Search results for "Matrix Metalloproteinase 3"

showing 4 items of 14 documents

Meprins process matrix metalloproteinase-9 (MMP-9)/gelatinase B and enhance the activation kinetics by MMP-3

2012

Abstract Meprin α and β, members of the astacin family of zinc metalloproteinases, are unique plasma membrane and secreted proteases known to cleave a wide range of biological substrates involved in inflammation, cancer and fibrosis. In this study, we identified proMMP-9 as a novel substrate and show that aminoterminal meprin-mediated clipping improves the activation kinetics of proMMP-9 by MMP-3, an efficient activator of proMMP-9. Interestingly, the NH2-terminus LVLFPGDL, generated by incubation with meprin α, is identical to the form produced in conditioned media from human neutrophils and monocytes. Hence, this meprin-mediated processing and enhancement of MMP-9 activation kinetics may …

ProteasesNeutrophilsMolecular Sequence DataBiophysicsMatrix metalloproteinaseBiochemistryMonocytesProtein–protein interactionAminoterminal cleavageStructural BiologyGeneticsHumansProMMP-9ZymographyAmino Acid SequenceMolecular BiologyCells Culturedchemistry.chemical_classificationChemistryActivator (genetics)TioproninMeprinCell BiologyTissue inhibitor of metalloproteinaseEnzymeMatrix Metalloproteinase 9BiochemistryCulture Media ConditionedMatrix Metalloproteinase 3AstacinFEBS Letters
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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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Cross-talk between Different Enhancer Elements during Mitogenic Induction of the Human Stromelysin-1 Gene

1996

Platelet-derived growth factor (PDGF) induces the expression of human stromelysin-1, a matrix metalloproteinase involved in tumor invasion and metastasis. Here it is shown that stromelysin-1 gene induction by PDGF depends on Ras and involves three previously identified promoter elements (the stromelysin-1 PDGF-responsive element (SPRE) site, the two head-to-head polyomavirus enhancer A-binding protein-3 (PEA3) sites, and the activator protein-1 (AP-1) binding site). During mitogenic induction, these responsive elements appear to be organized in two independent transcriptional units, SPRE-AP-1 and PEA3-AP-1, which result from specific element cross-talking. Interestingly, expression of a dom…

Transcription GeneticProto-Oncogene Proteins c-junMolecular Sequence DataProtein Serine-Threonine KinasesBiologyTransfectionBiochemistryStromelysin 1Proto-Oncogene Proteins p21(ras)MiceProto-Oncogene ProteinsAnimalsHumansBinding siteEnhancerMolecular BiologyTranscription factorGeneProtein Kinase CProtein kinase CPlatelet-Derived Growth FactorBase SequenceActivator (genetics)Metalloendopeptidases3T3 CellsCell BiologyMolecular biologyRecombinant ProteinsDNA-Binding ProteinsProto-Oncogene Proteins c-rafTranscription Factor AP-1Enhancer Elements GeneticEnzyme Inductionbiology.proteinMatrix Metalloproteinase 3MitogensPlatelet-derived growth factor receptorJournal of Biological Chemistry
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Effects of BIS076 in a model of osteoarthritis induced by anterior cruciate ligament transection in ovariectomised rats

2015

Background Osteoarthritis (OA) is the most frequent articular disease and a leading cause of disability. There is a need for effective treatments able to slow the progression of disease. Some of the available treatments are dietary supplements providing natural components. Recent studies have shown that estrogen deficiency contributes to the pathophysiological events of OA progression. Methods We have used the anterior cruciate ligament transection model of OA in ovariectomised rats to study the effects of BIS076, a new formulation of a natural porcine cartilage extract associated with hydroxyapatite (as a source of calcium) and vitamin D3. Cartilage degradation, proteoglycan depletion and …

medicine.medical_specialtySwineOvariectomyType II collagenOsteoarthritisCartilage Oligomeric Matrix ProteinBIS076DinoprostoneBone remodelingRheumatologyOsteoprotegerinInternal medicineOsteoarthritismedicineAnimalsOrthopedics and Sports MedicineRats WistarVitamin DCollagen Type IIGlycosaminoglycansBone mineralCartilage oligomeric matrix proteinbiologybusiness.industryTissue ExtractsCartilageAnterior Cruciate Ligament InjuriesArticular cartilage damageOsteoarthritis Kneemedicine.diseasePeptide FragmentsSurgeryRatsDisease Models Animalmedicine.anatomical_structureEndocrinologyDurapatiteTreatment Outcomebiology.proteinAnterior cruciate ligament transection modelCytokinesFemaleMatrix Metalloproteinase 3businessOvariectomised ratsBiomarkersResearch ArticleBMC Musculoskeletal Disorders
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