Search results for "Tissue inhibitor of metalloproteinase"

showing 6 items of 46 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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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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Cigarette smoke exposure inhibits extracellular MMP-2 (gelatinase A) activity in human lung fibroblasts

2007

Abstract Background Exposure to cigarette smoke is considered a major risk factor for the development of lung diseases, since its causative role has been assessed in the induction and maintenance of an inflamed state in the airways. Lung fibroblasts can contribute to these processes, due to their ability to produce proinflammatory chemotactic molecules and extracellular matrix remodelling proteinases. Among proteolytic enzymes, gelatinases A and B have been studied for their role in tissue breakdown and mobilisation of matrix-derived signalling molecules. Multiple reports linked gelatinase deregulation and overexpression to the development of inflammatory chronic lung diseases such as COPD.…

Pulmonary and Respiratory MedicineGelatinase ABiologyMatrix metalloproteinaseProinflammatory cytokineExtracellular matrixExtracellularHumansGelatinaseRNA MessengerLungCells Culturedlcsh:RC705-779Cell DeathPlant ExtractsResearchProteolytic enzymessmoke MMP-2Tissue Inhibitor of MetalloproteinasesEnvironmental Exposurelcsh:Diseases of the respiratory systemEnvironmental exposureFibroblastsrespiratory systemrespiratory tract diseasesCulture Media ConditionedImmunologyMatrix Metalloproteinase 2Tobacco Smoke PollutionEnvironmental MonitoringRespiratory Research
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Behaviour of the plasma concentration of gelatinases and their tissue inhibitors in subjects with venous leg ulcers.

2015

Venous leg ulcers are common in subjects with chronic venous insufficiency. The increased intraluminal pressure causes alteration of the skin microcirculation, leukocyte activation and release of proteolytic enzymes leading to ulceration. An impaired expression and activity of matrix metalloproteases (MMPs) and their tissue inhibitors (TIMPs) might influence extracellular matrix degradation and deposition in chronic venous ulcers with the failure of the healing process. Our aim was to evaluate plasma concentration of gelatinases (MMP-2 and MMP-9) and their inhibitors (TIMP-1 and TIMP-2) in subjects with venous leg ulcers before and after the compression therapy. We enrolled 36 subjects (12 …

Ulcer healingMalemedicine.medical_specialtyGelatinasesSettore MED/09 - Medicina InternaPhysiologyChronic venous insufficiencyMatrix metalloproteinaseGastroenterologyMicrocirculationVaricose UlcerTIMP-2TIMP-1Physiology (medical)Internal medicinemedicineHumansAgedTissue Inhibitor of Metalloproteinase-2Tissue Inhibitor of Metalloproteinase-1MMP-2business.industryMMP-2; MMP-9; TIMP-1; TIMP-2; Venous leg ulcersLeg UlcerProteolytic enzymesHematologyVenous bloodmedicine.diseaseMatrix MetalloproteinasesSurgeryVenous leg ulcersVenous InsufficiencyGelatinasesPlasma concentrationMatrix Metalloproteinase 2FemaleMMP-9Cardiology and Cardiovascular Medicinebusiness
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NephroCheck: should we consider urine osmolality?

2019

medicine.medical_specialtyLetterCritical Care030232 urology & nephrologyMEDLINEUrine030204 cardiovascular system & hematologyCritical Care and Intensive Care MedicineAcute Kidney Injury; Biomarkers Humans Insulin-Like Growth Factor Binding Proteins Research Design Tissue Inhibitor of Metalloproteinase-2 Urine Osmolar ConcentrationOsmolar Concentration03 medical and health sciences0302 clinical medicinemedicineHumansTissue Inhibitor of Metalloproteinase-2Intensive Care Medicinebusiness.industryOsmolar Concentrationlcsh:Medical emergencies. Critical care. Intensive care. First aidlcsh:RC86-88.9Acute Kidney InjuryInsulin-Like Growth Factor Binding ProteinsResearch DesignEmergency medicineUrine osmolalitybusinessBiomarkersCritical Care
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Acute exercise induced changes in rat skeletal muscle mRNAs and proteins regulating type IV collagen content

2001

This experiment tested the hypothesis that running-induced damage to rat skeletal muscle causes changes in synthesis and degradation of basement membrane type IV collagen and to proteins regulating its degradation. Samples from soleus muscle and red and white parts of quadriceps femoris muscle (MQF) were collected 6 h or 1, 2, 4, or 7 days after downhill running. Increased muscle β-glucuronidase activity indicated greater muscle damage in the red part of MQF than in the white part of MQF or soleus. In the red part of MQF, type IV collagen expression was upregulated at the pretranslational level and the protein concentration decreased, whereas matrix metalloproteinase-2 (MMP-2), a protein th…

medicine.medical_specialtyTime FactorsTranscription GeneticPhysiologyPhysical ExertionMatrix metalloproteinaseBiologyRunningType IV collagenPhysiology (medical)Internal medicineGene expressionmedicineAnimalsRNA MessengerRats WistarMuscle SkeletalGlucuronidaseSoleus muscleBasement membranechemistry.chemical_classificationTissue Inhibitor of Metalloproteinase-2Tissue Inhibitor of Metalloproteinase-1Skeletal muscleTissue inhibitor of metalloproteinaseRatsmedicine.anatomical_structureEndocrinologyGene Expression RegulationMatrix Metalloproteinase 9chemistryProtein BiosynthesisMuscle Fibers Fast-TwitchMatrix Metalloproteinase 2FemaleCollagenGlycoproteinAmerican Journal of Physiology-Regulatory, Integrative and Comparative Physiology
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