Search results for "Metalloproteases"

showing 10 items of 32 documents

Protective and causative killer Ig-like receptor (KIR) and metalloproteinase genetic patterns associated with Herpes simplex virus 1 (HSV-1) encephal…

2020

Abstract Background The cerebral innate immune system has a critical role in control processes of viral replication in the brain after primary infactivo and immunologic disregulation and inflammation has been reported as a primary determinant of pathogenesis and prognosis of subsequent HSV-1 related encephalitis (HSE). Interaction linking LTR3-activated DCs is also represented by the killer Ig-like receptor (KIR) + pathways on NK cells. Only a few studies analyzed the role of of MMP-9 activity regulating genetic polymorphism on clinical outcome of viral infections. Susceptibility to symptomatic encephalitis depends on SNC viral invasion and BBB disruption. We hypothesize that certain KIR ge…

0301 basic medicineMaleImmunologyHuman leukocyte antigenHerpesvirus 1 Humanmedicine.disease_causePathogenesisCohort StudiesMetalloprotease03 medical and health sciences0302 clinical medicineReceptors KIRHLA AntigensEncephalitiGenotypemedicineImmunology and AllergyHumansEncephalitis ViralHLA AntigenAllele frequencyAgedbusiness.industryHaplotypeHerpes SimplexMiddle Agedmedicine.diseaseHSV-1KIR030104 developmental biologyHerpes simplex virusNeurologyViral replicationMatrix Metalloproteinase 9ImmunologyMetalloproteasesFemaleNeurology (clinical)Cohort StudiebusinessInfectionMMP-9030217 neurology & neurosurgeryEncephalitis
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Handling Metalloproteinases.

2016

Substrate cleavage by metalloproteinases involves nucleophilic attack on the scissile peptide bond by a water molecule that is polarized by a catalytic metal, usually a zinc ion, and a general base, usually the carboxyl group of a glutamic acid side chain. The zinc ion is most often complexed by imidazole nitrogens of histidine side chains. This arrangement suggests that the physiological pH optimum of most metalloproteinases is in the neutral range. In addition to their catalytic metal ion, many metalloproteinases contain additional transition metal or alkaline earth ions, which are structurally important or modulate the catalytic activity. As a consequence, these enzymes are generally sen…

0301 basic medicineMetal ions in aqueous solutionGlutamic AcidMatrix metalloproteinaseHydrogen-Ion ConcentrationBiochemistryCombinatorial chemistryCatalysisMetal03 medical and health scienceschemistry.chemical_compoundZinc030104 developmental biologychemistryStructural Biologyvisual_artvisual_art.visual_art_mediumMetalloproteasesMoleculeImidazolePeptide bondAnimalsHumansAstacinHistidineCurrent protocols in protein scienceLiterature Cited
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New Insights into the Occurrence of Matrix Metalloproteases -2 and -9 in a Cohort of Breast Cancer Patients and Proteomic Correlations

2018

Matrix metalloproteases (MMPS) are a family of well-known enzymes which operate prevalently in the extracellular domain, where they fulfil the function of remodeling the extracellular matrix. Within the about 26 family members, encoded by 24 genes in humans, MMP-2 and MMP-9, have been regarded as the primary responsibility for the basement membrane and pericellular ECM rearrangement. In cases of infiltrating carcinomas, which arise from the epithelial tissues of a gland or of an internal organ, a marked alteration of the expression and the activity levels of both MMPs is known to occur. Present investigation represents the continuation and upgrading of our previous studies, now focusing on …

0301 basic medicineOncologymedicine.medical_specialtyMatrix metalloproteinaseBiologyProteomicsArticleExtracellular matrix03 medical and health sciences0302 clinical medicinebreast cancerproteomicsBreast cancermatrix metalloproteasesInternal medicineExtracellularmedicineMatrix metalloproteasesSettore BIO/06 - Anatomia Comparata E CitologiaGenelcsh:QH301-705.5oncology_oncogenicsBasement membranebusiness.industryGeneral Medicinemedicine.diseasematrix metalloprotease030104 developmental biologymedicine.anatomical_structurelcsh:Biology (General)030220 oncology & carcinogenesisCohortCancer researchbusinessFunction (biology)
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Mammalian plasma fetuin-B is a selective inhibitor of ovastacin and meprin metalloproteinases

2019

AbstractVertebrate fetuins are multi-domain plasma-proteins of the cystatin-superfamily. Human fetuin-A is also known as AHSG, α2-Heremans-Schmid-glycoprotein. Gene-knockout in mice identified fetuin-A as essential for calcified-matrix-metabolism and bone-mineralization. Fetuin-B deficient mice, on the other hand, are female infertile due to zona pellucida ‘hardening’ caused by the metalloproteinase ovastacin in unfertilized oocytes. In wildtype mice fetuin-B inhibits the activity of ovastacin thus maintaining oocytes fertilizable. Here we asked, if fetuins affect further proteases as might be expected from their evolutionary relation to single-domain-cystatins, known as proteinase-inhibito…

0301 basic medicineProteasesGlycosylationalpha-2-HS-Glycoproteinmedicine.medical_treatmentProteolysislcsh:MedicineAstacoideaMatrix metalloproteinaseArticle03 medical and health sciencesMicePlasma0302 clinical medicinemedicineAnimalsHumansFibrinolysinZona pellucidalcsh:ScienceMammalsMetalloproteinaseMultidisciplinaryProteasemedicine.diagnostic_testChemistrylcsh:RWild typeMetalloendopeptidasesFetuinFetuin-BRecombinant ProteinsCell biology030104 developmental biologymedicine.anatomical_structureMatrix Metalloproteinase 9FertilizationProteolysisMetalloproteasesCattlelcsh:Q030217 neurology & neurosurgery
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The C-terminal region of human plasma fetuin-B is dispensable for the raised-elephant-trunk mechanism of inhibition of astacin metallopeptidases

2019

© The Author(s) 2019.

0301 basic medicineProteasesProtein Conformationlcsh:MedicineAstacoideaCrystallography X-RayCleavage (embryo)Protein Structure SecondaryArticleMice03 medical and health sciencesScissile bondHydrolaseAnimalsHumansAmino Acid Sequencelcsh:ScienceProtein secondary structureX-ray crystallographyBinding SitesMultidisciplinary030102 biochemistry & molecular biologyChemistrylcsh:RMetalloendopeptidasesProteasesFetuinFetuin-BCell biologyZincFertility030104 developmental biologyProteolysisMetalloproteaseslcsh:QAstacinLinkerScientific Reports
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Quantitative Proteomics Reveals Changes Induced by TIMP-3 on Cell Membrane Composition and Novel Metalloprotease Substrates

2021

Ectodomain shedding is a key mechanism of several biological processes, including cell-communication. Disintegrin and metalloproteinases (ADAMs), together with the membrane-type matrix metalloproteinases, play a pivotal role in shedding transmembrane proteins. Aberrant shedding is associated to several pathological conditions, including arthritis. Tissue inhibitor of metalloproteases 3 (TIMP-3), an endogenous inhibitor of ADAMs and matrix metalloproteases (MMPs), has been proven to be beneficial in such diseases. Thus, strategies to increase TIMP-3 bioavailability in the tissue have been sought for development of therapeutics. Nevertheless, high levels of TIMP-3 may lead to mechanism-based …

0301 basic medicineProteomicsADAM15ProteomeCellMatrix metalloproteinaseMass SpectrometryCell membranelcsh:Chemistryanalysis [Proteome]lcsh:QH301-705.5proteomicSpectroscopybiologyChemistrytissue inhibitor of metalloproteases 3 (TIMP-3)General MedicineTransmembrane proteinComputer Science ApplicationsCell biologymedicine.anatomical_structureEctodomainddc:540TIMP3 protein humanmetalloproteinaseectodomain sheddingmetabolism [Tissue Inhibitor of Metalloproteinase-3]Quantitative proteomicsADAM15 protein humanchemistry [Cell Membrane]Catalysismetabolism [Cell Membrane]ArticlemetalloproteinasesInorganic Chemistry03 medical and health sciencestissue inhibitor of metalloproteases 3 (TIMP-3).medicineDisintegrinHumansPhysical and Theoretical ChemistryMolecular BiologyTissue Inhibitor of Metalloproteinase-3030102 biochemistry & molecular biologyOrganic ChemistryCell MembraneMembrane Proteinsmetabolism [Proteome]ADAM Proteins030104 developmental biologyHEK293 Cellslcsh:Biology (General)lcsh:QD1-999metabolism [ADAM Proteins]biology.proteinmetabolism [Membrane Proteins]International Journal of Molecular Sciences
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Is proteomics of value in cardiovascular risk assessment?

2019

Purpose of review To briefly summarize recently published evidence in the field of cardiovascular proteomics, focusing on its ability to improve cardiovascular risk stratification and critically discussing still open and burning issues and future perspectives of proteomics research. Recent findings Several epidemiological studies have demonstrated an improvement in cardiovascular risk prediction beyond traditional risk factors by adding novel biomarkers, identified by both discovery and targeted proteomics. However, only a moderate improvement in risk discrimination over clinical variables was observed. Moreover, despite different outcomes there was also a strong overlap of identified candi…

0301 basic medicineProteomicsClinical variablesGrowth Differentiation Factor 15Endocrinology Diabetes and MetabolismDisease030204 cardiovascular system & hematologyProteomicsBioinformaticsRisk Assessment03 medical and health sciences0302 clinical medicineRisk FactorsGeneticsMedicineAnimalsHumansBiomarker discoveryNatriuretic PeptidesMolecular BiologyNutrition and Dieteticsbusiness.industryInterleukinsCell BiologyTargeted proteomics030104 developmental biologyC-Reactive ProteinCardiovascular DiseasesRisk stratificationMetalloproteasesCardiology and Cardiovascular MedicinebusinessRisk assessmentBiomarkersCurrent opinion in lipidology
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Dipeptidyl Peptidase IV as a Muscle Myokine

2020

Dipeptidyl peptidase IV (DPP-IV) is a unique serine protease that exists in a membrane bound state and in a soluble state in most tissues in the body. DPP-IV has multiple targets including cytokines, neuropeptides, and incretin hormones, and plays an important role in health and disease. Recent work suggests that skeletal muscle releases DPP-IV as a myokine and participates in control of muscle blood flow. However, few of the functions of DPP-IV as a myokine have been investigated to date and there is a poor understanding about what causes DPP-IV to be released from muscle.

0301 basic medicinemedicine.medical_specialtyanimal structuresPhysiologymuscleMini ReviewNeuropeptideIncretin030204 cardiovascular system & hematologyDipeptidyl peptidaselcsh:Physiology03 medical and health sciences0302 clinical medicinePhysiology (medical)Internal medicineMyokinemedicinemetalloproteasesSerine proteaseMetalloproteinasebiologyexerciselcsh:QP1-981ChemistrySkeletal musclewhey proteinpeptidasesecretome030104 developmental biologyEndocrinologymedicine.anatomical_structurebiology.proteinHormoneFrontiers in Physiology
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Carbon Monoxide-Releasing Molecules: A Pharmacological Expedient to Counteract Inflammation

2008

Carbon monoxide (CO) mediates many of the biological effects that are attributed to heme oxygenase (HO), the enzyme responsible for CO production in mammals. Antioxidant and anti-inflammatory activities of HO-1, the inducible isoform of heme oxygenase, have been demonstrated in a variety of disease models and a therapeutic exploitation of this pathway is currently under scrutiny. In this context, the liberation of CO from CO-releasing molecules (CO-RMs) is extremely attractive as these compounds may form the basis of a new class of pharmaceuticals. Recent investigations indicate that HO-1 and CO modulate important processes in chronic inflammation; these include the control of immune respon…

Anti-Inflammatory AgentsContext (language use)InflammationOsteoarthritisPharmacologyRutheniumArthritis RheumatoidDegenerative diseaseImmune systemOsteoarthritisDrug DiscoveryOrganometallic CompoundsAnimalsHumansMedicineInflammationPharmacologyCarbon Monoxidebusiness.industrymedicine.diseaseCarbon monoxide-releasing moleculesHeme oxygenaseOxidative StressImmunologyMetalloproteasesCytokinesmedicine.symptomSignal transductionbusinessHeme Oxygenase-1Signal TransductionCurrent Pharmaceutical Design
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Matrix Metalloproteases in Arterial Hypertension and their Trend after Antihypertensive Treatment

2017

<b><i>Background/Aims</i></b><b><i>:</i></b> Arterial hypertension is characterized by vascular remodelling, atherosclerosis and cardiovascular complications. Matrix metalloproteases (MPPs) are endopeptidases produced by all the cells present in the vascular wall and are involved in the regulation of the extracellular matrix protein turnover. MMPs contribute to blood vessel formation, remodelling, angiogenesis; whereas an altered expression or activity of MMPs or their tissue inhibitors (TIMPs) results correlated with the development and progression of cardiovascular complications. <b><i>Methods:</i></b> We examined the…

Arterial hypertensionVascular remodelling0301 basic medicinelcsh:Diseases of the circulatory (Cardiovascular) systemmedicine.medical_specialtyAngiogenesisMatrix metalloproteasesMatrix metalloproteaseHemodynamics030204 cardiovascular system & hematologyPharmacologyMatrix metalloproteinaselcsh:RC870-923Vascular remodelling in the embryoExtracellular matrix03 medical and health scienceschemistry.chemical_compound0302 clinical medicineFibrosisInternal medicinelcsh:DermatologymedicineHumansAntihypertensive AgentsAldosteronebusiness.industryTissue Inhibitor of MetalloproteinasesGeneral Medicinelcsh:RL1-803lcsh:Diseases of the genitourinary system. Urologymedicine.diseaseMatrix Metalloproteinases030104 developmental biologymedicine.anatomical_structurechemistrylcsh:RC666-701Cardiovascular DiseasesNephrologyHypertensionCardiologyArterial hypertension; Matrix metalloproteases; Vascular remodelling; Cardiology and Cardiovascular Medicine; NephrologyCardiology and Cardiovascular MedicinebusinessBlood vesselKidney and Blood Pressure Research
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