Search results for "Transfection"

showing 10 items of 581 documents

Rho prevents apoptosis through Bcl-2 expression: Implications for interleukin-2 receptor signal transduction

1997

Here we describe a Rho-mediated apoptosis suppression pathway driven by Bcl-2 expression in the interleukin (IL)-4- or IL-2-dependent murine T cell line TS1 alpha beta. IL-2, but not IL-4, induces Bcl-2 expression through RhoA activation which is inhibited by the specific Rho family inhibitor, Clostridium difficile Toxin B, as well as by a dominant negative RhoA mutant. Using transient transfections of RhoA mutants tagged with the vesicular stomatitis virus glycoprotein, we show that a constitutively active RhoA mutant induces Bcl-2 expression and prevents apoptosis upon IL-4 withdrawal. Finally, we have identified the signaling pathway involved together with RhoA in Bcl-2 induction and sho…

RHOAImmunologyDown-RegulationClostridium difficile toxin AApoptosisClostridium difficile toxin BTransfectionCell LineMicePhosphatidylinositol 3-Kinaseschemistry.chemical_compoundGTP-Binding ProteinsAnimalsHumansImmunology and AllergyPhosphatidylinositolProtein kinase AProtein Kinase CbiologyKinaseInterleukinReceptors Interleukin-2Molecular biologyCell biologyProto-Oncogene Proteins c-bcl-2chemistrybiology.proteinInterleukin-2Signal transductionrhoA GTP-Binding ProteinSignal TransductionEuropean Journal of Immunology
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Clathrin-independent entry of baculovirus triggers uptake of E. coli in non-phagocytic human cells

2008

The prototype baculovirus, Autographa californica multiple nucleopolyhedrovirus, an insect pathogen, holds great potential as a gene therapy vector. To develop transductional targeting and gene delivery by baculovirus, we focused on characterizing the nature and regulation of its uptake in human cancer cells. Baculovirus entered the cells along fluid-phase markers from the raft areas into smooth-surfaced vesicles devoid of clathrin. Notably, regulators associated with macropinocytosis, namely EIPA, Pak1, Rab34, and Rac1, had no significant effect on viral transduction, and the virus did not induce fluid-phase uptake. The internalization and nuclear uptake was, however, affected by mutants o…

RHOASciencevirusesmedia_common.quotation_subjecteducationGene deliveryClathrinCell LineMembrane Lipids03 medical and health sciencesPhagocytosisCell Biology/Membranes and SortingViral entryVirologyEscherichia coliBiochemistry/Cell Signaling and Trafficking StructuresHumansInternalization030304 developmental biologymedia_commonAdenosine Triphosphatases0303 health sciencesMultidisciplinaryBase SequencebiologyADP-Ribosylation FactorsQ030302 biochemistry & molecular biologyHEK 293 cellsRTransfectionMolecular biologyClathrinEndocytosisNucleopolyhedroviruses3. Good healthCell biologyvirologiaADP-Ribosylation Factor 6Cell culturebiology.proteinMedicineRNA InterferenceResearch Article
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APOBEC4 Enhances the Replication of HIV-1

2016

APOBEC4 (A4) is a member of the AID/APOBEC family of cytidine deaminases. In this study we found a high mRNA expression of A4 in human testis. In contrast, there were only low levels of A4 mRNA detectable in 293T, HeLa, Jurkat or A3.01 cells. Ectopic expression of A4 in HeLa cells resulted in mostly cytoplasmic localization of the protein. To test whether A4 has antiviral activity similar to that of proteins of the APOBEC3 (A3) subfamily, A4 was co-expressed in 293T cells with wild type HIV-1 and HIV-1 luciferase reporter viruses. We found that A4 did not inhibit the replication of HIV-1 but instead enhanced the production of HIV-1 in a dose-dependent manner and seemed to act on the viral L…

RNA virusesMale0301 basic medicineMolecular biologylcsh:MedicineArtificial Gene Amplification and ExtensionCytidinePathology and Laboratory MedicineVirus ReplicationBiochemistryPolymerase Chain ReactionJurkat cellschemistry.chemical_compoundCytidine deaminationImmunodeficiency VirusesTranscription (biology)TestisMedicine and Health Scienceslcsh:SciencePromoter Regions GeneticMultidisciplinaryCytidineTransfectionEnzymesImmunoblot AnalysisMedical MicrobiologyDeaminationViral PathogensViruses293T cellsCell linesPathogensOxidoreductasesBiological culturesLuciferaseResearch ArticleMolecular Probe TechniquesDNA constructionBiologyMicrobiologyCell Line03 medical and health sciencesCytidine DeaminaseRetrovirusesHumansMicrobial PathogensHIV Long Terminal Repeat030102 biochemistry & molecular biologylcsh:RLentivirusHEK 293 cellsOrganismsBiology and Life SciencesHIVProteinsPromoterMolecular biologyResearch and analysis methodsMolecular biology techniques030104 developmental biologychemistryPlasmid ConstructionHIV-1Enzymologylcsh:QEctopic expressionCloningPLOS ONE
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Evolutionary plasticity of SH3 domain binding by Nef proteins of the HIV-1/SIVcpz lentiviral lineage

2021

The accessory protein Nef of human and simian immunodeficiency viruses (HIV and SIV) is an important pathogenicity factor known to interact with cellular protein kinases and other signaling proteins. A canonical SH3 domain binding motif in Nef is required for most of these interactions. For example, HIV-1 Nef activates the tyrosine kinase Hck by tightly binding to its SH3 domain. An archetypal contact between a negatively charged SH3 residue and a highly conserved arginine in Nef (Arg77) plays a key role here. Combining structural analyses with functional assays, we here show that Nef proteins have also developed a distinct structural strategy—termed the "R-clamp”—that favors the formation …

RNA virusesviruksetvirusesSimian Acquired Immunodeficiency SyndromeHIV InfectionsPathology and Laboratory MedicineSH3 domainWhite Blood CellsImmunodeficiency VirusesAnimal CellsMedicine and Health SciencesBiology (General)MammalsGenetics11832 Microbiology and virology0303 health sciencesKinase030302 biochemistry & molecular biologyEukaryotavirus diseasesTransfection3. Good healthSIVMedical MicrobiologyViral PathogensViral evolutionVirusesVertebratesProto-Oncogene Proteins c-hckApesSimian Immunodeficiency VirusPathogensCellular TypesTyrosine kinaseResearch ArticlePrimateskinaasitEvolutionary ImmunologyLineage (genetic)QH301-705.5Immune CellsImmunologyevoluutioBiologyTransfectionResearch and Analysis MethodsHIV-tartuntaMicrobiologyViral EvolutionEvolution Molecularsrc Homology Domains03 medical and health sciencesVirologyRetrovirusesGeneticsAnimalsHumansLuciferaseAmino Acid Sequencenef Gene Products Human Immunodeficiency VirusChimpanzeesMolecular Biology TechniquesMicrobial PathogensMolecular Biology030304 developmental biologyEvolutionary BiologyBlood CellsSequence Homology Amino AcidMacrophagesLentivirusOrganismsBiology and Life SciencesHIVCell BiologyRC581-607Organismal Evolution3121 General medicine internal medicine and other clinical medicineMicrobial EvolutionAmniotesHIV-1ParasitologySalt bridgeproteiinitImmunologic diseases. AllergyZoology
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The Proteoglycan NG2 Is Complexed with α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors by the PDZ Glutamate Receptor Interactio…

2003

The proteoglycan NG2 is expressed by immature glial cells in the developing and adult central nervous system. Using the COOH-terminal region of NG2 as bait in a yeast two-hybrid screen, we identified the glutamate receptor interaction protein GRIP1, a multi-PDZ domain protein, as an interacting partner. NG2 exhibits a PDZ binding motif at the extreme COOH terminus which binds to the seventh PDZ domain of GRIP1. In addition to the published expression in neurons, GRIP1 is expressed by immature glial cells. GRIP1 is known to bind to the GluRB subunit of the AMPA glutamate receptor expressed by subpopulations of neurons and immature glial cells. In cultures of primary oligodendrocytes, cells c…

Receptor complexbiologyProtein subunitPDZ domainProtein domainGlutamate receptorCell BiologyAMPA receptorTransfectionBiochemistryMolecular biologynervous systemProteoglycanbiology.proteinMolecular BiologyJournal of Biological Chemistry
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The N-terminal Amino Group of [Tyr8]Bradykinin Is Bound Adjacent to Analogous Amino Acids of the Human and Rat B2 Receptor

1996

To obtain data of the bradykinin B2 receptor's agonist binding site, we used a combined approach of affinity labeling and "immunoidentification" of receptor fragments generated by cyanogen bromide cleavage. Domain-specific antibodies to the various extracellular receptor domains were applied to detect receptor fragments with covalently attached [125I-Tyr8]bradykinin. As a cross-linker we used the homobifunctional reagent disuccinimidyl tartarate (DST), which reacts preferentially with primary amines. With this technique a [125I-Tyr8]bradykinin-labeled receptor fragment derived from the third extracellular domain was identified. The epsilon-amino group of lysine (Lys172) of the human B2 rece…

Receptor Bradykinin B2StereochemistryAffinity labelMolecular Sequence DataBradykininBradykininTransfectionBiochemistryProtein Structure SecondaryCell LineIodine Radioisotopeschemistry.chemical_compoundAnimalsHumansAmino Acid SequenceBradykinin receptorReceptorMolecular BiologyPeptide sequencechemistry.chemical_classificationBinding SitesAffinity labelingbiologyLysineReceptors BradykininAffinity LabelsCell BiologyRecombinant ProteinsRatsAmino acidCross-Linking ReagentschemistryBiochemistryCOS CellsFree fatty acid receptorbiology.proteinJournal of Biological Chemistry
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T Cell Receptor Mimic Peptidesand Their Potential Application in T-Cell-Mediated Diseas e

2001

<i>Background:</i> A T cell receptor (TCR) peptide was designed that mimics the intramembranous amino acid sequence of the TCR chain. Prior studies had shown that this mimic peptide would inhibit TCR signaling. This study was designed to investigate the use of this mimic peptide for the treatment of T-cell-mediated skin diseases. <i>Methods:</i> Synthesized mimic peptides were first tested for their T-cell-inhibitory effect in proliferation assays. Afterwards, mimic peptides were applied to murine ear skin prior to application of a contact allergen and tested for their inhibitory effect in the model of murine allergic contact sensitivity. The effect of epicutaneous t…

Receptors Antigen T-Cell alpha-betaT-LymphocytesT cellmedicine.medical_treatmentImmunologyPeptideBiologyTransfectionmedicine.disease_causeSkin DiseasesMiceImmune systemmedicineAnimalsHumansImmunology and AllergyAmino Acid SequencePeptide sequencechemistry.chemical_classificationMolecular MimicryT-cell receptorGeneral MedicineImmunotherapyPeptide FragmentsMolecular mimicrymedicine.anatomical_structureImmune System DiseaseschemistryImmunologyImmunosuppressive AgentsCD8International Archives of Allergy and Immunology
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Requirement of Retinoic Acid Receptor Isotypes α, β, and γ during the Initial Steps of Neural Differentiation of PCC7 Cells

2005

Retinoic acid (RA) is indispensable for morphogenesis and differentiation of several tissues, including the nervous system. The requirement of the RA receptor (RAR) isotypes alpha, beta, and gamma and the putative role of retinoid X receptor-(RXR) signaling in RA-induced neural differentiation, was analyzed. For this compound-selective retinoids and the murine embryonal carcinoma cell line PCC7, a model system for RA-dependent neural differentiation was used. The present paper shows that proliferating PCC7 cells primarily express RXRalpha and RARalpha, lower levels of RXRbeta, and barely detectable amounts of RARbeta, RARgamma, and RXRgamma. At receptor-selective concentrations, only a RARa…

Receptors Retinoic AcidRetinoic acidReceptors Cytoplasmic and NuclearApoptosisLigandsMicechemistry.chemical_compoundEndocrinologyGenes ReporterNuclear Receptor Subfamily 6 Group A Member 1Protein IsoformsRetinoidReceptorGlutathione TransferaseNeuronsCell DeathReverse Transcriptase Polymerase Chain ReactionCell DifferentiationGeneral MedicineImmunohistochemistryUp-RegulationCell biologyDNA-Binding ProteinsBiochemistrySignal transductionPlasmidsProtein BindingSignal Transductionmedicine.drugTranscriptional ActivationDNA Complementarymedicine.drug_classRecombinant Fusion ProteinsBlotting WesternDown-RegulationTretinoinRetinoid X receptorBiologyTransfectionCell LineTretinoinCell Line TumormedicineAnimalsHumansMolecular BiologyCell ProliferationKineticsRetinoic acid receptorRetinoid X ReceptorschemistryNuclear receptorRNAOctamer Transcription Factor-3Transcription FactorsMolecular Endocrinology
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The unique complexity of the CYP3A4 upstream region suggests a nongenetic explanation of its expression variability.

2010

The individually variable and unpredictable expression of CYP3A4 compromises therapies with 50% of contemporary drugs. Gene variants explain only a fraction of this variability.We investigated the evolution of CYP3A4 transcriptional regulation by nuclear receptors such as the xenobiotics sensors PXR and CAR.The combination of a proximal ER6 element with XREM and CLEM represents the original scheme of CYP3A regulation by nuclear receptors in placental mammals. Among human CYP3A genes, this scheme is retained only in CYP3A4, whereas non-CYP3A4 genes lost these elements to a variable extent during primate evolution. In parallel, the number of elements outside XREM and CLEM potentially responsi…

Receptors SteroidMolecular Sequence DataReceptors Cytoplasmic and NuclearBiologyLigandsTransfectionGene Expression Regulation EnzymologicXenobioticsTranscription (biology)PhylogeneticsLuciferases FireflyGeneticsTranscriptional regulationCytochrome P-450 CYP3AHumansGeneral Pharmacology Toxicology and PharmaceuticsReceptorPromoter Regions GeneticMolecular BiologyGeneGenetics (clinical)Constitutive Androstane ReceptorRegulation of gene expressionGeneticsPregnane X receptorBinding SitesBase SequencePregnane X ReceptorNuclear receptorMolecular MedicineSequence AnalysisProtein BindingPharmacogenetics and genomics
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The induction of cytochrome P450 3A5 (CYP3A5) in the human liver and intestine is mediated by the xenobiotic sensors pregnane X receptor (PXR) and co…

2004

Induction of cytochrome P450 3A (CYP3A) by xenobiotics may lead to clinically relevant drug interactions. In contrast with other CYP3A family members, studies on the inducibility of CYP3A5 indicate conflicting results. We report the induction of CYP3A5 mRNA in 13 of 16 hepatocyte preparations exposed to rifampin. Furthermore, induction of CYP3A5 mRNA was observed in intestinal biopsies in three of eight probands following exposure to the antibiotic. The highest absolute levels of CYP3A5 transcripts were found following rifampin treatment in hepatocytes and intestines from carriers of CYP3A5*1 alleles. Elucidation of the mechanism involved in CYP3A5 induction revealed that constitutively act…

Receptors SteroidTime FactorsCYP3ABiopsyAmino Acid MotifsReceptors Cytoplasmic and NuclearPharmacology030226 pharmacology & pharmacyBiochemistryTransactivation0302 clinical medicineCytochrome P-450 Enzyme SystemGenes ReporterCytochrome P-450 CYP3AIntestinal MucosaReceptorPromoter Regions GeneticGenes Dominant0303 health sciencesPregnane X receptorPregnane X Receptor3. Good healthmedicine.anatomical_structureLiverHepatocyteRifampinPlasmidsProtein BindingTranscriptional ActivationHeterozygoteGenotypeBiologyTransfectionXenobiotics03 medical and health sciencesmedicineHumansRNA MessengerMolecular BiologyAllelesConstitutive Androstane Receptor030304 developmental biologyMessenger RNACYP3A4Cell BiologyMolecular biologyProtein Structure TertiaryHepatocytesRNADrug metabolismTranscription FactorsThe Journal of biological chemistry
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