Search results for "Gelatinases"

showing 10 items of 24 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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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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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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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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Gelatinases and their tissue inhibitors in a group of subjects with metabolic syndrome.

2013

Aim To evaluate matrix metalloproteases (MMP)-2 and MMP-9 and tissue inhibitor of metalloproteases (TIMP)-1 and TIMP-2 in a group of subjects with metabolic syndrome (MS) subdivided according to the presence or absence of diabetes mellitus. Methods We examined in 90 subjects (51 men and 39 women) with MS, defined following the International Diabetes Federation criteria, and subsequently subdivided into diabetic subjects (22 men and 11 women) and nondiabetic subjects s (29 men and 28 women), the plasma concentrations of MMP-2 and MMP-9 and of TIMP-1 and TIMP-2 using specific enzyme-linked immunosorbent assay kits. Results We found a significant increase in plasma concentrations of MMP-2, MMP…

MaleGelatinasesmedicine.medical_specialtyMatrix metalloproteinase insulin resistanceMatrix metalloproteinaseBiologyMatrix Metalloproteinase InhibitorsGeneral Biochemistry Genetics and Molecular BiologyDiabetes mellitusInternal medicinemedicineMatrix metalloproteasesHumansInternational diabetes federationMetabolic SyndromeMetalloproteinaseTissue Inhibitor of Metalloproteinase-2Tissue Inhibitor of Metalloproteinase-1General MedicineMiddle Agedmedicine.diseaseEndocrinologyMatrix Metalloproteinase 9GelatinasesPlasma concentrationMatrix Metalloproteinase 2FemaleMetabolic syndromeBiomarkersJournal of investigative medicine : the official publication of the American Federation for Clinical Research
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Study of the Correlations among Some Parameters of the Oxidative Status, Gelatinases, and Their Inhibitors in a Group of Subjects with Metabolic Synd…

2014

Our aim was to examine some parameters of oxidative status, gelatinases, and their inhibitors and to evaluate their interrelationships in subjects with metabolic syndrome (MS). We enrolled 65 MS subjects, subdivided according to the presence or not of diabetes mellitus. We examined lipid peroxidation (expressed as thiobarbituric acid reacting substances, TBARS), protein oxidation (expressed as carbonyl groups), nitric oxide metabolites (NOx), total antioxidant status (TAS), MMP-2, MMP-9, TIMP-1, and TIMP-2. We found that MS subjects, diabetics and nondiabetics, showed an increase in TBARS, PC, and NOx. A significant decrease in TAS was observed only in nondiabetic MS subjects in comparison …

Malemedicine.medical_specialtyGelatinasesSettore MED/09 - Medicina InternaArticle SubjectThiobarbituric acidImmunologymedicine.disease_causeProtein oxidationNitric OxideThiobarbituric Acid Reactive SubstancesAntioxidantsLipid peroxidationchemistry.chemical_compoundOxidative Status Gelatinases Metabolic SyndromeInternal medicineDiabetes mellitusmedicineTBARSlcsh:PathologyHumansMetabolic SyndromeTissue Inhibitor of Metalloproteinase-2Tissue Inhibitor of Metalloproteinase-1business.industryCell BiologyMiddle Agedmedicine.diseaseEndocrinologychemistryBiochemistryMatrix Metalloproteinase 9GelatinasesMatrix Metalloproteinase 2FemaleLipid PeroxidationMetabolic syndromebusinessOxidative stresslcsh:RB1-214Research ArticleMediators of Inflammation
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Gelatinases and their tissue inhibitors in a group of subjects with obstructive sleep apnea syndrome.

2016

Obstructive sleep apnea syndrome (OSAS) is associated with an elevated risk of cardiovascular events and stroke. Matrix metalloproteinases (MMPs) are endopeptidases involved in extracellular matrix degradation and then in the development and progression of cardiovascular diseases. Our aim was to evaluate plasma levels of gelatinases (MMP-2 and MMP-9) and their tissue inhibitors (TIMP-1 and TIMP-2) in a group of subjects with OSAS. We enrolled 48 subjects (36 men and 12 women; mean age 49.7 ± 14.68 yrs) with OSAS diagnosed with a 1-night cardiorespiratory study and then we subdivided these subjects into two subgroups according to the apnea/hypopnea index (AHI): Low (L = 21 subjects with AHI …

Malemedicine.medical_specialtyGelatinasesSettore MED/09 - Medicina InternaPhysiologyMMP-2; MMP-9; obstructive sleep apnea; TIMP-1; TIMP-2; Disease Progression; Female; Gelatinases; Humans; Male; Middle Aged; Sleep Apnea Obstructive; Tissue Inhibitor of Metalloproteinase-1; Physiology; Hematology; Cardiology and Cardiovascular Medicine; Physiology (medical)030204 cardiovascular system & hematologyMatrix metalloproteinaseGastroenterologyTIMP-203 medical and health sciencesTIMP-10302 clinical medicinePhysiology (medical)Internal medicinemedicineHumansStrokeobstructive sleep apneaOxygen saturation (medicine)Sleep Apnea ObstructiveTissue Inhibitor of Metalloproteinase-1MMP-2business.industryApneaCardiorespiratory fitnessHematologyMiddle Agedmedicine.diseasenervous system diseasesrespiratory tract diseasesObstructive sleep apneaEndocrinology030228 respiratory systemGelatinaseGelatinasesDisease ProgressionFemalemedicine.symptomMMP-9Settore MED/36 - Diagnostica Per Immagini E RadioterapiaCardiology and Cardiovascular MedicinebusinessHypopneaHumanClinical hemorheology and microcirculation
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