Search results for "metalloproteinases"

showing 10 items of 83 documents

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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TIMP-3 facilitates binding of target metalloproteinases to the endocytic receptor LRP-1 and promotes scavenging of MMP-1.

2020

AbstractMatrix metalloproteinases (MMPs) and the related families of disintegrin metalloproteinases (ADAMs) and ADAMs with thrombospondin repeats (ADAMTSs) play a crucial role in extracellular matrix (ECM) turnover and shedding of cell-surface molecules. The proteolytic activity of metalloproteinases is post-translationally regulated by their endogenous inhibitors, known as tissue inhibitors of metalloproteinases (TIMPs). Several MMPs, ADAMTSs and TIMPs have been reported to be endocytosed by the low-density lipoprotein receptor-related protein-1 (LRP-1). Different binding affinities of these proteins for the endocytic receptor correlate with different turnover rates which, together with di…

Cell biologyTIMP-3 LRP-1 MMP-1 extracellular matrix endocytosis metalloproteinases endocytic receptorlcsh:MedicinePlasma protein bindingMatrix metalloproteinaseBiochemistryArticleExtracellular matrixDisintegrinHumanslcsh:ScienceReceptorTissue Inhibitor of Metalloproteinase-3MetalloproteinaseThrombospondinMultidisciplinarybiologyChemistrylcsh:RLigand (biochemistry)EndocytosisMatrix MetalloproteinasesCell biologyKineticsMultiprotein Complexesbiology.proteinlcsh:Qlipids (amino acids peptides and proteins)Matrix Metalloproteinase 1Low Density Lipoprotein Receptor-Related Protein-1Protein BindingScientific reports
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Vascular Microarchitecture of Murine Colitis-Associated Lymphoid Angiogenesis

2009

In permissive tissues, such as the gut and synovium, chronic inflammation can result in the ectopic development of anatomic structures that resemble lymph nodes. These inflammation-induced structures, termed lymphoid neogenesis or tertiary lymphoid organs, may reflect differential stromal responsiveness to the process of lymphoid neogenesis. To investigate the structural reorganization of the microcirculation involved in colonic lymphoid neogenesis, we studied a murine model of dextran sodium sulfate (DSS)-induced colitis. Standard 2-dimensional histology demonstrated both submucosal and intramucosal lymphoid structures in DSS-induced colitis. A spatial frequency analysis of serial histolog…

Colitis LymphocyticPathologymedicine.medical_specialtyHistologyStromal cellLymphoid TissueAngiogenesisBiologyArticleMicrocirculationMicemedicineAnimalsIntestinal MucosaColoring AgentsEcology Evolution Behavior and SystematicsMicrodissectionMicroscopy ConfocalNeovascularization PathologicStaining and LabelingMicrocirculationDextran SulfateHistologyMatrix MetalloproteinasesCapillariesMice Inbred C57BLDisease Models AnimalLymphatic systemRegional Blood FlowCytokinesLymphChemokinesAnatomyIntravital microscopyBiotechnologyThe Anatomical Record: Advances in Integrative Anatomy and Evolutionary Biology
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Vitamin A deficiency disturbs collagen IV and laminin composition and decreases matrix metalloproteinase concentrations in rat lung. Partial reversib…

2011

Vitamin A is essential for lung development and pulmonary cell differentiation. Its deficiency leads to altered lung structure and function and to basement membrane architecture and composition disturbances. Previously, we showed that lack of retinoids thickens the alveolar basement membrane and increases collagen IV, which are reversed by retinoic acid, the main biologically active vitamin A form. This study analyzed how vitamin A deficiency affects the subunit composition of collagen IV and laminin of lung basement membranes and pulmonary matrix metalloproteinase content, plus the recovering effect of all-trans-retinoic acid. Male weanling pups were fed a retinol-adequate/-deficient diet …

Collagen Type IVMaleVitaminmedicine.medical_specialtyEndocrinology Diabetes and MetabolismClinical BiochemistryRetinoic acidGene ExpressionTretinoinMatrix metalloproteinaseBiochemistryBasement Membranechemistry.chemical_compoundLamininInternal medicineGene expressionmedicineAnimalsRats WistarVitamin ALungMolecular BiologyBasement membraneNutrition and DieteticsLungbiologyVitamin A DeficiencyTissue Inhibitor of Metalloproteinasesmedicine.diseaseMatrix MetalloproteinasesRatsVitamin A deficiencymedicine.anatomical_structureEndocrinologyBiochemistrychemistrybiology.proteinFemaleLamininThe Journal of Nutritional Biochemistry
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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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Role of the Netrin-like Domain of Procollagen C-Proteinase Enhancer-1 in the Control of Metalloproteinase Activity

2010

The netrin-like (NTR) domain is a feature of several extracellular proteins, most notably the N-terminal domain of tissue inhibitors of metalloproteinases (TIMPs), where it functions as a strong inhibitor of matrix metalloproteinases and some other members of the metzincin superfamily. The presence of a C-terminal NTR domain in procollagen C-proteinase enhancers (PCPEs), proteins that stimulate the activity of astacin-like tolloid proteinases, raises the possibility that this might also have inhibitory activity. Here we show that both long and short forms of the PCPE-1 NTR domain, the latter beginning at the N-terminal cysteine known to be critical for TIMP activity, show no inhibition, at …

Glycobiology and Extracellular MatricesMatrix metalloproteinaseBiochemistryBONE MORPHOGENETIC PROTEIN-1AdamalysinFIBRILLAR PROCOLLAGENSTolloid ProteinaseExtracellular Matrix Proteins0303 health sciencesADAMTSFRIZZLED-RELATED PROTEINS030302 biochemistry & molecular biologyTissue Inhibitor of Metalloproteinases11 Medical And Health SciencesALPHA-CONVERTING-ENZYMEI PROCOLLAGENADAM ProteinsExtracellular MatrixPLASMINOGEN ACTIVATIONBiochemistryCollagen03 Chemical SciencesLife Sciences & BiomedicineProcollagenBiochemistry & Molecular BiologyTERMINAL DOMAINTolloid-Like MetalloproteinasesADAMTSBiologyBone morphogenetic protein 1Cell Line03 medical and health sciencesDisintegrinHumansHUMAN TISSUE INHIBITORMatrix MetalloproteinaseMolecular BiologyGlycoproteins030304 developmental biologyThrombospondinScience & TechnologyHeparinADAMCell Biology06 Biological SciencesMATRIX-METALLOPROTEINASESProtein Structure TertiaryADAM ProteinsProcollagen peptidaseSULFATED GLYCOSAMINOGLYCANSEnzymologybiology.proteinJournal of Biological Chemistry
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Mutant p53 gain of function can be at the root of dedifferentiation of human osteosarcoma MG63 cells into 3AB-OS cancer stem cells

2014

Osteosarcoma is a highly metastatic tumor affecting adolescents, for which there is no second-line chemotherapy. As suggested for most tumors, its capability to overgrow is probably driven by cancer stem cells (CSCs), and finding new targets to kill CSCs may be critical for improving patient survival. TP53 is the most frequently mutated tumor suppressor gene in cancers and mutant p53 protein (mutp53) can acquire gain of function (GOF) strongly contributing to malignancy. Studies thus far have not shown p53-GOF in osteosarcoma. Here, we investigated TP53 gene status/role in 3AB-OS cells-a highly aggressive CSC line previously selected from human osteosarcoma MG63 cells-to evaluate its involv…

HistologyTumor suppressor genePhysiologyEndocrinology Diabetes and MetabolismApoptosisIn situ hybridizationBiologyTNF-Related Apoptosis-Inducing LigandCell MovementCancer stem cellCell Line TumorSettore BIO/10 - BiochimicaBiomarkers TumormedicineHumansNeoplasm Invasiveness3AB-OS cells CSCs Cancer cell dedifferentiation Cancer stem cells FISH Fluorescent in situ hybridization GOF Gain of function Human osteosarcoma MMPs Matrix metalloproteinases Mutant p53 Mutant p53 gain of function Mutp53 OS OsteosarcomaClonogenic assayTumor Stem Cell AssayCell ProliferationMembrane Potential MitochondrialOsteosarcomaCancerReceptors Death DomainCell DedifferentiationCell cyclemedicine.diseaseMolecular biologyAmino Acid SubstitutionProto-Oncogene Proteins c-bcl-2Gene Knockdown TechniquesMutationNeoplastic Stem CellsCancer researchOsteosarcomaEctopic expressionTumor Suppressor Protein p53Bone
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Intramuscular Extracellular Matrix: Complex Environment of Muscle Cells

2002

KOVANEN, V. Intramuscular extracellular matrix: Complex environment of muscle cells. Exerc. Sport Sci. Rev., Vol. 30, No. 1, pp 20–25, 2002. Different collagen types among other extracellular matrix molecules, remodeling of the extracellular matrix with the aid of matrix metalloproteinases, and inte

IntegrinsChemistryFibrillar CollagensPhysical Therapy Sports Therapy and RehabilitationNon-Fibrillar CollagensExtracellular matrix moleculesMatrix metalloproteinaseBasement MembraneMatrix MetalloproteinasesExtracellular MatrixCell biologyExtracellular matrixHumansMyocyteOrthopedics and Sports MedicineMuscle SkeletalExercise and Sport Sciences Reviews
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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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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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