Search results for "gelatinase"

showing 10 items of 31 documents

The gelatinase MMP-9like is involved in regulation of LPS inflammatory response in Ciona robusta

2019

Matrix metalloproteinases (MMPs) are a family of endopeptidases collectively able to degrade the components of the extracellular matrix (ECM), with important roles in many biological processes, such as embryogenesis, normal tissue remodelling, angiogenesis and wound healing. New views on the function of MMPs reveal that they regulate inflammatory response and therefore might represent an early step in the evolution of the immune system. MMPs can affect the activity of cytokines involved in inflammation including TGF-β and TNF-α. MMPs are widely distributed in all kingdoms of life and have likely evolved from a single-domain protein which underwent successive rounds of duplications. In this …

0301 basic medicineLipopolysaccharidesModels MolecularAngiogenesisSettore BIO/05 - ZoologiaInflammationAquatic ScienceMatrix metalloproteinaseExtracellular matrixCiona robustaMatrix metalloproteinases (MMPs)MMP-2MMP-9PharynxInflammationLPS03 medical and health sciencesDownregulation and upregulationTransforming Growth Factor betamedicineEnvironmental ChemistryGelatinaseAnimalsCiona intestinalisPhylogenyInflammationbiologyTumor Necrosis Factor-alphafungi04 agricultural and veterinary sciencesGeneral Medicinebiology.organism_classificationMatrix MetalloproteinasesCell biologyCiona intestinalis030104 developmental biologyGelatinases040102 fisheries0401 agriculture forestry and fisheriesmedicine.symptomWound healing
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Propeptide glycosylation and galectin‐3 binding decrease proteolytic activation of human proMMP‐9/progelatinase B

2019

Matrix metalloproteinases (MMPs) are secreted as proenzymes, containing propeptides that interact with the catalytic zinc, thereby controlling MMP activation. The MMP‐9 propeptide is unique in the MMP family because of its post‐translational modification with an N‐linked oligosaccharide. ProMMP‐9 activation by MMP‐3 occurs stepwise by cleavage of the propeptide in an aminoterminal (pro‐AT) and carboxyterminal (pro‐CT) peptide. We chemically synthesized aglycosyl pro‐AT and pro‐CT and purified recombinant glycosylated pro‐ATS f−9. First, we report new cleavage sites in the MMP‐9 propeptide by MMP‐3 and neutrophil elastase. Additionally, we demonstrated with the use of western blot analysis a…

0301 basic medicinePNGase FN-linked glycosylationGlycosylationGlycosylationmatrix metalloproteinase‐9Galectin 3GalectinsProteolysisgalectin‐3Biochemistry03 medical and health scienceschemistry.chemical_compoundCongenital Disorders of Glycosylation0302 clinical medicineN-linked glycosylationmatrix metalloproteinase-9galectin-3medicineHumansZymographyAmino Acid SequenceProtein precursorMolecular BiologyN‐linked glycosylationEnzyme Precursorspropeptidemedicine.diagnostic_testbiologyBlood ProteinsOriginal ArticlesCell BiologyTrypsinEnzyme Activation030104 developmental biologyMatrix Metalloproteinase 9chemistryBiochemistryGelatinasesCase-Control Studiesproteolytic activation030220 oncology & carcinogenesisNeutrophil elastaseProteolysisbiology.proteinMatrix Metalloproteinase 3Original ArticleLeukocyte Elastasemedicine.drug
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Proteolytic Enzymes Clustered in Specialized Plasma-Membrane Domains Drive Endothelial Cells’ Migration

2016

In vitro cultured endothelial cells forming a continuous monolayer establish stable cell-cell contacts and acquire a "resting" phenotype; on the other hand, when growing in sparse conditions these cells acquire a migratory phenotype and invade the empty area of the culture. Culturing cells in different conditions, we compared expression and clustering of proteolytic enzymes in cells having migratory versus stationary behavior. In order to observe resting and migrating cells in the same microscopic field, a continuous cell monolayer was wounded. Increased expression of proteolytic enzymes was evident in cell membranes of migrating cells especially at sprouting sites and in shed membrane vesi…

0301 basic medicinekalininsepraseCell Membranesbeta1 integrinCelllcsh:MedicineurokinaseBiochemistryEpitheliumCell membrane0302 clinical medicineAnimal CellsMedicine and Health Sciencesdipeptidyl peptidase IVlcsh:ScienceMultidisciplinarybiologyVesicleProteolytic enzymesCell migrationProteasesEnzymesCell biologyLaboratory EquipmentCell Motilitymedicine.anatomical_structureBiochemistry030220 oncology & carcinogenesisEngineering and TechnologyBiological Culturesmatrix metalloproteinase 14Cellular Structures and OrganellesCellular TypesAnatomyResearch ArticleEquipmentCell MigrationResearch and Analysis MethodsGelatin MediaCell Linegelatinase B03 medical and health sciencescollagen type 4fibronectinmedicineHumansVesiclescollagen type 1gelatinase Alcsh:RCell MembraneBiology and Life SciencesEndothelial CellsProteinsMembrane ProteinsEpithelial CellsCell BiologyCulture MediaFibronectinBiological Tissue030104 developmental biologyMembrane proteinCell cultureProteolysisMicroscopy Electron ScanningEnzymologybiology.proteinlcsh:QCollagensDevelopmental BiologyPLOS ONE
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Zymographic analysis of circulating and tissue forms of colon carcinoma gelatinase A (MMP-2) and B (MMP-9) separated by mono- and two-dimensional ele…

2001

Gelatinase A (MMP-2) and gelatinase B (MMP-9) play a key role in the proteolytic cascade leading to ECM degradation during invasion and metastasis. The enzyme activity is regulated both at the intra- and extra-cellular level. Extracellular regulation is achieved mainly through the balance between proenzyme activation and inhibition, which appears to be altered in cancer patients. One of the mechanisms of MMP inhibition is the binding of the enzymes to appropriate tissue inhibitors (TIMP). In the recent literature, it has been suggested that MMP-2 and/or MMP-9 are indeed over-produced in many carcinomas, while the identity of the various enzymatic forms (latent, activated and enzyme/inhibito…

AdultGelatin ZymographyGelatinase AMatrix metalloproteinaseBiologyMetastasisExtracellularmedicineGelatinaseHumansElectrophoresis Gel Two-DimensionalMolecular Biologychemistry.chemical_classificationEnzyme Precursorsmedicine.diseaseMolecular biologyEnzyme assayEnzymeBiochemistrychemistryMatrix Metalloproteinase 9Colonic Neoplasmsbiology.proteinMatrix Metalloproteinase 2Electrophoresis Polyacrylamide GelDensitometryMatrix biology : journal of the International Society for Matrix Biology
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Lipid Peroxidation, Protein Oxidation, Gelatinases, and Their Inhibitors in a Group of Adults with Obesity

2019

AbstractThe association between obesity and cardiovascular diseases has a multifactorial pathogenesis, including the synthesis of inflammatory molecules, the increase in oxidative stress and the dysregulation of the matrix metalloprotease (MMP) concentration and activity. In a group of adults with obesity, divided in 2 subgroups according to the body mass index (BMI), we examined lipid peroxidation, expressed as thiobarbituric acid-reactive substances (TBARS), protein oxidation, expressed as protein carbonyl groups (PCs), plasma gelatinases (MMP-2 and MMP-9), and their tissue inhibitors (TIMP-1 and TIMP-2). In the whole group, as well as in the 2 subgroups (with BMI 30–35 or BMI>35) of o…

AdultMalemedicine.medical_specialtySettore MED/09 - Medicina InternaEndocrinology Diabetes and MetabolismClinical Biochemistry030209 endocrinology & metabolism030204 cardiovascular system & hematologyMatrix metalloproteinasemedicine.disease_causeProtein oxidationBiochemistryPathogenesisLipid peroxidation03 medical and health scienceschemistry.chemical_compound0302 clinical medicineEndocrinologyInternal medicineTBARSHumansMedicineObesityTissue Inhibitor of Metalloproteinase-2Tissue Inhibitor of Metalloproteinase-1business.industryBiochemistry (medical)ProteinsGeneral MedicineMiddle Agedmedicine.diseaseObesityOxidative StressEndocrinologyMatrix Metalloproteinase 9chemistryCase-Control Studiesobesity lipid peroxidation protein oxidation gelatinases TIMPsProteolysisMatrix Metalloproteinase 2FemaleLipid PeroxidationbusinessOxidation-ReductionBody mass indexBiomarkersOxidative stressHormone and Metabolic Research
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Variation of serum and urinary neutrophil gelatinase associated lipocalin (NGAL) after strenuous physical exercise.

2012

AbstractStrenuous exercise may trigger acute complications, such as exertional rhabdomyolysis and gastrointestinal complaint. As less is known about the potential renal impairment after long distance running, we assessed creatinine and neutrophil gelatinase associated lipocalin (NGAL) in serum (sNGAL) and urine (uNGAL) before and after an ultramarathon.The study population consisted of 16 trained male athletes who ran a 60 km ultramarathon. Blood and spot urine samples were collected 20 min before and immediately after the run. Creatinine was assessed by Jaffe assay on Beckman Coulter AU5800 and renal function was expressed as estimated glomerular filtration rate (eGFR) by MDRD formula. NGA…

AdultMalemedicine.medical_specialtyUrinary systemClinical BiochemistryUrologyRenal functionPhysical exerciseUrineCreatinine; neutrophil gelatinase associated lipocalin (NGAL); physical exercise; sportsLipocalinchemistry.chemical_compoundLipocalin-2physical exerciseProto-Oncogene ProteinsmedicineHumansExerciseCreatininebusiness.industryBiochemistry (medical)Acute kidney injuryneutrophil gelatinase associated lipocalin (NGAL)General MedicineAcute Kidney InjuryMiddle Agedmedicine.diseaseLipocalinschemistryCreatinineExertional rhabdomyolysissportsbusinessAcute-Phase ProteinsGlomerular Filtration RateClinical chemistry and laboratory medicine
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Cell-cell and cell-collagen interactions influence gelatinase production by human breast-carcinoma cell line 8701-BC

1995

We previously produced evidence that the human mammary-carcinoma cell line 8701-BC expresses several metalloproteinases (MMP-1, -2, -9, and -10) and their tissue inhibitors. In order to obtain a better understanding of the environmental control over gelatinolytic activities, we have tested the enzyme production of 8701-BC cells, at time intervals after plating on different collagen substrates, i.e., types I, III, IV, V and OF/LB, used as films in culture dishes. Proteinase activities, released in the conditioned culture media, were tested by zymography on SDS-PAGE, and by quantificative analyses, using 14C carboxy-methylated transferrin as substrate in a liquid incubation medium. Enzymatic …

Cancer ResearchConfluencyKunitz STI protease inhibitorBreast NeoplasmsCell CommunicationBiologyTrypsinCulture MediaMolecular WeightOncologyBiochemistryCell–cell interactionGelatinasesCell cultureEndopeptidasesTumor Cells CulturedmedicineHumansGelatinaseSerine Proteinase InhibitorsZymographyCollagenCell Divisionmedicine.drugInternational Journal of Cancer
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Leukocyte subtypes, gelatinases, and their tissue inhibitors in a group of subjects with asymptomatic carotid atherosclerosis

2022

In a cohort of subjects with asymptomatic carotid atherosclerosis (ACA), we have evaluated the neutrophil and lymphocyte count and their ratio (NLR), the gelatinases (MMP-2 and MMP-9) and their tissue inhibitors (TIMP-1 and TIMP-2). At baseline, no difference was observed between ACA subjects and subject control group regarding neutrophil and lymphocyte count while was evident in ACA subjects a significant increase in MMP-2, MMP-9 and TIMP-2 associated to a significant decrease in TIMP-1. Dividing the ACA according to the number of cardiovascular risk factors (CRFs) we have observed an increase in lymphocyte count in the subgroup with 3–5 CRFs. Evaluating the leukocyte subtypes according to…

Carotid Artery Diseasescardiovascular risk factorslymphocytesTissue Inhibitor of Metalloproteinase-2Tissue Inhibitor of Metalloproteinase-1PhysiologyHematologyTIMP-2Asymptomatic carotid atherosclerosisTIMP-1Matrix Metalloproteinase 9neutrophilsinsulin resistancePhysiology (medical)LeukocytesHumansMatrix Metalloproteinase 2Cardiology and Cardiovascular MedicinegelatinasesBiomarkersResearch ArticleClinical Hemorheology and Microcirculation
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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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The immunoexpression of matrix metalloproteinase MMP2 and MMP9 as prognostic significance in cutaneous metastases of breast carcinoma

2004

Aim. Many types of cutaneous metastasis occur in carcinoma of the breast. Cutaneous metastasis has been reported as having a poor prognosis. A fundamental prerequisite for carcinoma cells to metastatize is the ability of the tumour cells to dissociate from the primary tumour and to breach matrix proteins. Degradation and remodelling of matrix proteins can be affected by a variety of enzymatic activities including the matrix metalloproteinases (MMPs). We have analysed the sensitivity, specificity and predictive value of immunohistochemical staining with monoclonal antibodies directed against gelatinase A (MMP-2) and B (MMP-9) in cutaneous metastatic breast carcinoma. Methods. Twenty-two pati…

Gelatinase ABreast neoplasmMetalloproteinase 9Gelatinase BSkin neoplasmsMetalloproteinase 2
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