Search results for "Protease"

showing 10 items of 463 documents

Molecular Co-operation between Protein PAM and Streptokinase for Plasmin Acquisition by Streptococcus pyogenes

1998

Bacterial surface-associated plasmin formation is believed to contribute to invasion, although the underlying molecular mechanisms are poorly understood. To define the components necessary for plasmin generation on group A streptococci we used strain AP53 which exposes an M-like protein ("PAM") that contains a plasminogen-binding sequence with two 13-amino acid residues long tandem repeats (a1 and a2). Utilizing an Escherichia coli-streptococcal shuttle vector, we replaced a 29-residue long sequence segment of Arp4, an M-like protein that does not bind plasminogen, with a single (a1) or the combined a1a2 repeats of PAM. When expressed in E. coli, the purified chimeric Arp/PAM proteins both …

Streptococcus pyogenesPlasminRecombinant Fusion Proteinsmedicine.medical_treatmentStreptokinasemedicine.disease_causeBiochemistryMicrobiologyBacterial Proteinsstomatognathic systemShuttle vectorTandem repeatEscherichiaparasitic diseasesmedicineStreptokinaseFibrinolysinMolecular BiologyGeneAntigens BacterialProteasebiologyPlasminogenCell Biologybiology.organism_classificationBiochemistryStreptococcus pyogenesTransformation BacterialCarrier ProteinsBacterial Outer Membrane Proteinsmedicine.drugJournal of Biological Chemistry
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Inactivation of the ftsH gene of Lactobacillus plantarum WCFS1: Effects on growth, stress tolerance, cell surface properties and biofilm formation

2012

FtsH proteins are ubiquitous membrane-bound, ATP-dependent metalloproteases of the AAA family. In eubacteria, FtsH is involved in protein quality control under stress conditions. Lactobacillus plantarum is a widespread lactic acid bacterium that is encountered in several fermented food, including dairy products, vegetables and meat. In the present work the expression of the ftsH gene of L. plantarum was studied by quantitative real time RT-PCR in bacterial cultures subjected to various abiotic stresses. Both oxidative stress and addition of a membrane-fluidizing agent induced ftsH transcription, while a depletion of carbon-source repressed its mRNA level. Mutants deprived of the FtsH protea…

Surface Propertiesmedicine.medical_treatmentMutantReal-Time Polymerase Chain Reactionmedicine.disease_causeMicrobiologyMicrobiologyATP-Dependent ProteasesBacterial ProteinsStress PhysiologicalTranscription (biology)medicineGeneProteasebiologyReverse Transcriptase Polymerase Chain ReactionGene Expression ProfilingTemperatureBiofilmbiology.organism_classificationBiochemistryBiofilmsSaltsProtein qualityGene DeletionLactobacillus plantarumOxidative stressLactobacillus plantarumMicrobiological Research
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Topotecan triggers apoptosis in p53-deficient cells by forcing degradation of XIAP and survivin thereby activating caspase-3-mediated Bid cleavage.

2009

The topoisomerase I inhibitor topotecan (TPT) is used in the therapy of different tumors including high-grade gliomas. We previously showed that TPT-induced apoptosis depends on p53 with p53 wild-type (wt) cells being more resistant because of p53-controlled degradation of topoisomerase I. Here, we show that p53-deficient (p53(-/-)) fibroblasts undergo excessive mitochondrial apoptosis featuring H2AX phosphorylation, Bcl-x(L) decline, cytochrome c release, caspase-9/-3/-2 activation, and cleavage of Bid. In wt and apaf-1(-/-) cells, caspase-2 did not become activated and Bid was not cleaved. In addition, p53(-/-) cells cotreated with TPT and caspase-3 inhibitor showed neither caspase-2 acti…

SurvivinBlotting WesternDown-RegulationCaspase 3ApoptosisX-Linked Inhibitor of Apoptosis ProteinBiologyTopoisomerase-I InhibitorInhibitor of apoptosisTransfectionInhibitor of Apoptosis ProteinsHistonesMiceCell Line TumorSurvivinAnimalsHumansPhosphorylationRNA Small InterferingPharmacologyMice KnockoutCaspase 3Caspase 2TransfectionFibroblastsFlow CytometryMolecular biologyXIAPMice Inbred C57BLRepressor ProteinsApoptotic Protease-Activating Factor 1ApoptosisCancer researchMolecular MedicineApoptosomeTopoisomerase I InhibitorsTumor Suppressor Protein p53TopotecanMicrotubule-Associated ProteinsBH3 Interacting Domain Death Agonist ProteinThe Journal of pharmacology and experimental therapeutics
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The Swedish dilemma - the almost exclusive use of APPswe-based mouse models impedes adequate evaluation of alternative β-secretases.

2022

Abstract Alzheimer's disease (AD) is the most common form of dementia, however incurable so far. It is widely accepted that aggregated amyloid β (Aβ) peptides play a crucial role for the pathogenesis of AD, as they cause neurotoxicity and deposit as so-called Aβ plaques in AD patient brains. Aβ peptides derive from the amyloid precursor protein (APP) upon consecutive cleavage at the β- and γ-secretase site. Hence, mutations in the APP gene are often associated with autosomal dominant inherited AD. Almost thirty years ago, two mutations at the β-secretase site were observed in two Swedish families (termed Swedish APP (APPswe) mutations), which led to early-onset AD. Consequently, APPswe was …

SwedenProteasesbiologyBACE1-ASNeurotoxicityMice TransgenicCell Biologymedicine.diseaseCathepsin BPathogenesisAmyloid beta-Protein PrecursorDisease Models AnimalADAMTS4Alzheimer Diseasemental disordersbiology.proteinAmyloid precursor proteinmedicineAnimalsHumansAmyloid Precursor Protein SecretasesMolecular BiologyAmyloid precursor protein secretaseNeuroscienceBiochimica et biophysica acta. Molecular cell research
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Synaptobrevin cleavage by the tetanus toxin light chain is linked to the inhibition of exocytosis in chromaffin cells

1994

AbstractExocytosis of secretory granules by adrenal chromaffin cells is blocked by the tetanus toxin light chain in a zinc specific manner. Here we show that cellular synaptobrevin is almost completely degraded by the tetanus toxin light chain within 15 min. We used highly purified adrenal secretory granules to show that synaptobrevin, which can be cleaved by the tetanus toxin light chain, is localized in the vesicular membrane. Proteolysis of synaptobrevin in cells and in secretory granules is reversibly inhibited by the zinc chelating agent dipicolinic acid. Moreover, cleavage of synaptobrevin present in secretory granules by the tetanus toxin light chain is blocked by the zinc peptidase …

SynaptobrevinProteolysismedicine.medical_treatmentMolecular Sequence DataBiophysicsSynaptobrevinNerve Tissue ProteinsIn Vitro Techniquesmedicine.disease_causeImmunoglobulin light chainBiochemistryExocytosisExocytosisR-SNARE ProteinsStructural BiologyGeneticsmedicineAnimalsChromaffin GranulesAmino Acid SequenceMolecular BiologySecretory granuleR-SNARE ProteinsAdrenal medullaProteasemedicine.diagnostic_testChemistryToxinMembrane ProteinsCell BiologyPeptide FragmentsTetanus toxinmedicine.anatomical_structureBiochemistryCattleAdrenal medullaFEBS Letters
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Taspase1: a 'misunderstood' protease with translational cancer relevance

2015

Proteolysis is not only a critical requirement for life, but the executing enzymes also play important roles in numerous pathological conditions, including cancer. Therefore, targeting proteases is clearly relevant for improving cancer patient care. However, to effectively control proteases, a profound knowledge of their mechanistic function as well as their regulation and downstream signalling in health and disease is required. The highly conserved protease Threonine Aspartase1 (Taspase1) is overexpressed in numerous liquid and solid malignancies and was characterized as a 'non-oncogene addiction' protease. Although Taspase1 was shown to cleave various regulatory proteins in humans as well…

Threonine0301 basic medicineCancer ResearchProteasesmedicine.medical_treatmentProteolysisComputational biologyDiseaseBiologyBioinformaticsmedicine.disease_causeAspartate Ammonia-LyaseGene Expression Regulation EnzymologicTranslational Research Biomedical03 medical and health sciencesNeoplasmsEndopeptidasesGeneticsmedicineHumansEnzyme InhibitorsMolecular BiologyProteaseMolecular Structuremedicine.diagnostic_testCancermedicine.diseaseGene Expression Regulation Neoplastic030104 developmental biologyProteasomeCarcinogenesisBiologieFunction (biology)Oncogene
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Induction of apoptosis in human osteosarcoma Saos-2 cells by the proteasome inhibitor MG132 and the protective effect of pRb

2003

Induction of apoptosis in human osteosarcoma Saos-2 cells by the proteasome inhibitor MG132 and the protective effect of pRb

Time FactorsLeupeptinsApoptosisRetinoblastoma ProteinAntioxidantsAmino Acid Chloromethyl KetonesMembrane Potentialschemistry.chemical_compoundSettore BIO/10 - BiochimicaMG132Caspase 8OsteosarcomaChemistryCaspase 3Cytochromes cFlow CytometryMitochondriaCysteine EndopeptidasesProto-Oncogene Proteins c-bcl-2CaspasesOsteosarcomamedicine.drugmusculoskeletal diseasesProteasome Endopeptidase ComplexCell SurvivalBlotting Westernbcl-X Proteinmacromolecular substancesTransfectionMultienzyme ComplexesCell Line Tumorparasitic diseasesmedicineHumansProtease InhibitorsneoplasmsMolecular BiologySaos-2 cellsDose-Response Relationship DrugCell Biologymedicine.diseaseAcetylcysteineApoptosis osteosarcoma proteasome inhibitorsMicroscopy FluorescenceApoptosisCancer researchProteasome inhibitorTumor Suppressor Protein p53Reactive Oxygen Specieshuman activities
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Factor VIIa-induced interaction with integrin controls the release of tissue factor on extracellular vesicles from endothelial cells.

2019

Essentials Prothrombotic extracellular vesicles (EV) carry agonist pathway-specific proteomes Agonists for protease activated receptor (PAR) 2 signaling have distinct effects on EV composition PAR2 signaling rapidly generates prothrombotic EV and slowly EV with inactive tissue factor (TF) FVIIa integrin ligation restricts TF incorporation into EV from endothelial cells SUMMARY: Background Cell injury signal-induced activation and release of tissue factor (TF) on extracellular vesicles (EVs) from immune and vessel wall cells propagate local and systemic coagulation initiation. TF trafficking and release on EVs occurs in concert with the release of cell adhesion receptors, including integrin …

Time Factorsmedia_common.quotation_subjectIntegrinFactor VIIa030204 cardiovascular system & hematologyThromboplastin03 medical and health sciencesTissue factorchemistry.chemical_compoundExtracellular Vesicles0302 clinical medicineHumansReceptor PAR-2Protease-activated receptorintegrin traffickingInternalizationReceptorCell adhesionBlood CoagulationCells Culturedmedia_commonbiologyFactor VIIChemistryIntegrin beta1protease-activated receptorsEndothelial CellsHematologytissue factorCell biologyProtein Transportbiology.proteinOligopeptidesIntracellularSignal TransductionJournal of thrombosis and haemostasis : JTH
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Regulation of stress response in Oenococcus oeni as a function of environmental changes and growth phase

2000

International audience; Oenococcus oeni is a lactic acid bacterium which is able to grow in wine and perform malolactic fermentation. To survive and grow in such a harsh environment as wine, O. oeni uses several mechanisms of resistance including stress protein synthesis. The molecular characterisation of three stress genes hsp18, clpX, trxA encoding for a small heat shock protein, an ATPase regulation component of ClpP protease and a thioredoxin, respectively, allow us to suggest the existence in O. oeni of multiple regulation mechanisms as is the case in Bacillus subtilis. One common feature of these genes is that they are expressed under the control of housekeeping promoters. The express…

Transcription Geneticmedicine.medical_treatment[SDV]Life Sciences [q-bio]bactérie lactiqueBacillus subtilisatpaseMicrobiologygène clppoenococcus oenicaractérisation moléculaire03 medical and health sciencesBacterial ProteinsHeat shock proteinOenococcus;Malolactic fermentation;Stress gene;ATPaseMalolactic fermentationmedicineprotéine de choc thermiquePromoter Regions GeneticGeneHeat-Shock ProteinsOenococcus030304 developmental biologyOenococcus oeniAdenosine Triphosphatases0303 health sciencesProteasebiology030306 microbiologyMalolactic fermentationStress genefood and beveragesGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationGram-Positive CocciBiochemistryThioredoxinOenococcusLeuconostocFood Scienceexpression des gènes
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Pharmacologic Inhibition of ADAM10 Attenuates Brain Tissue Loss, Axonal Injury and Pro-inflammatory Gene Expression Following Traumatic Brain Injury …

2021

The α-secretase A disintegrin and metalloprotease 10 (ADAM10) regulates various physiological and pathophysiological processes. Despite its broad functional implications during development, plasticity, and disease, no pharmacological approaches to inhibit ADAM10 in acute brain injury have been reported. Here, we examined the effects of the ADAM10 inhibitor GI254023X on the neurological and histopathological outcome after experimental traumatic brain injury (TBI). C57BL/6N mice were subjected to the controlled cortical impact (CCI) model of TBI or sham procedure and received GI254023X or vehicle during the acute phase of injury (n = 40, 100 mg/kg, 25% DMSO, 0.1 M Na2CO3, intraperitoneal, 30 …

Traumatic brain injuryADAM10PharmacologyBlood–brain barrierNeuroprotectionneuroinflammationaxonal injuryCell and Developmental Biologymedicinelcsh:QH301-705.5NeuroinflammationOriginal ResearchMicrogliabiologybusiness.industrytraumatic brain injuryADAM10 (a disintegrin and metalloprotease 10)Glutamate receptorCell Biologymedicine.diseaseGI254023Xmedicine.anatomical_structurelcsh:Biology (General)biology.proteinneuroprotectionGRIN2BbusinessDevelopmental BiologyFrontiers in Cell and Developmental Biology
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