Search results for "Cyst"

showing 10 items of 1960 documents

Caspase-dependent apoptosis during infection with Cryptosporidium parvum

1999

The protozoan parasite Cryptosporidium parvum causes persistent diarrhea and malnutrition in children and the diarrhea-wasting syndrome in AIDS. No therapy exists for eliminating the parasite in the absence of a healthy immune response. Although it had been reported that infection of intestinal cell lines with C. parvum leads to host cell death, the mechanisms of cytolysis have not been characterized. We show here that infection with C. parvum leads to typical apoptotic nuclear condensation and DNA fragmentation in host cells. Both nuclear condensation and DNA fragmentation are inhibited by a caspase inhibitor, showing that caspases are involved in this type of apoptosis. Finally, blocking …

Programmed cell deathImmunologyCryptosporidiosisApoptosisDNA FragmentationCysteine Proteinase InhibitorsMicrobiologyCaspase-Dependent ApoptosisAmino Acid Chloromethyl KetonesCell LineImmune systemparasitic diseasesAnimalsHumansComputingMilieux_MISCELLANEOUSCaspaseCryptosporidium parvumbiologybiology.organism_classificationCaspase InhibitorsVirologyCytolysisPOUVOIR PATHOGENE[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyInfectious DiseasesCryptosporidium parvumMicroscopy FluorescenceApoptosisCaspasesbiology.proteinDNA fragmentationHeLa CellsMicrobes and Infection
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Inhibition of proteasome function induces programmed cell death in proliferating endothelial cells.

2000

Proteolysis mediated by the ubiquitin-proteasome system has been implicated in the regulation of programmed cell death. Here we investigated the differential effects of proteasomal inhibitors on the viability of proliferating and quiescent primary endothelial cells in vitro and in vivo. Subconfluent, proliferating cells underwent carbobenzoxy-L-isoleucyl-gamma-t-butyl-L-glutamyl-L-alanyl-L-leucinal (PSI) -induced apoptosis at low concentrations (EC(50)=24 nM), whereas at least 340-fold higher concentrations of PSI were necessary to obtain the same effect in confluent, contact-inhibited cells. PSI-mediated cell death could be blocked by a caspase-3 inhibitor (Ac-DEVD-H), but not by a caspase…

Programmed cell deathProteasome Endopeptidase ComplexAngiogenesisProteolysisApoptosisChick EmbryoCysteine Proteinase InhibitorsBiochemistryDogsMultienzyme ComplexesGeneticsmedicineAnimalsHumansMolecular BiologyCells Culturedmedicine.diagnostic_testChemistryCell cycleDifferential effectsCell biologyCysteine EndopeptidasesProteasomeCattleEndothelium VascularFunction (biology)Cell DivisionBiotechnologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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µ-Calpain conversion of antiapoptotic Bfl-1 (BCL2A1) into a prodeath factor reveals two distinct alpha-helices inducing mitochondria-mediated apoptos…

2011

Anti-apoptotic Bfl-1 and pro-apoptotic Bax, two members of the Bcl-2 family sharing a similar structural fold, are classically viewed as antagonist regulators of apoptosis. However, both proteins were reported to be death inducers following cleavage by the cysteine protease µ-calpain. Here we demonstrate that calpain-mediated cleavage of full-length Bfl-1 induces the release of C-terminal membrane active α-helices that are responsible for its conversion into a pro-apoptotic factor. A careful comparison of the different membrane-active regions present in the Bfl-1 truncated fragments with homologous domains of Bax show that helix α5, but not α6, of Bfl-1 induces cell death and cytochrome c r…

Programmed cell deathProtein StructureCancer Treatmentlcsh:MedicineApoptosisMitochondrionCleavage (embryo)BiochemistryProtein Structure SecondaryMinor Histocompatibility AntigensMiceCell Line TumorMolecular Cell BiologyAnimalsHumanslcsh:ScienceProtein InteractionsBiologyMultidisciplinaryMicroscopy ConfocalbiologyCell DeathCalpainCytochrome clcsh:RCytochromes cProteinsCalpainCysteine proteaseCell biologyMitochondriaProto-Oncogene Proteins c-bcl-2OncologyApoptosisbiology.proteinMedicinelcsh:QElectrophoresis Polyacrylamide GelGlobular ProteinsBCL2-related protein A1Research ArticlePloS one
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Enzymatically modified LDL induces cathepsin H in human monocytes: potential relevance in early atherogenesis.

2003

Objective—Modification with proteases and cholesterylesterase transforms LDL to a moiety that resembles lipoproteins isolated from atherosclerotic lesions and possesses atherogenic properties. To identify changes in monocyte-derived foam cells laden with enzymatically modified LDL (E-LDL), we compared patterns of the most abundant transcripts in these cells after incubation with LDL or E-LDL.Methods and Results—Serial analyses of gene expression (SAGE) libraries were constructed from human monocytes after treatment with LDL or E-LDL. Several tags were differentially expressed in LDL-treated versus E-LDL–treated cells, whereby marked selective induction by E-LDL of cathepsin H was conspicuou…

ProteasesCathepsin HCoronary Artery DiseaseBiologyCathepsin HCathepsin L1medicineMacrophageHumansFoam cellGene LibraryCathepsinMonocyteGene Expression ProfilingColocalizationSterol EsteraseMolecular biologyCathepsinsLipoproteins LDLCysteine Endopeptidasesmedicine.anatomical_structureCholesterolBiochemistryGene Expression Regulationlipids (amino acids peptides and proteins)Cardiology and Cardiovascular MedicineFoam CellsArteriosclerosis, thrombosis, and vascular biology
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Unnatural amino acids increase activity and specificity of synthetic substrates for human and malarial cathepsin C

2014

Mammalian cathepsin C is primarily responsible for the removal of N-terminal dipeptides and activation of several serine proteases in inflammatory or immune cells, while its malarial parasite ortholog dipeptidyl aminopeptidase 1 plays a crucial role in catabolizing the hemoglobin of its host erythrocyte. In this report, we describe the systematic substrate specificity analysis of three cathepsin C orthologs from Homo sapiens (human), Bos taurus (bovine) and Plasmodium falciparum (malaria parasite). Here, we present a new approach with a tailored fluorogenic substrate library designed and synthesized to probe the S1 and S2 pocket preferences of these enzymes with both natural and a broad ran…

ProteasesPlasmodium falciparumClinical BiochemistryProtozoan ProteinsBiologysubstrate libraryAminopeptidaseBiochemistryCathepsin CCathepsin CSubstrate SpecificitySerineAnimalsHumanscysteine proteaseunnatural amino acidAmino AcidsCathepsinchemistry.chemical_classificationMolecular StructureOrganic ChemistryPlasmodium falciparumnon-proteinogenicDipeptidesbiology.organism_classificationCysteine proteaseAmino acidKineticsBiochemistrychemistryfluorogenic substrateOriginal ArticleCattleAmino Acids
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Enteroviruses and coronaviruses: similarities and therapeutic targets

2021

ABSTRACT Introduction: Enteroviruses are common viruses causing a huge number of acute and chronic infections and producing towering economic costs. Similarly, coronaviruses cause seasonal mild infections, epidemics, and even pandemics and can lead to severe respiratory symptoms. It is important to develop broadly acting antiviral molecules to efficiently tackle the infections caused by thes. Areas covered: This review illuminates the differences and similarities between enteroviruses and coronaviruses and examines the most appealing therapeutic targets to combat both virus groups. Publications of both virus groups and deposited structures discovered through PubMed to March 2021 for viral p…

ProteasesPolyproteinsvirusesmedicine.medical_treatmentClinical BiochemistrycoronavirusReviewSARS-COV-2Biologymedicine.disease_causeAntiviral Agents3C proteaseVirusSubstrate Specificity03 medical and health sciencesDrug DiscoveryPandemicmedicineAnimalsHumansVirus classificationEnterovirus030304 developmental biologyCoronavirusPharmacology0303 health sciencesProtease030306 microbiologyCOVID-19Virology3. Good healthCysteine Endopeptidasesmain proteaseMolecular MedicineEnterovirusResearch ArticleExpert Opinion on Therapeutic Targets
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Development of rhodesain inhibitors with a 3-bromoisoxazoline warhead

2013

Novel rhodesain inhibitors were obtained by combining an enantiomerically pure 3-bromoisoxazoline warhead with a specific peptidomimetic recognition moiety. All derivatives behaved as inhibitors of rhodesain, with low micromolar Ki values. Their activity against the enzyme was found to be paralleled by an in vitro antitrypanosomal activity, with IC50 values in the mid-micromolar range. Notably, a preference for parasitic over human proteases, specifically cathepsins B and L, was observed.

ProteasesStereochemistryPeptidomimeticCathepsin LMolecular ConformationStereoisomerismCysteine Proteinase InhibitorsBiologyCrystallography X-RayBiochemistryCysteine Proteinase InhibitorsCathepsin BCathepsin LinhibitorsDrug DiscoveryHumansMoietyGeneral Pharmacology Toxicology and PharmaceuticstrypanosomarhodesainPharmacologychemistry.chemical_classificationOrganic ChemistryStereoisomerismIsoxazolesisoxazolinesCombinatorial chemistryIn vitroCysteine EndopeptidasesEnzymechemistrypeptidomimeticsbiology.proteinMolecular Medicineinhibitors; isoxazolines; peptidomimetics; rhodesain; trypanosomaProtein Binding
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Identification of Plakortide E from the Caribbean Sponge Plakortis halichondroides as a Trypanocidal Protease Inhibitor using Bioactivity-Guided Frac…

2014

In this paper, we report new protease inhibitory activity of plakortide E towards cathepsins and cathepsin-like parasitic proteases. We further report on its anti-parasitic activity against Trypanosoma brucei with an IC50 value of 5 mu M and without cytotoxic effects against J774.1 macrophages at 100 mu M concentration. Plakortide E was isolated from the sponge Plakortis halichondroides using enzyme assay-guided fractionation and identified by NMR spectroscopy and mass spectrometry. Furthermore, enzyme kinetic studies confirmed plakortide E as a non-competitive, slowly-binding, reversible inhibitor of rhodesain.

ProteasesStereochemistrymedicine.medical_treatmentTrypanosoma brucei bruceiPlakortis halichondroidesPharmaceutical ScienceTrypanosoma brucei01 natural sciences570 Life sciencesDioxanesprotease inhibitor03 medical and health sciencesddc:593Drug DiscoverymedicineAnimalsHumansProtease Inhibitorscathepsinlcsh:QH301-705.5Pharmacology Toxicology and Pharmaceutics (miscellaneous)IC50030304 developmental biologyTrypanocidal agentrhodesainchemistry.chemical_classification0303 health sciencesProteaseAntiparasitic Agentsbiology010405 organic chemistryCommunicationplakortide Ebiology.organism_classificationCathepsinsTrypanocidal AgentsAntiparasitic agentProtease inhibitor (biology)Porifera0104 chemical sciencesCysteine Endopeptidasesslowly-binding reversible inhibitorEnzymelcsh:Biology (General)BiochemistrychemistryDrug Screening Assays Antitumor570 Biowissenschaftenmedicine.drug
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Cryo-negative staining

1998

Abstract A procedure is presented for the preparation of thin layers of vitrified biological suspensions in the presence of ammonium molybdate, which we termcryo-negative staining. The direct blotting of sample plus stain solution on holey carbon supports produces thin aqueous films across the holes, which are routinely thiner than the aqueous film produced by conventional negative staining on a continuous carbon layer. Because of this, a higher than usual concentration of negative stain (ca. 16% rather than 2%) is required for cryo-negative staining in order to produce an optimal image contrast. The maintenance of the hydrated state, the absence of adsorption to a carbon film and associate…

Proteasome Endopeptidase ComplexAnalytical chemistryGeneral Physics and AstronomyNegative Staininglaw.inventionMultienzyme ComplexesStructural BiologylawImage Processing Computer-AssistedTobacco mosaic virusAnimalsGeneral Materials ScienceColoring AgentsMolybdenumAmmonium molybdateTurnip yellow mosaic virusbiologyChemistryChaperonin 60Cell BiologyCatalasebiology.organism_classificationNegative stainStainingCysteine EndopeptidasesMicroscopy ElectronCrystallographyFreeze DryingElectron diffractionHemocyaninsVirusesCattleElectron microscopeTomato bushy stunt virusMicron
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Analysis of the MHC Class I Antigen Presentation Machinery in Human Embryonal Carcinomas: Evidence for Deficiencies in TAP, LMP and MHC Class I Expre…

1998

The expression of the major histocompatibility complex (MHC) class I antigens is suppressed in early post-implantation embryonic cells as well as in embryonal carcinoma (EC) cells, but could be upregulated by treatment with interferon (IFN)-gamma or retinoic acid. In a number of human and murine tumours, defects in the expression of the different components of the MHC class I antigen processing machinery, such as the proteasomal subunits LMP-2 and LMP-7 and the peptide transporters TAP-1 and TAP-2, account for impaired MHC class I surface expression. Here, we analysed the constitutive and IFN-gamma regulated mRNA and protein expression of the LMP, TAP and MHC class I molecules in the human …

Proteasome Endopeptidase ComplexCD74HIV AntigensImmunologyCD1CytomegalovirusInterferon-gammaATP Binding Cassette Transporter Subfamily B Member 3Multienzyme ComplexesCarcinoma EmbryonalMHC class ITumor Cells CulturedHumansATP Binding Cassette Transporter Subfamily B Member 2Antigens ViralAntigen PresentationbiologyAntigen processingMHC class I antigenHistocompatibility Antigens Class ITemperatureGeneral MedicineTransporter associated with antigen processingMHC restrictionMolecular biologyUp-RegulationCysteine EndopeptidasesProtein Biosynthesisbiology.proteinATP-Binding Cassette TransportersPeptidesCD8Scandinavian Journal of Immunology
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