Search results for "proteolysis"

showing 10 items of 119 documents

Ticagrelor, but not clopidogrel, reduces arterial thrombosis via endothelial tissue factor suppression

2017

The P2Y12 antagonist ticagrelor reduces mortality in patients with acute coronary syndrome (ACS), compared with clopidogrel, and the mechanisms underlying this effect are not clearly understood. Arterial thrombosis is the key event in ACS; however, direct vascular effects of either ticagrelor or clopidogrel with focus on arterial thrombosis and its key trigger tissue factor have not been previously investigated.Methods and results: Human aortic endothelial cells were treated with ticagrelor or clopidogrel active metabolite (CAM) and stimulated with tumour necrosis factor-alpha (TNF-α); effects on procoagulant tissue factor (TF) expression and activity, its counter-player TF pathway inhibito…

0301 basic medicineMaleTicagrelorAdenosineTime FactorsPhysiology030204 cardiovascular system & hematology2737 Physiology (medical)0302 clinical medicineP2Y12AntithromboticCells CulturedClopidogrelReceptors Purinergic P2Y123. Good healthClopidogrelmedicine.anatomical_structureCoagulation10209 Clinic for CardiologyCardiologyCardiology and Cardiovascular MedicineTicagrelormedicine.drugBlood PlateletsAcute coronary syndromemedicine.medical_specialtyProteasome Endopeptidase ComplexTiclopidineEndotheliumDown-Regulation610 Medicine & health2705 Cardiology and Cardiovascular MedicineThromboplastinEquilibrative Nucleoside Transporter 103 medical and health sciencesTissue factorFibrinolytic AgentsPhysiology (medical)Internal medicinemedicineAnimalsHumanscardiovascular diseasesBlood Coagulationbusiness.industryTumor Necrosis Factor-alphaEndothelial CellsThrombosis1314 Physiologymedicine.diseaseMice Inbred C57BLDisease Models Animal030104 developmental biologyProteolysisPurinergic P2Y Receptor AntagonistsbusinessCarotid Artery InjuriesPlatelet Aggregation Inhibitors
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Limited proteolysis by acrosin affects sperm-binding and mechanical resilience of the mouse zona pellucida.

2021

Abstract The encounter of oocyte and sperm is the key event initiating embryonic development in mammals. Crucial functions of this existential interaction are determined by proteolytic enzymes, such as acrosin, carried in the sperm head acrosome, and ovastacin, stored in the oocyte cortical granules. Ovastacin is released upon fertilisation to cleave the zona pellucida, a glycoprotein matrix surrounding the oocyte. This limited proteolysis hardens the oocyte envelope, and thereby provides a definitive block against polyspermy and protects the developing embryo. On the other hand, acrosin, the renowned and most abundant acrosomal protease, has been thought to enable sperm to penetrate the oo…

0301 basic medicineMaleendocrine systemEmbryologyBiologyZona Pellucida Glycoproteins03 medical and health sciencesMice0302 clinical medicineGeneticsmedicineAnimalsAcrosomeZona pellucidaMolecular Biologyreproductive and urinary physiologyFertilisationZona PellucidaMammalsSperm-Ovum InteractionsAcrosinurogenital systemProteolytic enzymesObstetrics and GynecologyCell BiologyPolyspermyAcrosinOocyteSpermSpermatozoaCell biology030104 developmental biologymedicine.anatomical_structureReproductive Medicineembryonic structuresProteolysisAcrosome030217 neurology & neurosurgeryDevelopmental BiologyMolecular human reproduction
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New Functions of APC/C Ubiquitin Ligase in the Nervous System and Its Role in Alzheimer’s Disease

2017

The E3 ubiquitin ligase Anaphase Promoting Complex/Cyclosome (APC/C) regulates important processes in cells, such as the cell cycle, by targeting a set of substrates for degradation. In the last decade, APC/C has been related to several major functions in the nervous system, including axon guidance, synaptic plasticity, neurogenesis, and neuronal survival. Interestingly, some of the identified APC/C substrates have been related to neurodegenerative diseases. There is an accumulation of some degradation targets of APC/C in Alzheimer’s disease (AD) brains, which suggests a dysregulation of the protein complex in the disorder. Moreover, recently evidence has been provided for an inactivation o…

0301 basic medicineNervous systemNeurogenesisUbiquitin-Protein LigasesReviewubiquitin ligaseNervous SystemCatalysisAnaphase-Promoting Complex-CyclosomeCdh1 ProteinsInorganic Chemistrylcsh:Chemistry03 medical and health sciencesMiceAlzheimer Diseasemedicineoxidative stressAnimalsHumansPhysical and Theoretical ChemistryMolecular Biologylcsh:QH301-705.5SpectroscopyNeuronsNeuronal PlasticitybiologyOrganic ChemistryNeurodegenerationNeurogenesisCell CycleneurodegenerationGeneral MedicineCell cyclemedicine.diseaseComputer Science ApplicationsUbiquitin ligaseCell biology030104 developmental biologymedicine.anatomical_structurelcsh:Biology (General)lcsh:QD1-999ImmunologyKnockout mouseProteolysisbiology.proteinAxon guidanceAnaphase-promoting complexexcitotoxicityInternational Journal of Molecular Sciences
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Identification of noncovalent proteasome inhibitors with high selectivity for chymotrypsin-like activity by a multistep structure-based virtual scree…

2016

Noncovalent proteasome inhibitors introduce an alternative mechanism of inhibition to that of covalent inhibitors, e.g. carfilzomib, used in cancer therapy. A multistep hierarchical structure-based virtual screening (SBVS) of the 65,375 NCI lead-like compound library led to the identification of two compounds (9 and 28) which noncovalently inhibited the chymotrypsin-like (ChT-L) activity (Ki = 2.18 and 2.12 μM, respectively) with little or no effects on the other two major proteasome proteolytic activities, trypsin-like (T-L) and post-glutamyl peptide hydrolase (PGPH) activities. A subsequent hierarchical similarity search over the full NCI database with the most active tripeptide-based inh…

0301 basic medicineNon-covalentVirtual screeningProteasome Endopeptidase ComplexStereochemistryProtein ConformationProteolysisDrug Evaluation PreclinicalTripeptideSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundStructure-Activity RelationshipUser-Computer Interface0302 clinical medicineProtein structureCell Line TumorDrug DiscoverymedicineStructure–activity relationshipChymotrypsinHumansProteasome inhibitorCell ProliferationPharmacologyVirtual screeningmedicine.diagnostic_testOrganic ChemistryGeneral MedicineCarfilzomibPeptide scaffoldMolecular Docking SimulationProteasome inhibitors; Non-covalent; Peptide scaffold; Docking studies; Virtual screening030104 developmental biologyProteasomechemistryBiochemistryDocking (molecular)030220 oncology & carcinogenesisDocking studieProteolysisProteasome InhibitorsEuropean journal of medicinal chemistry
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αB-crystallin response to a pro-oxidant non-cytotoxic environment in murine cardiac cells: An "in vitro" and "in vivo" study.

2020

The αB-crystallin (HSPB5) protein is modulated in response to a wide variety of stressors generated by multiple physio-pathological conditions, sustained by reactive oxygen species (ROS) production. In cardiac muscle tissue, this protein regulates various cellular processes, such as protein degradation, apoptosis and the stabilization of cytoskeletal elements. In this work, we studied the role of HSPB5 expression, activation and localization in HL-1 murine cardiomyocytes exposed to pro-oxidant and non-cytotoxic H2O2 concentration, as well as in cardiac tissue isolated from mice following an acute, non-damaging endurance exercise. Our results demonstrated that HSPB5 is the most abundant HSP …

0301 basic medicineOxidative eustressOxidative phosphorylationProtein degradationBiochemistry03 medical and health sciencesMice0302 clinical medicineIn vivoPhysiology (medical)medicineAnimalsCardiac musclePhosphorylationchemistry.chemical_classificationReactive oxygen speciesHSPB5ChemistryCardiac musclealpha-Crystallin B ChainHydrogen PeroxidePro-oxidantEndurance exerciseHSPA1ACell biology030104 developmental biologymedicine.anatomical_structureProteolysisCardiac muscle tissueReactive Oxygen SpeciesOxidation-Reduction030217 neurology & neurosurgeryFree radical biologymedicine
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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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Vitamin D and Its Analogues Decrease Amyloid-β (Aβ) Formation and Increase Aβ-Degradation

2017

Alzheimer’s disease (AD) is characterized by extracellular plaques in the brain, mainly consisting of amyloid-β (Aβ), as derived from sequential cleavage of the amyloid precursor protein. Epidemiological studies suggest a tight link between hypovitaminosis of the secosteroid vitamin D and AD. Besides decreased vitamin D level in AD patients, an effect of vitamin D on Aβ-homeostasis is discussed. However, the exact underlying mechanisms remain to be elucidated and nothing is known about the potential effect of vitamin D analogues. Here we systematically investigate the effect of vitamin D and therapeutically used analogues (maxacalcitol, calcipotriol, alfacalcidol, paricalcitol, doxercalcife…

0301 basic medicineParicalcitolPlaque Amyloidvitamin Damyloid precursor proteinlcsh:ChemistrySecosteroidMicechemistry.chemical_compound0302 clinical medicinevitamin D analoguesvitamin D; vitamin D analogues; amyloid precursor protein; amyloid-β; secretases; Aβ-degradationAmyloid precursor proteinlcsh:QH301-705.5CalcipotriolSpectroscopybiologysecretasesBrainAlfacalcidolVitaminsGeneral Medicine3. Good healthComputer Science ApplicationsFemalemedicine.drugmedicine.medical_specialtyAβ-degradationNicastrinamyloid-βArticleCatalysisInorganic Chemistry03 medical and health sciencesCell Line TumorInternal medicinemedicineVitamin D and neurologyAnimalsHumansPhysical and Theoretical ChemistryMolecular BiologyAmyloid beta-PeptidesOrganic ChemistryMice Inbred C57BL030104 developmental biologyEndocrinologylcsh:Biology (General)lcsh:QD1-999chemistryProteolysisbiology.proteinAmyloid Precursor Protein SecretasesAmyloid precursor protein secretase030217 neurology & neurosurgeryInternational Journal of Molecular Sciences
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Post-transcriptional, post-translational and pharmacological regulation of tissue factor pathway inhibitor.

2018

: Tissue factor (TF) pathway inhibitor (TFPI) is an endogenous natural anticoagulant that readily inhibits the extrinsic coagulation initiation complex (TF-FVIIa-Xa) and prothrombinase (FXa, FVa and calcium ions). Alternatively, spliced TFPI isoforms (α, β and δ) are expressed by vascular and extravascular cells and regulate thrombosis and haemostasis, as well as cell signalling functions of TF complexes via protease-activated receptors (PARs). Proteolysis of TFPI plays an important role in regulating physiological roles of the TF pathway in host defense and possibly haemostasis. Elimination of TFPI inhibition has therefore been proposed as an approach to improve haemostasis in haemophilia …

0301 basic medicineProteasesCell signalingProteolysisLipoproteinsEndogeny030204 cardiovascular system & hematology03 medical and health sciencesTissue factor0302 clinical medicineTissue factor pathway inhibitorProthrombinasemedicineAnimalsHumansRNA Processing Post-TranscriptionalReceptorHemostasismedicine.diagnostic_testChemistryThrombosisHematologyGeneral MedicineCell biology030104 developmental biologyProtein Processing Post-TranslationalBlood coagulationfibrinolysis : an international journal in haemostasis and thrombosis
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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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Insights into the Structure of the Vip3Aa Insecticidal Protein by Protease Digestion Analysis

2017

Vip3 proteins are secretable proteins from Bacillus thuringiensis whose mode of action is still poorly understood. In this study, the activation process for Vip3 proteins was closely examined in order to better understand the Vip3Aa protein stability and to shed light on its structure. The Vip3Aa protoxin (of 89 kDa) was treated with trypsin at concentrations from 1:100 to 120:100 (trypsin:Vip3A, w:w). If the action of trypsin was not properly neutralized, the results of SDS-PAGE analysis (as well as those with Agrotis ipsilon midgut juice) equivocally indicated that the protoxin could be completely processed. However, when the proteolytic reaction was efficiently stopped, it was revealed t…

0301 basic medicineProteasesHealth Toxicology and MutagenesisSize-exclusion chromatographyBeta sheetBacillus thuringiensislcsh:MedicineBiologyToxicologyCleavage (embryo)ArticleProtein Structure Secondary03 medical and health sciencestrypsin inhibitorsBacterial ProteinsSDS-PAGE artefactprotease stabilitymedicinebacterial secreted proteinsAnimalsTrypsinMode of actionProtein secondary structureVip proteinsIntestinal Secretionslcsh:Rtoxin activationVip proteins; bacterial secreted proteins; toxin activation; proteolytic activation; trypsin inhibitors; <i>Bacillus thuringiensis</i>; SDS-PAGE artefact; protease stabilityTrypsinMolecular biologyLepidoptera030104 developmental biologyBiochemistryproteolytic activationLarvaProteolysisPeptidesAlpha helixmedicine.drugToxins
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