substances (TBARS), protein oxidation, expressed as protein carbonyl groups (PCs), plasma gelatinases (MMP-2 and MMP-9), and their tissue inhibitors (TIMP-1 and TIMP-2). In the whole group, as well as in the 2 subgroups (with BMI 30–35 or BMI>35) of o…

AdultMalemedicine.medical_specialtySettore MED/09 - Medicina InternaEndocrinology Diabetes and MetabolismClinical Biochemistry030209 endocrinology & metabolism030204 cardiovascular system & hematologyMatrix metalloproteinasemedicine.disease_causeProtein oxidationBiochemistryPathogenesisLipid peroxidation03 medical and health scienceschemistry.chemical_compound0302 clinical medicineEndocrinologyInternal medicineTBARSHumansMedicineObesityTissue Inhibitor of Metalloproteinase-2Tissue Inhibitor of Metalloproteinase-1business.industryBiochemistry (medical)ProteinsGeneral MedicineMiddle Agedmedicine.diseaseObesityOxidative StressEndocrinologyMatrix Metalloproteinase 9chemistryCase-Control Studiesobesity lipid peroxidation protein oxidation gelatinases TIMPsProteolysisMatrix Metalloproteinase 2FemaleLipid PeroxidationbusinessOxidation-ReductionBody mass indexBiomarkersOxidative stressHormone and Metabolic Research
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Effects of zoledronic acid on proteinase plasma levels in patients with bone metastases.

2006

Background: The effects of the bisphosphonate derivative zoledronic acid (ZA) on the > circulating levels of matrix metalloproteinase-2 (MMP-2), matrix metallo-proteinases-9 > (MMP-9), cathepsin B (Cath B) and urokinase-type plasminogen activator (uPA) in > patients with bone metastasis (BMTS) and the possible correlation with the symptomatic > response induced by this drug in these patients were evaluated. Patients and Methods: > Proteinase levels were determined by enzyme-linked immunosorbent assay (ELISA) in the > plasma of 30 patients with painful bone metastases from breast or prostate cancer > undergoing multiple treatment with ZA (4 mg i.v., every 4 weeks). Healthy subjects > (HS) of…

Aged 80 and overMaleBone Density Conservation AgentsDiphosphonatesZoledronic > acidImidazolesProstatic NeoplasmsBone NeoplasmsBreast NeoplasmsMiddle AgedProteinaseZoledronic AcidCathepsin BMatrix > metalloproteinase-9Matrix Metalloproteinase 9Matrix metalloproteinase-2Bone metastasiBisphosphonates; Bone metastasis; Cathepsin B; Matrix metalloproteinase-2; Matrix > metalloproteinase-9; Proteinases; Urokinase-type plasminogen activator; Zoledronic > acidHumansMatrix Metalloproteinase 2BisphosphonateFemaleUrokinase-type plasminogen activatorAged
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Inhibition of Histone Deacetylase Activity in Human Endometrial Stromal Cells Promotes Extracellular Matrix Remodelling and Limits Embryo Invasion

2011

Invasion of the trophoblast into the maternal decidua is regulated by both the trophoectoderm and the endometrial stroma, and entails the action of tissue remodeling enzymes. Trophoblast invasion requires the action of metalloproteinases (MMPs) to degrade extracellular matrix (ECM) proteins and in turn, decidual cells express tissue inhibitors of MMPs (TIMPs). The balance between these promoting and restraining factors is a key event for the successful outcome of pregnancy. Gene expression is post-transcriptionally regulated by histone deacetylases (HDACs) that unpacks condensed chromatin activating gene expression. In this study we analyze the effect of histone acetylation on the expressio…

Anatomy and PhysiologyGene ExpressionHydroxamic AcidsEndometriumEndocrinologyPregnancyMolecular Cell BiologyCells Culturedreproductive and urinary physiologyRegulation of gene expressionMultidisciplinarybiologyQRObstetrics and GynecologyExtracellular MatrixChromatinCell biologyHistonemedicine.anatomical_structureMatrix Metalloproteinase 9embryonic structuresMatrix Metalloproteinase 2MedicineFemaleHistone deacetylase activityResearch Articlemedicine.drugAdultStromal cellScienceDown-RegulationGene Expression Regulation EnzymologicYoung AdultmedicineHumansEmbryo ImplantationBiologyTissue Inhibitor of Metalloproteinase-3Tissue Inhibitor of Metalloproteinase-1Reproductive SystemTrophoblastUrokinase-Type Plasminogen ActivatorMolecular biologyHistone Deacetylase InhibitorsTrichostatin AAcetylationbiology.proteinStromal CellsDevelopmental Biology
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miR-29b negatively regulates human osteoclastic cell differentiation and function: Implications for the treatment of multiple myeloma-related bone di…

2013

Skeletal homeostasis relies upon a fine tuning of osteoclast (OCLs)-mediated bone resorption and osteoblast (OBLs)-dependent bone formation. This balance is unsettled by multiple myeloma (MM) cells, which impair OBL function and stimulate OCLs to generate lytic lesions. Emerging experimental evidence is disclosing a key regulatory role of microRNAs (miRNAs) in the regulation of bone homeostasis suggesting the miRNA network as potential novel target for the treatment of MM-related bone disease. Here, we report that miR-29b expression decreases progressively during human OCL differentiation in vitro. We found that lentiviral transduction of miR-29b into OCLs, even in the presence of MM cells,…

Bone diseasePhysiologyCellular differentiationCathepsin KClinical BiochemistryGene ExpressionOsteoclastsOsteolysisMMP9Cathepsin KCells CulturedTartrate-resistant acid phosphataseTumorCulturedReceptor Activator of Nuclear Factor-kappa BGenes fosCell DifferentiationOsteoblastCell biologyIsoenzymesmultiple myelomamedicine.anatomical_structureMatrix Metalloproteinase 9osteoclastMatrix Metalloproteinase 2medicine.medical_specialtyfosCellsAcid PhosphataseBiologyCollagen Type IBone resorptionCell LineOsteoclastCell Line TumorInternal medicinemedicineHumansBone ResorptionOsteoblastsmicroRNA.NFATC Transcription FactorsTartrate-Resistant Acid PhosphatasemiR-29bCell Biologymedicine.diseaseActinsMicroRNAsEndocrinologyGenesAcid Phosphatase; Actins; Bone Resorption; Cathepsin K; Cell Differentiation; Cell Line Tumor; Cells Cultured; Collagen Type I; Gene Expression; Genes fos; Humans; Isoenzymes; Matrix Metalloproteinase 2; Matrix Metalloproteinase 9; MicroRNAs; Multiple Myeloma; NFATC Transcription Factors; Osteoblasts; Osteoclasts; Osteolysis; Receptor Activator of Nuclear Factor-kappa BJournal of Cellular Physiology
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Expression of Hugl-1 is strongly reduced in malignant melanoma.

2005

The human gene Hugl-1 (Llgl/Lgl1) has significant homology to the Drosophila tumor suppressor gene lethal(2)giant larvae (lgl). The lgl gene codes for a cortical cytoskeleton protein, Lgl, that is involved in maintaining cell polarity and epithelial integrity. We speculate that Hugl-1 might play a role in epithelial-mesenchymal transition (EMT) and that loss of Hugl-1 expression plays a role in the development or progression of malignant melanoma. Thus, we evaluated melanoma cell lines and tissue samples of malignant melanoma for loss of Hugl-1 transcription. We found that Hugl-1 was downregulated or lost in all cell lines and in most of the tumor samples analysed, and that these losses wer…

Cancer ResearchMMP2Tumor suppressor geneMatrix Metalloproteinases Membrane-AssociatedTranscription GeneticCellBlotting WesternDown-RegulationBiologyTransfectionEpitheliumCell MovementCell Line TumorGeneticsmedicineCell AdhesionMatrix Metalloproteinase 14HumansNeoplasm InvasivenessTissue DistributionRNA MessengerCell adhesionMolecular BiologyMelanomaReverse Transcriptase Polymerase Chain ReactionMelanomaProteinsCell migrationmedicine.diseaseCadherinsImmunohistochemistryMatrix MetalloproteinasesGene Expression Regulation NeoplasticCytoskeletal Proteinsmedicine.anatomical_structureMicroscopy FluorescenceCell cultureImmunologyCancer researchDisease ProgressionMMP14Matrix Metalloproteinase 2RNAOncogene
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Leukocyte subtypes, gelatinases, and their tissue inhibitors in a group of subjects with asymptomatic carotid atherosclerosis

2022

In a cohort of subjects with asymptomatic carotid atherosclerosis (ACA), we have evaluated the neutrophil and lymphocyte count and their ratio (NLR), the gelatinases (MMP-2 and MMP-9) and their tissue inhibitors (TIMP-1 and TIMP-2). At baseline, no difference was observed between ACA subjects and subject control group regarding neutrophil and lymphocyte count while was evident in ACA subjects a significant increase in MMP-2, MMP-9 and TIMP-2 associated to a significant decrease in TIMP-1. Dividing the ACA according to the number of cardiovascular risk factors (CRFs) we have observed an increase in lymphocyte count in the subgroup with 3–5 CRFs. Evaluating the leukocyte subtypes according to…

Carotid Artery Diseasescardiovascular risk factorslymphocytesTissue Inhibitor of Metalloproteinase-2Tissue Inhibitor of Metalloproteinase-1PhysiologyHematologyTIMP-2Asymptomatic carotid atherosclerosisTIMP-1Matrix Metalloproteinase 9neutrophilsinsulin resistancePhysiology (medical)LeukocytesHumansMatrix Metalloproteinase 2Cardiology and Cardiovascular MedicinegelatinasesBiomarkersResearch ArticleClinical Hemorheology and Microcirculation
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Expression of Gelatinases (MMP-2, MMP-9) in human articular cartilage

2013

Osteoarthritis (OA) is a chronic degenerative joint disorder characterized by destruction of the articular cartilage, subchondral bone alterations and synovitis. Matrix metalloproteinases (MMPs) are expressed in joint tissues of patients with osteoarthritis (OA). The objective of this study was to define the steady state levels of two different MMPs to provide more insight into the role of MMPs in cartilage destruction in OA. We investigated the expression of gelatinases through immunohistochemistry Our results show that high levels of MMP-2 and MMP-9 are present in OA and suggest that once these MMPs are fully activated they may contribute to the cartilage destruction in OA.

Cartilage ArticularSettore BIO/17 - IstologiaGelatinasesPathologymedicine.medical_specialtyImmunologyArticular cartilage; Metalloproteinases; Immunohistochemistry; OsteoarthritisArticular cartilageOsteoarthritisMatrix metalloproteinaseArticular cartilageOsteoarthritis HipDownregulation and upregulationSynovitisOsteoarthritisHumansImmunology and AllergyMedicineMetalloproteinasePharmacologybusiness.industryCartilageAnatomyOsteoarthritis Kneemedicine.diseaseImmunohistochemistryUp-Regulationmedicine.anatomical_structureMatrix Metalloproteinase 9Case-Control StudiesMatrix Metalloproteinase 2Immunohistochemistrybusiness
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Regulation of type IV collagen gene expression and degradation in fast and slow muscles during dexamethasone treatment and exercise.

2003

Glucocorticoids have anti-anabolic effects on many tissues and can cause muscle atrophy. However, their effects on type IV collagen gene expression and degradation in skeletal muscle have not been studied previously. Rats were treated daily with dexamethasone or saline. Half the groups of experimental and control animals were also subjected to daily endurance or uphill running exercise to determine the possible preventive effects of exercise. After an experimental period of 3 or 10 days, the extensor digitorum longus, soleus and tibialis anterior muscles were studied. Dexamethasone treatment for 10 days reduced muscle weight and type IV collagen mRNA abundance in all muscles. Gene expressio…

Collagen Type IVmedicine.medical_specialtyPhysiologyClinical BiochemistryAnti-Inflammatory AgentsRadioimmunoassayMatrix metalloproteinaseDexamethasoneRats Sprague-DawleyType IV collagenPhysiology (medical)Internal medicinePhysical Conditioning AnimalGene expressionmedicineAnimalsRNA MessengerReceptorMuscle SkeletalGlucocorticoidsDexamethasoneRegulation of gene expressionTissue Inhibitor of Metalloproteinase-2ChemistrySkeletal muscleBlotting NorthernMuscle atrophyRatsEndocrinologymedicine.anatomical_structureMuscle Fibers Slow-TwitchGene Expression RegulationMuscle Fibers Fast-TwitchMatrix Metalloproteinase 2Femalemedicine.symptommedicine.drugPflugers Archiv : European journal of physiology
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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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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
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