Search results for "Matrix metalloproteinase"

showing 10 items of 212 documents

Endothelial cell-matrix interactions.

2002

Dynamic interactions between endothelial cells and components of their surrounding extracellular matrix are necessary for the invasion, migration, and survival of endothelial cells during angiogenesis. These interactions are mediated by matrix receptors that initiate intracellular signaling cascades in response to binding to specific extracellular matrix molecules. The interactions between endothelial cells and their environment are also modulated by enzymes that degrade different matrix components and thus enable endothelial invasion. Recent reports on gene targeting in mice have confirmed the role of two classes of matrix receptors, integrins and cell surface heparan sulfate proteoglycans…

IntegrinsHistologybiologyNeovascularization PathologicAngiogenesisIntegrinProteolytic enzymesNeovascularization PhysiologicMatrix (biology)Matrix metalloproteinaseMatrix MetalloproteinasesCell biologyExtracellular MatrixExtracellular matrixEndothelial stem cellFibronectinMedical Laboratory TechnologyMicebiology.proteinAnimalsHumansEndothelium VascularAnatomyInstrumentationHeparan Sulfate ProteoglycansMicroscopy research and technique
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Transcription of α2 Integrin Gene in Osteosarcoma Cells Is Enhanced by Tumor Promoters

1998

Integrin alpha2beta1 is a heterodimeric transmembrane receptor for collagens. In osteogenic cells the expression of alpha2beta1 integrin is induced by both Kirsten sarcoma virus and chemical transformation. The association of alpha2 integrin with transformed cell phenotype was studied further by testing the effects of two tumor promoters, 12-O-tetradecanoylphorbol 13-acetate (TPA) and okadaic acid (OA), on human MG-63 osteosarcoma cells. TPA, an activator of protein kinase C, increased the cell surface expression of alpha2 integrin and the corresponding mRNA levels. Nuclear run-on assays indicated that TPA activated the transcription of alpha2 integrin gene. TPA also slightly increased the …

IntegrinsTime FactorsTranscription GeneticIntegrin alpha3IntegrinIntegrin alpha2CD18Integrin alpha5CD49cCD49bCollagen receptorAntigens CDOkadaic AcidCell AdhesionTumor Cells CulturedHumansCollagenasesRNA MessengerOsteosarcomabiologyActivator (genetics)Integrin beta1Cell BiologyIntegrin alphaVBlotting NorthernFlow CytometryMolecular biologyUp-RegulationIntegrin alpha MCarcinogensbiology.proteinTetradecanoylphorbol AcetateIntegrin beta 6CollagenMatrix Metalloproteinase 1Experimental Cell Research
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The Dorsocross T-box transcription factors promote tissue morphogenesis in the Drosophila wing imaginal disc.

2012

The Drosophila wing imaginal disc is subdivided into notum, hinge and blade territories during the third larval instar by formation of several deep apical folds. The molecular mechanisms of these subdivisions and the subsequent initiation of morphogenic processes during metamorphosis are poorly understood. Here, we demonstrate that the Dorsocross (Doc) T-box genes promote the progression of epithelial folds that not only separate the hinge and blade regions of the wing disc but also contribute to metamorphic development by changing cell shapes and bending the wing disc. We found that Doc expression was restricted by two inhibitors, Vestigial and Homothorax, leading to two narrow Doc stripes…

Integrinsanimal structuresTime FactorsMorphogenesisBiologyMicrotubulesExtracellular matrixMicrotubuleMorphogenesisAnimalsDrosophila ProteinsWings AnimalTransgenesMolecular BiologyAllelesWingAnatomyNotumCell biologyExtracellular MatrixImaginal discT-boxDrosophila melanogasterMutationMatrix Metalloproteinase 2RNA InterferenceDrosophila ProteinDevelopmental BiologyProtein BindingSignal TransductionTranscription FactorsDevelopment (Cambridge, England)
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Regulation of ghrelin receptor by microbial and inflammatory signals in human osteoblasts

2019

Made available in DSpace on 2019-10-06T16:29:44Z (GMT). No. of bitstreams: 0 Previous issue date: 2019-04-25. Added 1 bitstream(s) on 2019-10-09T18:35:25Z : No. of bitstreams: 1 S1806-83242019000100221.pdf: 2536737 bytes, checksum: 9a25b4f5849a4b7f35298e8e3e000889 (MD5) Recently, it has been suggested that the anti-inflammatory hormone ghrelin (GHRL) and its receptor GHS-R may play a pivotal role in periodontal health and diseases. However, their exact regulation and effects in periodontitis are not known. The aim of this in-vitro study was to investigate the effect of microbial and inflammatory insults on the GHS-R1a expression in human osteoblast-like cells. MG-63 cells were exposed to in…

Interleukin-1betaImmunocytochemistry610 Medicine & healthMatrix metalloproteinaseReal-Time Polymerase Chain ReactionStatistics NonparametricProinflammatory cytokine03 medical and health sciences0302 clinical medicineDownregulation and upregulationHumansGeneral Materials Science030212 general & internal medicineReceptor610 Medicine & healthReceptors GhrelinPeriodontitisCells CulturedAnalysis of VarianceOsteoblastsbiologyFusobacterium nucleatumChemistryInterleukin030206 dentistrybiology.organism_classificationImmunohistochemistryGhrelinUp-RegulationCell biologylcsh:RK1-715stomatognathic diseasesMicroscopy Fluorescencelcsh:DentistryGhrelinFusobacterium nucleatumhormones hormone substitutes and hormone antagonists
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Depletion of alphaV integrins from osteosarcoma cells by intracellular antibody expression induces bone differentiation marker genes and suppresses g…

1999

Integrin heterodimers sharing the common alphaV subunit are receptors for adhesion glycoproteins such as vitronectin and fibronectin. They are suggested to play an essential role in cell anchoring, differentiation, and survival. Here, we describe the construction of an expression plasmid coding for an intracellular single-chain antibody against alphaV integrin subunit. Saos-2 osteosarcoma cells transfected with this DNA construct showed an approximately 70-100% decrease in the cell surface expression of alphaVbeta3 and alphaVbeta5 integrins as shown by flow cytometry. Intracellular antibody expression had no effect on the mRNA levels of alphaV integrin. Pulse chase experiments of metabolica…

Intracellular FluidSialoglycoproteinsCellIntegrinBone and Bones03 medical and health sciences0302 clinical medicineAntigens CDmedicineCell AdhesionTumor Cells CulturedHumansOsteopontinVitronectinMolecular BiologyImmunoglobulin Fragments030304 developmental biologyGlycoproteins0303 health sciencesOsteosarcomabiologyOsteoblastCell DifferentiationTransfectionIntegrin alphaVAlkaline PhosphataseMolecular biologyFibronectinsFibronectinmedicine.anatomical_structure030220 oncology & carcinogenesisEnzyme Inductionbiology.proteinMatrix Metalloproteinase 2VitronectinOsteopontinIntracellularBiomarkersMatrix biology : journal of the International Society for Matrix Biology
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Processing of procollagen III by meprins: new players in extracellular matrix assembly?

2010

Meprins α and β, a subgroup of zinc metalloproteinases belonging to the astacin family, are known to cleave components of the extracellular matrix, either during physiological remodeling or in pathological situations. In this study we present a new role for meprins in matrix assembly, namely the proteolytic processing of procollagens. Both meprins α and β release the N- and C-propeptides from procollagen III, with such processing events being critical steps in collagen fibril formation. In addition, both meprins cleave procollagen III at exactly the same site as the procollagen C-proteinases, including bone morphogenetic protein-1 (BMP-1) and other members of the tolloid proteinase family. …

Keratinocytesmacromolecular substancesDermatologyMatrix metalloproteinaseCleavage (embryo)BiochemistryBone Morphogenetic Protein 1Substrate SpecificityExtracellular matrix03 medical and health sciencesDermismedicineHumansEnhancerMolecular BiologyCells Cultured030304 developmental biology0303 health sciencesExtracellular Matrix Proteinsintegumentary systemChemistryExtracellular matrix assembly030302 biochemistry & molecular biologyMetalloendopeptidasesCell BiologyDermisFibroblastsFibrosisProcollagen peptidasemedicine.anatomical_structureCollagen Type IIIHEK293 CellsBiochemistryKeloidAstacinThe Journal of investigative dermatology
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Collagenolytic proteinases in keratoconus.

2006

To study the proteolytic phenomena contributing to the pathogenesis of keratoconus, corneal enzymes with potential to cleave fibrillar collagen were studied.Immunohistochemical labeling was undertaken of conventional and novel mammalian collagenases (MMP-1, -2, -8, -13, and -14) of the matrix metalloproteinase (MMP) family and other collagenolytic proteinases of the serine (human trypsin-2) and cysteine (cathepsin K) endoproteinase families. The results were analyzed using a semiquantitative scoring system.Labeling of MMP-8 was moderate in healthy controls, but weak in keratoconus. Moderate MMP-2 and weak MMP-14 expressions were similar in controls and keratoconus. MMP-1 was slightly overex…

KeratoconusPathologymedicine.medical_specialtygenetic structuresCathepsin KMatrix metalloproteinaseKeratoconusPathogenesisCorneaImmunoenzyme TechniquesCorneamedicineCathepsin KHumansTrypsinCollagenaseschemistry.chemical_classificationmedicine.diseaseCathepsinseye diseasesMatrix MetalloproteinasesOphthalmologyEnzymemedicine.anatomical_structurechemistryCollagenaseTrypsinogenImmunohistochemistrysense organsKeratoplasty Penetratingmedicine.drugCornea
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Tissue inhibitor of metalloproteinases-2 (TIMP-2) in rat liver cells is increased by lipopolysaccharide and prostaglandin E2

1995

AbstractTo explore the functional role of TIMP-2 in liver, we determined TIMP-2 mRNA levels in primary rat hepatocytes and in total rat liver. Rat hepatocytes constitutively express TIMP-2 mRNA at a low level. Incubation with dexamethasone, prostaglandin E2 and a combination of inflammatory cytokines leads to an up-regulation of TIMP-2 mRNA. In rats in vivo we found a dramatic increase of TIMP-2 expression after intraperitoneal injection of lipopolysaccharide. Compared to our previous findings on TIMP-1 we conclude that TIMP-2 mRNA expression is regulated in a distinct and partially opposite manner. Over-production of TIMP-2 could inhibit the activity of metalloproteinases and thus lead to …

Lipopolysaccharidesmedicine.medical_specialtyLipopolysaccharidemedicine.medical_treatmentInflammatory mediatorIntraperitoneal injectionBiophysicsTissue inhibitor of metalloproteinaseMatrix metalloproteinaseBiochemistryDexamethasoneDinoprostoneCell LineProinflammatory cytokineMicechemistry.chemical_compoundStructural BiologyFibrosisIn vivoInternal medicineGeneticsmedicineAnimalsHumansRNA MessengerProstaglandin E2Molecular BiologyCells CulturedTissue Inhibitor of Metalloproteinase-2ChemistryMetalloendopeptidasesProteinsExtracellular matrixCell BiologyTissue inhibitor of metalloproteinasemedicine.diseaseFibrosisRatsEndocrinologyGene Expression RegulationLiverProtein BiosynthesisCytokinesRat hepatocytemedicine.drug
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Manganese overload affects p38 MAPK phosphorylation and metalloproteinase activity during sea urchin embryonic development.

2014

Abstract In the marine environment, manganese represents a potential emerging contaminant, resulting from an increased production of manganese-containing compounds. In earlier reports we found that the exposure of Paracentrotus lividus sea urchin embryos to manganese produced phenotypes with no skeleton. In addition, manganese interfered with calcium uptake, perturbed extracellular signal-regulated kinase (ERK) signaling, affected the expression of skeletogenic genes, and caused an increase of the hsc70 and hsc60 protein levels. Here, we extended our studies focusing on the temporal activation of the p38 mitogen-activated protein kinase (p38 MAPK) and the proteolytic activity of metalloprot…

MAPK/ERK pathwayEmbryo NonmammalianAquatic ScienceBiologyMatrix metalloproteinaseOceanographyp38 Mitogen-Activated Protein KinasesParacentrotus lividusbiology.animalECM ERK Embryo-toxicity Immunoblotting MAPK MMPs Marine organisms' calcification Mn SDS-PAGE Zymography extracellular matrix extracellular signal-regulated kinase manganese metalloproteinases mitogen-activated protein kinase p38 MAPK sodium dodecyl sulfate-polyacrylamide gel electrophoresisAnimalsSettore BIO/06 - Anatomia Comparata E CitologiaPhosphorylationProtein kinase ASea urchinManganeseKinaseGeneral Medicinebiology.organism_classificationPollutionMatrix MetalloproteinasesBiochemistryMitogen-activated protein kinasebiology.proteinParacentrotusPhosphorylationWater Pollutants ChemicalMarine environmental research
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Induction of collagenase-3 (MMP-13) expression in human skin fibroblasts by three-dimensional collagen is mediated by p38 mitogen-activated protein k…

1999

Collagenase-3 (matrix metalloproteinase-13, MMP-13) is a recently identified human MMP with an exceptionally wide substrate specificity and restricted tissue-specific expression. Here we show that MMP-13 expression is induced in normal human skin fibroblasts cultured within three-dimensional collagen gel resulting in production and proteolytic activation of MMP-13. Induction of MMP-13 mRNAs by collagen gel was potently inhibited by blocking antibodies against alpha1 and alpha2 integrin subunits and augmented by activating antibody against beta1 integrin subunit, indicating that both alpha1 beta1 and alpha2 beta1 integrins mediate the MMP-13-inducing cellular signal generated by three-dimens…

MAPK/ERK pathwayIntegrinsReceptors CollagenSB 203580IntegrinDown-RegulationBiologyBiochemistryp38 Mitogen-Activated Protein KinasesCollagen receptorIntegrin alpha1beta1chemistry.chemical_compoundTransforming Growth Factor betaMatrix Metalloproteinase 13medicineHumansCollagenasesProtein kinase AMolecular BiologyDNA PrimersSkinBase SequenceKinaseTumor Necrosis Factor-alphaCell BiologyFibroblastsProtein-Tyrosine KinasesMolecular biologyEnzyme ActivationchemistryCalcium-Calmodulin-Dependent Protein KinasesCollagenasebiology.proteinCollagenMitogen-Activated Protein KinasesTyrosine kinasemedicine.drugInterleukin-1The Journal of biological chemistry
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