Search results for "Subcellular Fraction"

showing 8 items of 58 documents

Pyrrolo[3,4-h]quinolinones a new class of photochemotherapeutic agents

2011

Abstract Pyrrolo[3,4- h ]quinolin-2-ones were synthesized as nitrogen isosters of the angular furocoumarin angelicin, with the aim of obtaining new photochemotherapeutic agents with increased antiproliferative activity and lower undesired toxic effects. A versatile synthetic pathway was approached to allow the isolation of derivatives of the new ring system with a good substitution pattern on the pyrrole moiety. Photobiological screenings of the new compounds revealed a potent phototoxic effect and a great UVA dose dependence, reaching IC 50 values at submicromolar level. The induced cellular photocytotoxicity was related to apoptosis with the involvement of mitochondria and lysosomes, alte…

Pyrrolo[3; 4-h]quinolinones; Angelicin heteroanalogues; Photochemotherapeutic agents; PhototoxicityStereochemistryClinical BiochemistryMembrane lipid peroxidationPharmaceutical ScienceHL-60 CellsPhosphatidylserinesQuinolonesMitochondrionBiochemistryPhototoxicityJurkat CellsStructure-Activity Relationshipchemistry.chemical_compoundPhotochemotherapeutic agentsAngelicinCell Line TumorDrug DiscoveryHumansMoietyFluorometryPyrrolesPyrrolo[3Molecular BiologyPyrrolePyrrolo[34-h]quinolinoneFurocoumarinCell CycleOrganic Chemistry4-h]quinolinonesDNAPhotochemical ProcessesSettore CHIM/08 - Chimica FarmaceuticaAngelicin heteroanaloguesPhotochemotherapeutic agentPhotochemotherapychemistryApoptosisMolecular MedicineLipid PeroxidationPhototoxicityAngelicin heteroanalogueSubcellular FractionsBioorganic & Medicinal Chemistry
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Convergence of the target of rapamycin and the Snf1 protein kinase pathways in the regulation of the subcellular localization of Msn2, a transcriptio…

2002

The subcellular localization of Msn2, a transcriptional activator of STRE (stress response element)-regulated genes, is modulated by carbon source availability. In cells growing in glucose, Msn2 is located mainly in the cytosol, whereas in carbon source-starved cells, Msn2 is located largely inside the nucleus. However, in cells lacking Reg1 (the regulatory subunit of the Reg1/Glc7 protein phosphatase complex), the regulation of subcellular distribution is absent, Msn2 being constitutively present in the cytosol. The localization defect in these mutants is specific for carbon starvation stress, and it is because of the presence of an abnormally active Snf1 protein kinase that inhibits the n…

Saccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeMitogen-activated protein kinase kinaseBiologyProtein Serine-Threonine KinasesBiochemistryASK1Molecular BiologyDNA PrimersSirolimusMAP kinase kinase kinaseBase SequenceKinaseCell BiologySubcellular localizationCarbonCell biologyCulture MediaDNA-Binding ProteinsCytosolBiochemistryTrans-ActivatorsCyclin-dependent kinase 9Nuclear localization sequenceSubcellular FractionsTranscription FactorsThe Journal of biological chemistry
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A novel Usher protein network at the periciliary reloading point between molecular transport machineries in vertebrate photoreceptor cells.

2008

Contains fulltext : 69178.pdf (Publisher’s version ) (Closed access) The human Usher syndrome (USH) is the most frequent cause of combined deaf-blindness. USH is genetically heterogeneous with at least 12 chromosomal loci assigned to three clinical types, USH1-3. Although these USH types exhibit similar phenotypes in human, the corresponding gene products belong to very different protein classes and families. The scaffold protein harmonin (USH1C) was shown to integrate all identified USH1 and USH2 molecules into protein networks. Here, we analyzed a protein network organized in the absence of harmonin by the scaffold proteins SANS (USH1G) and whirlin (USH2D). Immunoelectron microscopic anal…

Scaffold proteinGenetics and epigenetic pathways of disease [NCMLS 6]XenopusCell Cycle ProteinsNerve Tissue ProteinsBiologyIn Vitro TechniquesNeuroinformatics [DCN 3]TransfectionModels BiologicalReceptors G-Protein-CoupledMiceChlorocebus aethiopsProtein Interaction MappingGeneticsPerception and Action [DCN 1]otorhinolaryngologic diseasesAnimalsHumansNeurosensory disorders [UMCN 3.3]Cell Cycle ProteinMicroscopy ImmunoelectronMolecular BiologyIntegral membrane proteinGenetics (clinical)Adaptor Proteins Signal TransducingRenal disorder [IGMD 9]GeneticsMice KnockoutExtracellular Matrix ProteinsCiliumSignal transducing adaptor proteinMembrane ProteinsGeneral MedicineTransmembrane proteinCell biologyMice Inbred C57BLCytoskeletal ProteinsEctodomainGenetic defects of metabolism [UMCN 5.1]COS CellsNIH 3T3 CellsCervical collarUsher SyndromesFunctional Neurogenomics [DCN 2]Photoreceptor Cells VertebrateSubcellular FractionsImmunity infection and tissue repair [NCMLS 1]
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Regulation of cell cycle transcription factor Swi5 by karyopherin Msn5

2012

AbstractInactivation of S. cerevisiae β-karyopherin Msn5 causes hypersensitivity to the overexpression of mitotic cyclin Clb2 and aggravates growth defects of many mutant strains in mitotic exit, suggesting a connection between Msn5 and mitotic exit. We determined that Msn5 controlled subcellular localization of the mitotic exit transcription factor Swi5, since it was required for Swi5 nuclear export. Msn5 physically interacted with the N-terminal end of Swi5. Inactivation of Msn5 caused a severe reduction in cellular levels of Swi5 protein. This effect occurred by a post-transcriptional mechanism, since SWI5 mRNA levels were not affected. The reduced amount of Swi5 in msn5 mutant cells was…

Swi5Saccharomyces cerevisiae ProteinsGenes FungalActive Transport Cell NucleusMitosisCell Cycle ProteinsSaccharomyces cerevisiaeKaryopherinsProtein degradationBiologyNuclear export signalMolecular BiologyMitosisTranscription factorKaryopherinMsn5Cell Nucleuschemistry.chemical_classificationProtein StabilityCell CycleCell BiologyCell cycleβ-karyopherinMolecular biologyCell biologyProtein TransportchemistryMitotic exitMutationNuclear transportProtein BindingSubcellular FractionsTranscription FactorsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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The Kelch protein NS1-BP interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control

2007

Alpha-enolase is a key glycolytic enzyme that plays a functional role in several physiological processes depending on the cellular localization. The enzyme is mainly localized in the cytoplasm whereas an alternative translated form, named MBP-1, is predominantly nuclear. The MBP-1 protein has been characterized as a c-Myc promoter binding protein that negatively controls transcription. In the present study, we identified the kelch protein NS1-BP as one of the alpha-enolase/MBP-1 partners by using a yeast two-hybrid screening. Although NS1-BP has been originally described as a protein mainly localized in the nucleus, we provide evidence that NS1-BP also interacts with actin in human cells, a…

Transcription GeneticTranscription FactorGlycolysiAlpha-enolaseKelch proteinsRNA-Binding ProteinHeLa CellChlorocebus aethiopsTranscriptional regulationPromoter Regions GeneticCellular localizationNuclear ProteinbiologyNuclear ProteinsRNA-Binding ProteinsCell biologyDNA-Binding ProteinsProtein TransportCOS CellsYeast two-hybrid assayGlycolysisHumanProtein BindingSubcellular FractionsImmunoprecipitationDNA-Binding ProteinTwo-hybrid screeningEnolaseChlorocebus aethiopProto-Oncogene Proteins c-mycCOS CellBiomarkers TumorAnimalsHumansKelch proteinMolecular BiologyActinTumor Suppressor ProteinAnimalTumor Suppressor ProteinsBinding proteinc-Myc transcriptionCell BiologyMolecular biologyActinsKelch proteinSubcellular FractionSettore BIO/18 - GeneticaGene Expression RegulationCytoplasmPhosphopyruvate Hydratasebiology.proteinHeLa CellsTranscription FactorsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Novel Insights into the Cellular Localization and Regulation of the Autophagosomal Proteins LC3A, LC3B and LC3C

2020

Macroautophagy is a conserved degradative process for maintaining cellular homeostasis and plays a key role in aging and various human disorders. The microtubule-associated protein 1A/1B light chain 3B (MAP1LC3B or LC3B) is commonly analyzed as a key marker for autophagosomes and as a proxy for autophagic flux. Three paralogues of the LC3 gene exist in humans: LC3A, LC3B and LC3C. The molecular function, regulation and cellular localization of LC3A and LC3C have not been investigated frequently, even if a similar function to that described for LC3B appears likely. Here, we have selectively decapacitated LC3B by three separate strategies in primary human fibroblasts and analyzed the evoked e…

autophagysequestosome 1 (p62)LC3CATG8GABARAPGABARAPCellular homeostasisProtein lipidationsirtuin 1ArticleCell LineAntibody SpecificityHumansSirtuinsAmino Acid SequenceLC3BRNA Small InterferingLC3Alcsh:QH301-705.5PhylogenyCellular localizationCell NucleusBinding SitesbiologyChemistrySirtuin 1AutophagosomesAutophagy-Related Protein 8 FamilyGeneral MedicineFibroblastsLipidsCell biologyProtein Transportlcsh:Biology (General)Gene Knockdown TechniquesSirtuinbiology.proteinApoptosis Regulatory ProteinsMicrotubule-Associated ProteinsATG8MAP1LC3BSubcellular FractionsCells
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Lipid peroxidation capacities in the myocardium of endurance-trained rats and mice in vitro.

1992

The endurance-training programme in Experiment 1 (Exp. 1) consisted of a total swimming time of 149–159 h per male Han Wistar rat and in Experiment 2 (Exp. 2) the male NMRI-mice run on a treadmill at a speed of 25 m min-1 1 h per day, 5 days a week for 3 weeks. One group of the rat hearts was perfused with 0.3 mm cumene hydroperoxide (CumOOH) while the others were fractioned (mitochondria, sarcolemma and sarcoplasmic reticulum) and these cell fractions and homogenates were used to determine the total concentration of peroxidative lipids and the susceptibility to lipid peroxidation. The perfusion with CumOOH caused the release of thiobarbituric acid reactive substances (TBARS) into the perfu…

medicine.medical_specialtyPhysiologyThiobarbituric acidThiobarbituric Acid Reactive SubstancesMitochondria HeartRunningLipid peroxidationchemistry.chemical_compoundMiceSarcolemmaEndurance trainingInternal medicinePhysical Conditioning AnimalmedicineTBARSAnimalsRats WistarCreatine KinaseSwimmingSarcolemmaChemistryMyocardiumGlutathioneGlutathioneRatsPerfusionSarcoplasmic ReticulumEndocrinologyBiochemistryCumene hydroperoxideLipid PeroxidationPerfusionSubcellular FractionsActa physiologica Scandinavica
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The non-neuronal cholinergic system in humans: expression, function and pathophysiology.

2003

Acetylcholine, a prime example of a neurotransmitter, has been detected in bacteria, algae, protozoa, and primitive plants, indicating an extremely early appearance in the evolutionary process (about 3 billion years). In humans, acetylcholine and/or the synthesizing enzyme, choline acetyltransferase (ChAT), have been found in epithelial cells (airways, alimentary tract, urogenital tract, epidermis), mesothelial (pleura, pericardium), endothelial, muscle and immune cells (mononuclear cells, granulocytes, alveolar macrophages, mast cells). The widespread expression of non-neuronal acetylcholine is accompanied by the ubiquitous presence of cholinesterase and receptors (nicotinic, muscarinic). …

medicine.medical_specialtyPlacentaBiologyGeneral Biochemistry Genetics and Molecular BiologyCholine O-AcetyltransferasePregnancyInternal medicineMuscarinic acetylcholine receptorMuscarinic acetylcholine receptor M5medicineMuscarinic acetylcholine receptor M4AnimalsHumansReceptors CholinergicGeneral Pharmacology Toxicology and PharmaceuticsInflammationMuscarinic acetylcholine receptor M3Muscarinic acetylcholine receptor M2General MedicineAcetylcholineCell biologyEndocrinologyNicotinic agonistCholinergicFemaleAcetylcholinemedicine.drugSubcellular FractionsLife sciences
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