Search results for "Enzyme complex"

showing 10 items of 55 documents

PKSP-dependent reduction of phagolysosome fusion and intracellular kill of Aspergillus fumigatus conidia by human monocyte-derived macrophages.

2002

Summary Previously, we described the isolation of an Aspergillus fumigatus mutant producing non-pigmented conidia, as a result of a defective polyketide synthase gene, pksP (polyketide synthase involved in pigment biosynthesis). The virulence of the pksP mutant was attenuated in a murine animal infection model and its conidia showed enhanced susceptibility towards damage by monocytes in vitro. Because macrophage-mediated killing is critical for host resistance to aspergillosis, the interaction of both grey-green wild-type conidia and white pksP mutant conidia with human monocyte-derived macrophages (MDM) was studied with respect to intracellular processing of ingested conidia. After phagocy…

PhagocytosisImmunologyMutantVirulenceMicrobiologyPhagolysosomeMonocytesMicrobiologyAspergillus fumigatusConidiumCell FusionPhagocytosisMultienzyme ComplexesVirologyPhagosomesAspergillosisHumansskin and connective tissue diseasesCells CulturedPhagosomebiologyAspergillus fumigatusMacrophagesfungirespiratory systembiology.organism_classificationAcridine OrangeIntracellularCellular microbiology
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Gene amplification in fibroblasts from ataxia telangiectasia (AT) patients and in X-ray hypersensitive AT-like Chinese hamster mutants.

2001

In search of functions involved in the regulation of gene amplification, and given the relevance of chromosome breakage in initiating the process, we analyzed the gene amplification ability of cells hypersensitive to inducers of DNA double-strand breaks and defective in cell cycle control: two human fibroblast strains derived from patients affected by ataxia telangiectasia (AT) and two hamster mutant cell lines belonging to complementation group XRCC8 of the rodent X-ray-sensitive mutants. These mutants are considered hamster models of AT cells. To measure gene amplification, the frequency and the rate of occurrence of N-(phosphonacetyl)-L-aspartate resistant cells were determined. In both …

Phosphonoacetic AcidCancer ResearchAntimetabolites AntineoplasticMutantHamstermedicine.disease_causeRadiation ToleranceChinese hamsterCell LineAtaxia TelangiectasiaCricetulusMultienzyme ComplexesCricetinaeGene duplicationmedicineAspartate CarbamoyltransferaseAnimalsHumansDihydroorotaseMutationAspartic AcidbiologyX-RaysGenetic Complementation TestGene AmplificationGeneral MedicineCell cycleFibroblastsmedicine.diseasebiology.organism_classificationMolecular biologyDrug Resistance NeoplasmAtaxia-telangiectasiaMutationCarbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)Chromosome breakageCarcinogenesis
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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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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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Bipartite regulation of different components of the MHC class I antigen-processing machinery during dendritic cell maturation

2001

Dendritic cells (DC) are professional antigen-presenting cells (APC) which proceed from immature to a mature stage during their final differentiation. Immature DC are highly effective in terms of antigen uptake and processing, whereas mature DC become potent immunostimulatory cells. Until now, the expression profiles of the major components of the MHC class I antigen-processing machinery (APM) during DC development have not been well characterized. In this study, the mRNA and protein expression levels of the IFN-gamma inducible proteasome subunits, of the proteasome activators PA28, and of key components required for peptide transport and MHC class I-peptide complex assembly have been evalu…

Proteasome Endopeptidase ComplexCD74ImmunologyAntigen presentationLipopolysaccharide ReceptorsDown-RegulationImmunoglobulinsMuscle ProteinsAntiportersMonocytesMultienzyme ComplexesMHC class IHumansImmunology and AllergyATP Binding Cassette Transporter Subfamily B Member 2Antigen PresentationMHC class IIbiologyAntigen processingMHC class I antigenHistocompatibility Antigens Class IMembrane Transport ProteinsProteinsCell DifferentiationDendritic CellsGeneral MedicineTransporter associated with antigen processingMHC restrictionMolecular biologyUp-RegulationCell biologyCysteine EndopeptidasesProtein TransportProtein Biosynthesisbiology.proteinATP-Binding Cassette TransportersPeptidesInternational Immunology
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Glucocorticoids inhibit MAP kinase via increased expression and decreased degradation of MKP-1

2001

Glucocorticoids inhibit the proinflammatory activities of transcription factors such as AP-1 and NF-kappa B as well as that of diverse cellular signaling molecules. One of these signaling molecules is the extracellular signal-regulated kinase (Erk-1/2) that controls the release of allergic mediators and the induction of proinflammatory cytokine gene expression in mast cells. The mechanism of inhibition of Erk-1/2 activity by glucocorticoids is unknown. Here we report a novel dual action of glucocorticoids for this inhibition. Glucocorticoids increase the expression of the MAP kinase phosphatase-1 (MKP-1) gene at the promoter level, and attenuate proteasomal degradation of MKP-1, which we re…

Proteasome Endopeptidase ComplexCell signalingMitogen-Activated Protein Kinase 3Cell Cycle ProteinsBiologyDexamethasoneGene Expression Regulation EnzymologicArticleGeneral Biochemistry Genetics and Molecular BiologyCell LineImmediate-Early ProteinsProinflammatory cytokineMiceGlucocorticoid receptorMultienzyme ComplexesProtein Phosphatase 1Phosphoprotein PhosphatasesAnimalsEnzyme InhibitorsPhosphorylationMolecular BiologyTranscription factorDNA PrimersMitogen-Activated Protein Kinase 1Regulation of gene expressionMitogen-Activated Protein Kinase 3Base SequenceGeneral Immunology and MicrobiologyKinaseHydrolysisGeneral NeuroscienceDual Specificity Phosphatase 1Cell biologyMice Inbred C57BLCysteine EndopeptidasesMitogen-activated protein kinasebiology.proteinMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesThe EMBO Journal
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Cloning of Sponge (Geodia cydonium) and Tunicate (Botryllus schlosseri) Proteasome Subunit Epsilon (PRCE): Implications about the Vertebrate MHC-Enco…

1996

Proteasomes are large protein complexes that play a major role in selective degradation of intracellular proteins. Eukaryotes feature seven different alpha and beta subunits. Two of the vertebrate housekeeping beta-subunits have MHC-encoded homologues that can substitute for the housekeeping counterparts upon interferon-gamma induction. In the present study we report the cloning of invertebrate beta-subunit proteasome epsilon (PRCE), from the marine sponge Geodia cydonium and from the colonial tunicate Botryllus schlosseri. Sequence comparisons revealed that the sponge and tunicate proteins are strikingly similar to vertebrate and yeast PRCEs and their MHC-linked counterparts the PRCCs (als…

Proteasome Endopeptidase ComplexDNA ComplementaryProtein subunitMolecular Sequence DataBiophysicsSaccharomyces cerevisiaeBotryllus schlosseriPolymerase Chain ReactionBiochemistryMiceMultienzyme ComplexesConsensus SequenceBotanyAnimalsHumansAmino Acid SequenceUrochordataCloning MolecularProtein precursorMolecular BiologyPhylogenyDNA Primerschemistry.chemical_classificationCloningBase SequenceSequence Homology Amino AcidbiologyProteinsCell Biologybiology.organism_classificationYeastPoriferaRatsAmino acidTunicateCell biologyCysteine EndopeptidaseschemistryProteasomeVertebratesChickensBiochemical and Biophysical Research Communications
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Functional deficiencies of components of the MHC class I antigen pathway in human tumors of epithelial origin

2000

An association between oncogenic transformation and repression of different components of the MHC class I antigen processing machinery (APM) have been described in murine model systems. In order to discover whether a similar correlation exists, human tumor cell lines of distinct histology with altered ras protein were analyzed for the expression of APM components utilizing RT-PCR and Western blot analyses. A heterogeneous expression pattern of MHC class I antigens, TAP peptide transporter, proteasome subunits, proteasome activator PA28 and the chaperones calnexin, calreticulin as well as tapasin was displayed by these tumor cell lines. Single or combined deficiencies in the expression and/o…

Proteasome Endopeptidase ComplexGene ExpressionInterferon-gammaMiceTapasinATP Binding Cassette Transporter Subfamily B Member 3Multienzyme ComplexesCalnexinGene expressionMHC class ITumor Cells CulturedAnimalsHumansNeoplasms Glandular and EpithelialATP Binding Cassette Transporter Subfamily B Member 2DNA PrimersAntigen PresentationTransplantationBase SequencebiologyAntigen processingMHC class I antigenHistocompatibility Antigens Class IProteinsHematologyTransporter associated with antigen processingRecombinant ProteinsCell biologyCysteine EndopeptidasesGenes rasMutationCancer researchbiology.proteinATP-Binding Cassette TransportersCalreticulinBone Marrow Transplantation
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Proteasomes shape the repertoire of T cells participating in antigen-specific immune responses

2006

Differences in the cleavage specificities of constitutive proteasomes and immunoproteasomes significantly affect the generation of MHC class I ligands and therefore the activation of CD8-positive T cells. Based on these findings, we investigated whether proteasomal specificity also influences CD8-positive T cells during thymic selection by peptides derived from self proteins. We find that one of the self peptides responsible for positive selection of ovalbumin-specific OT-1 T cells, which is derived from the f-actin capping protein (Cpalpha1), is efficiently generated only by immunoproteasomes. Furthermore, OT-1 mice backcrossed onto low molecular mass protein 7 (LMP7)-deficient mice show a…

Proteasome Endopeptidase ComplexOvalbuminActin Capping ProteinsT-LymphocytesMolecular Sequence DataReceptors Antigen B-CellThymus GlandBiologyEpitopeInterleukin 21MiceImmune systemAntigenMultienzyme ComplexesMHC class ICytotoxic T cellT cell repertoire; selectionAnimalsIL-2 receptorAmino Acid SequenceAntigensSelection GeneticBone Marrow TransplantationMice KnockoutMultidisciplinaryBiological SciencesMolecular biologyPeptide FragmentsMice Inbred C57BLCTL*biology.proteinLymph Nodes
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