Search results for "Metalloproteinase 9"

showing 10 items of 74 documents

Integrated multi-omics investigations of metalloproteinases in colon cancer: Focus on MMP2 and MMP9

2021

Colorectal cancer (CRC) develops by genetic and epigenetic alterations. However, the molecular mechanisms underlying metastatic dissemination remain unclear and could benefit from multi-omics investigations of specific protein families. Matrix metalloproteinases (MMPs) are proteolytic enzymes involved in ECM remodeling and the processing of bioactive molecules. Increased MMP expression promotes the hallmarks of tumor progression, including angiogenesis, invasion, and metastasis, and is correlated with a shortened survival. Nevertheless, the collective role and the possible coordination of MMP members in CRC are poorly investigated. Here, we performed a multi-omics analysis of MMP expression…

ProteomicsMMP2Epithelial-Mesenchymal TransitionQH301-705.5Colorectal cancerBioinformaticsKaplan-Meier EstimateBiologyMatrix metalloproteinaseMMP9ArticleCatalysisEpigenesis GeneticMetastasisCohort StudiesInorganic ChemistryLymphocytes Tumor-InfiltratingmedicineHumansEpithelial–mesenchymal transitionBiology (General)Physical and Theoretical ChemistrySettore BIO/06 - Anatomia Comparata E CitologiaQD1-999Molecular BiologySpectroscopyTissue Inhibitor of Metalloproteinase-2Functional analysisMMP9Organic ChemistryProteolytic enzymesGeneral Medicinemedicine.diseasePrognosisComputer Science ApplicationsColon cancerExtracellular MatrixGene Expression Regulation NeoplasticChemistryMatrix metalloproteinasesMatrix Metalloproteinase 9Tumor progressionCase-Control StudiesColonic NeoplasmsCancer researchMatrix Metalloproteinase 2Gene expressionMMP2
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Membrane vesicles containing matrix metalloproteinase-9 and fibroblast growth factor-2 are released into the extracellular space from mouse mesoangio…

2010

Certain proteins, including fibroblast growth factor-2 (FGF-2) and matrix metalloproteinase-9 (MMP-9), have proved very effective in increasing the efficacy of mesoangioblast stem cell therapy in repairing damaged tissue. We provide the first evidence that mouse mesoangioblast stem cells release FGF-2 and MMP-9 in their active form through the production of membrane vesicles. These vesicles are produced and turned over continuously, but are stable for some time in the extracellular milieu. Mesoangioblasts shed membrane vesicles even under oxygen tensions that are lower than those typically used for cell culture and more like those of mouse tissues. These findings suggest that mesoangioblast…

ProteomicsTime FactorsPhysiologyClinical BiochemistryBiologyFibroblast growth factorCell LineMiceMembrane MicrodomainsTubulinParacrine CommunicationmedicineExtracellularAnimalsSecretionSettore BIO/06 - Anatomia Comparata E CitologiaFibroblastCytoskeletonMembrane vesicles MMP9 FGF2 mouse mesoangioblastMesoangioblastSecretory VesiclesVesicleBiological TransportMesenchymal Stem CellsCell BiologyCell biologyOxygenmedicine.anatomical_structureMatrix Metalloproteinase 9Cell cultureFibroblast Growth Factor 2Stem cellExtracellular Space
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A particular phenotype of ascending aorta aneurysms as precursor of type A aortic dissection.

2012

Objectives: We aimed to identify a phenotype of ascending thoracic aortic aneurysm (TAA), which, more than others, evolves into type A dissection (TAD). Methods: Aortic specimens were obtained from patients undergoing surgical repair of TAA and TAD (108 and 26, respectively). Histopathological and immunohistochemical analyses were performed by using adequate tissue specimens, appropriate techniques and criteria. Results: We identified the three following TAA phenotypes: phenotype I (cystic medial degeneration balanced by a substitutive fibrosis, in absence of medial apoptosis and with a faint collagenase concentration), phenotype II (cystic medial degeneration of higher grade, respectively,…

Pulmonary and Respiratory MedicineMalePathologymedicine.medical_specialtyAorta ThoracicApoptosisThoracic aortic aneurysmAortic aneurysmAneurysmFibrosismedicine.arteryAscending aortamedicineSettore MED/05 - Patologia ClinicaThoracic aortaHumansAgedAortic dissectionAortaAortic Aneurysm Thoracicbusiness.industryDissectionSettore MED/23 - Chirurgia CardiacaOriginal ArticlesMiddle Agedmedicine.diseasePrognosisAneurysmFibrosisImmunohistochemistryAortic DissectionPhenotypeMatrix Metalloproteinase 9Disease ProgressionSurgeryFemaleThoracic aortic aneurysm phenotype IIICardiology and Cardiovascular MedicinebusinessAneurysm ; Dissection ; Thoracic aortic aneurysm phenotype IIIBiomarkersInteractive cardiovascular and thoracic surgery
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Expression of gelatinases (MMP-2, MMP-9) and cyclooxygenases (COX-1, COX-2) in some benign salivary gland tumors.

2012

Salivary gland tumors, most of which are rare benign tumors, represent a histologically heterogenous group with the greatest diversity of morphological and cellular features. The aim of this study is to analyse the expression and possible interactions between gelatinases (MMP-2, MMP-9) and cyclooxygenases (COX-1, COX-2) in some benign salivary gland tumors. We investigated the expression of gelatinases and cyclooxigenases in control salivary gland, Pleomorphic adenoma and Warthin's tumor through immunohistochemistry and Reverse Transcription – Polymerase Chain Reaction (PCR). We identified the expression of both classes of enzyme in normal samples and in the two types of pathological sampl…

Settore BIO/17 - IstologiaGelatinasesPathologymedicine.medical_specialtyImmunologyAdenoma PleomorphicBiologyMatrix metalloproteinaselaw.inventionPleomorphic adenomalawSettore MED/28 - Malattie OdontostomatologichemedicineHumansImmunology and AllergyProspective StudiesPathologicalPolymerase chain reactionPharmacologySalivary glandReverse Transcriptase Polymerase Chain Reactionbenign salivary gland tumorsgelatinasescyclooxygenasesAdenolymphomaSalivary Gland Neoplasmsmedicine.diseaseImmunohistochemistryReverse transcriptasemedicine.anatomical_structureSettore MED/31 - OtorinolaringoiatriaMatrix Metalloproteinase 9Cyclooxygenase 2Cyclooxygenase 1Matrix Metalloproteinase 2Immunohistochemistry
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Matrix metalloproteinase-2 matrix metalloproteinase-9 and inducible nitric oxide synthase in oral leukoplakia: Immunohistochemistry and RT-PCR analys…

2008

Oral leukoplakia is the most common and potentially malignant disorder of the oral mucosa. The definition of leukoplakia given by the World Health Organization is "a white plaque that cannot be characterized either from a clinical or from a histopathological point of view", thus the diagnosis of leukoplakia is based on the exclusion of other lesions of the oral mucosa. We believe it is necessary to identify molecular and immunohistochemical parameters that can contribute to discriminating between the different leukoplakia clinical subtypes coded by the epidemiology. In the present work we show the preliminary results of this research project. We investigated the expression of matrix metallo…

Settore BIO/17 - IstologiaMaleMatrix Metalloproteinase 9Reverse Transcriptase Polymerase Chain ReactionHumansMatrix Metalloproteinase 2Nitric Oxide Synthase Type IIFemaleLeukoplakia OralMiddle AgedImmunohistochemistryGene Expression Regulation EnzymologicOral leukoplakia MMP-2 MMP-9 iNOS PCR analysis
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Modulation of MMP-2 and MMP-9 in Churg-Strauss syndrome respiratory mucosa: potential monitoring parameters.

2014

Churg-Strauss (CSS) syndrome is rare and of unknown etiology. It is associated with vasculitis, blood eosinophilia and granulomatosis, and affects multiple organs and systems at various stages of the disease. Specific diagnostic and monitoring tests are not yet available. This study aims to assess the changes in MMP-2 and MMP-9 along with the histopathological alterations in two cases of CSS, as possible potential diagnostic and monitoring criteria. Two adult male patients were diagnosed with CSS in the otorhinolaryngology clinic in the University of Palermo, based on multiple clinical and histopathologic criteria. Biopsies of respiratory mucosa were taken after the consent of the patients…

Settore BIO/17 - IstologiaRespiratory MucosaAdultMalemedicine.medical_specialtyPathologyAngiogenesisBiopsyImmunologyRespiratory MucosaChurg-Strauss SyndromePredictive Value of TestsmedicineImmunology and AllergyEosinophiliaHumansRNA MessengerPharmacologyMMPbusiness.industrymedicine.diseaseImmunohistochemistryUp-RegulationReal-time polymerase chain reactionMatrix Metalloproteinase 9Case-Control StudiesEtiologyImmunohistochemistryMatrix Metalloproteinase 2Histopathologymedicine.symptomVasculitisbusinessBiomarkersInternational journal of immunopathology and pharmacology
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Immunohistochemical and transcriptional expression of matrix metalloproteinases in full-term human umbilical cord and Human Umbilical Vein Endothelia…

2010

Matrix metalloproteinases (MMPs) are extracellular zinc-dependent endopeptidases involved in the degradation and remodelling of extracellular matrix in physiological and pathological processes. MMPs also have a role on cell proliferation, migration, differentiation, angiogenesis and apoptosis. Umbilical cord is a special organ subjected to many changes during pre-natal life and whose cells can maintain a certain degree of plasticity also in post-natal period; for example recently they have been used as a source of stem cells. In this work we investigated the expression of MMPs in human umbilical cord and Human Umbilical Vein Endothelial Cells (HUVEC) though immunohistochemistry, RT-PCR and …

Settore BIO/17 - IstologiaUmbilical VeinsHistologyPhysiologyAngiogenesisBiologyMatrix metalloproteinaseUmbilical cordGene Expression Regulation EnzymologicUmbilical veinUmbilical CordExtracellular matrixMatrix Metalloproteinase 10Matrix Metalloproteinase 13ExtracellularmedicineHumansCells CulturedReverse Transcriptase Polymerase Chain ReactionEndothelial CellsCell BiologyGeneral MedicineMatrix metalloproteinases human umbilical cord HUVEC.ImmunohistochemistryMatrix MetalloproteinasesCord liningCell biologyMatrix Metalloproteinase 8medicine.anatomical_structureMatrix Metalloproteinase 9ImmunologyMatrix Metalloproteinase 2Matrix Metalloproteinase 3Stem cellJournal of Molecular Histology
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Matrix metalloproteinases 2 and 9, and extracellular matrix in Kaposi's sarcoma

2010

Matrix metalloproteinases (MMPs) are associated with Kaposi's sarcoma (KS) tumorigenesis and may contribute to the mechanism of KS invasive growth. To date, only a few MMPs have been studied in KS lesions, and exactly which MMPs are involved in KS development and progression remains unanswered. However, MMPs 2 and 9 have been associated with different phases of angiogenesis, but their role in the proteolytic modification of the extracellular matrix has not been investigated. The results of this study confirm that MMPs, specifically MMP-2 and MMP-9, can contribute to angiogenesis by disrupting the vessel basement membrane and other extracellular matrix barriers, and enabling endothelial cell…

Skin NeoplasmsAngiogenesisDermatologyMatrix metalloproteinasemedicine.disease_causeBasement MembraneExtracellular matrixCell Movementmatrix metalloproteinase-9Settore MED/35 - Malattie Cutanee E VenereemedicineHumansSarcoma KaposiKaposi's sarcomaBasement membraneNeovascularization Pathologicbusiness.industryGeneral Medicinemedicine.diseaseVirologyExtracellular Matrixmedicine.anatomical_structureMatrix Metalloproteinase 9Invasive growthsarcoma of KaposiCancer researchMatrix Metalloproteinase 2SarcomaCarcinogenesisbusinessmatrix metalloproteinase- 2Dermatologic Therapy
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Nitric oxide increases the decay of matrix metalloproteinase 9 mRNA by inhibiting the expression of mRNA-stabilizing factor HuR.

2003

Dysregulation of extracellular matrix turnover is an important feature of many inflammatory processes. Rat renal mesangial cells express high levels of matrix metalloproteinase 9 (MMP-9) in response to inflammatory cytokines such as interleukin-1 beta. We demonstrate that NO does strongly destabilize MMP-9 mRNA, since different luciferase reporter gene constructs containing the MMP-9 3' untranslated region (UTR) displayed significant reduced luciferase activity in response to the presence of NO. Moreover, by use of an in vitro degradation assay we found that the cytoplasmic fractions of NO-treated cells contained a higher capacity to degrade MMP-9 transcripts than those obtained from contro…

Untranslated regionCytoplasmRNA StabilityMolecular Sequence DataGene ExpressionRNA-binding proteinBiologyKidneyNitric OxideELAV-Like Protein 1Gene expressionAnimalsElectrophoretic mobility shift assayNitric Oxide DonorsRNA MessengerEnzyme InhibitorsMolecular Biology3' Untranslated RegionsCyclic GMPCells CulturedRepetitive Sequences Nucleic AcidMessenger RNABase SequenceThree prime untranslated regionMolecular MimicryRNARNA-Binding ProteinsCell BiologyMolecular biologyRecombinant ProteinsRatsELAV ProteinsMatrix Metalloproteinase 9RibonucleoproteinsGuanylate CyclaseAntigens SurfaceAminoquinolinesDactinomycinSoluble guanylyl cyclaseInterleukin-1Nitroso CompoundsMolecular and cellular biology
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Receptor for advanced glycation end products is subjected to protein ectodomain shedding by metalloproteinases.

2008

The receptor for advanced glycation end products (RAGE) is a 55-kDa type I membrane glycoprotein of the immunoglobulin superfamily. Ligand-induced up-regulation of RAGE is involved in various pathophysiological processes, including late diabetic complications and Alzheimer disease. Application of recombinant soluble RAGE has been shown to block RAGE-mediated pathophysiological conditions. After expression of full-length RAGE in HEK cells we identified a 48-kDa soluble RAGE form (sRAGE) in the culture medium. This variant of RAGE is smaller than a 51-kDa soluble version derived from alternative splicing. The release of sRAGE can be induced by the phorbol ester PMA and the calcium ionophore c…

endocrine system diseasesADAM10Receptor for Advanced Glycation End ProductsMatrix Metalloproteinase InhibitorsHydroxamic AcidsBiochemistryProtein biotinylationCell LineDiabetes ComplicationsADAM10 ProteinGlycationAlzheimer DiseaseHumansProtein IsoformsProtease Inhibitorscardiovascular diseasesRNA Small InterferingReceptors ImmunologicReceptorMolecular BiologyProtein kinase CCalcimycinIonophoresChemistryHEK 293 cellsCell Membranenutritional and metabolic diseasesMembrane ProteinsCell BiologyProtein Structure TertiaryADAM ProteinsAlternative SplicingEctodomainBiochemistryMatrix Metalloproteinase 9cardiovascular systemCarcinogensImmunoglobulin superfamilyTetradecanoylphorbol AcetateAmyloid Precursor Protein Secretaseshuman activitiesThe Journal of biological chemistry
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