Search results for "Mitochondrial"

showing 10 items of 919 documents

Mode of cell death induction by pharmacological Vacuolar H+-ATPase (V-ATPase) inhibition.

2012

The vacuolar H+-ATPase (V-ATPase), a multisubunit proton pump, has come into focus as an attractive target in cancer invasion. However, little is known about the role of V-ATPase in cell death, and especially the underlying mechanisms remain mostly unknown. We used the myxobacterial macrolide archazolid B, a potent inhibitor of the V-ATPase, as an experimental drug as well as a chemical tool to decipher V-ATPase-related cell death signaling. We found that archazolid induced apoptosis in highly invasive tumor cells at nanomolar concentrations which was executed by the mitochondrial pathway. Prior to apoptosis induction archazolid led to the activation of a cellular stress response including …

Programmed cell deathVacuolar Proton-Translocating ATPasesCellBiologyBiochemistryCellular stress responseCell Line TumormedicineAutophagyV-ATPaseHumansEnzyme InhibitorsMolecular BiologyCell ProliferationMembrane Potential MitochondrialMicroscopy ConfocalCell DeathCell growthAutophagyCytochromes cCell BiologyCell biologymedicine.anatomical_structureApoptosisSignal transductionSignal Transduction
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Prevention by Dietary Polyphenols (Resveratrol, Quercetin, Apigenin) Against 7-Ketocholesterol-Induced Oxiapoptophagy in Neuronal N2a Cells: Potentia…

2020

The Mediterranean diet is associated with health benefits due to bioactive compounds such as polyphenols. The biological activities of three polyphenols (quercetin (QCT), resveratrol (RSV), apigenin (API)) were evaluated in mouse neuronal N2a cells in the presence of 7-ketocholesterol (7KC), a major cholesterol oxidation product increased in patients with age-related diseases, including neurodegenerative disorders. In N2a cells, 7KC (50 &micro

Programmed cell deathanimal diseasesSOD2N2a cellsApoptosisresveratrolmedicine.disease_causeoxiapoptophagyArticleCell LinequercetinMiceage-related diseasesmedicineAutophagyPeroxisomesAnimalsHumansApigeninlcsh:QH301-705.5Ketocholesterols7-ketocholesterolchemistry.chemical_classificationNeuronsReactive oxygen speciesDose-Response Relationship DrugChemistryfood and beveragesPolyphenolsNeurodegenerative DiseasesGeneral MedicinePeroxisomeMolecular biologyMitochondriaOxidative StresspolyphenolMitochondrial biogenesislcsh:Biology (General)ApoptosisACOX1Reactive Oxygen SpeciesoxysterolOxidative stressCells
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Transmembrane BAX Inhibitor-1 Motif Containing Protein 5 (TMBIM5) Sustains Mitochondrial Structure, Shape, and Function by Impacting the Mitochondria…

2020

The Transmembrane Bax Inhibitor-1 motif (TMBIM)-containing protein family is evolutionarily conserved and has been implicated in cell death susceptibility. The only member with a mitochondrial localization is TMBIM5 (also known as GHITM or MICS1), which affects cristae organization and associates with the Parkinson&rsquo

Programmed cell deathmitochondrial metabolismProtein familyApoptosisMitochondrioncell survivalArticleGHITMMitochondrial ProteinsTMBIMHumansInner mitochondrial membranelcsh:QH301-705.5bcl-2-Associated X ProteinBAX inhibitor 1ChemistryMembrane ProteinsGeneral MedicineTransmembrane proteinCell biologyDNA-Binding Proteinsmitochondriacell deathMitochondrial biogenesislcsh:Biology (General)Mitochondrial Membranes
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Peptides Derived from the Transmembrane Domain of Bcl-2 Proteins as Potential Mitochondrial Priming Tools

2014

The Bcl-2 family of proteins is crucial for apoptosis regulation. Members of this family insert through a specific C-terminal anchoring trans membrane domain (TMD) in the mitochondrial outer membrane where they hierarchically interact to determine cell fate. While the mitochondrial membrane has been proposed to actively participate in these protein protein interactions, the influence of the TMD in the membrane-mediated interaction is poorly understood. Synthetic peptides (TMD-pepts) corresponding to the putative TMD of antiapoptotic (Bcl-2, Bcl-xL, Bcl-w, and Mcl-1) and pro-apoptotic (Bax, Bak) members were synthesized and characterized. TMD-pepts bound more efficiently to mitochondria-like…

Protein ConformationMolecular Sequence DataCell fate determinationBiochemistryHumansCell LineageAmino Acid SequenceInner mitochondrial membranebiologyChemistryCircular DichroismCytochrome cGeneral MedicineMolecular biologyMitochondriaCell biologystomatognathic diseasesTransmembrane domainMembraneProto-Oncogene Proteins c-bcl-2Cell cultureApoptosisbiology.proteinMolecular MedicinePeptidesBacterial outer membranehuman activitiesHeLa Cells
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Curcumin Affects HSP60 Folding Activity and Levels in Neuroblastoma Cells.

2020

The fundamental challenge in fighting cancer is the development of protective agents able to interfere with the classical pathways of malignant transformation, such as extracellular matrix remodeling, epithelial−mesenchymal transition and, alteration of protein homeostasis. In the tumors of the brain, proteotoxic stress represents one of the main triggering agents for cell transformation. Curcumin is a natural compound with anti-inflammatory and anti-cancer properties with promising potential for the development of therapeutic drugs for the treatment of cancer as well as neurodegenerative diseases. Among the mediators of cancer development, HSP60 is a key factor for the maintenance of…

Protein FoldingCurcuminCell SurvivalCellCatalysisMalignant transformationCell Linelcsh:ChemistryInorganic ChemistryMitochondrial Proteinschemistry.chemical_compoundNeuroblastomaDownregulation and upregulationHeat shock proteinmedicinepost-translational modificationsHumansSecretionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyCell ProliferationHeat shock proteinDose-Response Relationship DrugCommunicationOrganic Chemistrymolecular chaperonesUbiquitinationGeneral MedicineChaperonin 60Computer Science ApplicationsCell biologyUp-RegulationBrain tumorGene Expression Regulation Neoplasticmedicine.anatomical_structurelcsh:Biology (General)lcsh:QD1-999chemistryApoptosisheat shock proteinsMolecular chaperoneCurcuminbrain tumorsHSP60Post-translational modificationHSP60extracellular HSP60International journal of molecular sciences
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Proteins' Knotty Problems

2018

Abstract Knots in proteins are increasingly being recognized as an important structural concept, and the folding of these peculiar structures still poses considerable challenges. From a functional point of view, most protein knots discovered so far are either enzymes or DNA-binding proteins. Our comprehensive topological analysis of the Protein Data Bank reveals several novel structures including knotted mitochondrial proteins and the most deeply embedded protein knot discovered so far. For the latter, we propose a novel folding pathway based on the idea that a loose knot forms at a terminus and slides to its native position. For the mitochondrial proteins, we discuss the folding problem fr…

Protein FoldingProtein ConformationComputational biologyMitochondrial Proteins03 medical and health sciences0302 clinical medicineKnot (unit)Protein structurestomatognathic systemStructural BiologyHumansDatabases ProteinMolecular BiologyMitochondrial protein030304 developmental biologyPhysics0303 health sciencesMembrane Proteinsfood and beveragescomputer.file_formatProtein Data BankMitochondriaDNA-Binding Proteinssurgical procedures operativeMembrane proteincomputer030217 neurology & neurosurgeryJournal of Molecular Biology
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Proteins participating to the post-transcriptional regulation of the mitochondrial cytochrome c oxidase subunit IV via elements located in the 3′UTR

2009

Abstract In developing rat brain cytochrome c oxidase subunit IV (COXIV) expression is also regulated at post-transcriptional level and two 3′UTR-COXIV RNA-binding factors have been identified. Here, we report the enrichment and identification of the factors from just born rat brains by affinity chromatography of biotinylated 3′UTR-COXIV RNA–protein complexes on streptavidin-conjugated paramagnetic particles. We successfully isolated two main proteins of about 86 and 42 kDa, whose sequences were highly attributable to Hsp90 and Actin. The purified proteins maintain RNA-binding ability and specificity for COXIV messenger and, interacting with the 3′UTR, then could negatively modulate mRNA tr…

Protein subunitRNA-binding proteinMitochondrionChromatography AffinityElectron Transport Complex IVMitochondrial ProteinsRats Sprague-DawleySequence Analysis ProteinSerineAnimalsCytochrome c oxidaseHSP90 Heat-Shock ProteinsPhosphorylationPost-transcriptional regulation RNA-binding proteins Mitochondria Cytochrome c oxidase COXIV 3'UTR3' Untranslated RegionsMolecular BiologyPost-transcriptional regulationMessenger RNAbiologyThree prime untranslated regionBrainRNA-Binding ProteinsTranslation (biology)Cell BiologyActinsRatsMolecular WeightAnimals NewbornGene Expression RegulationBiochemistrybiology.proteinMolecular MedicineProtein BindingMitochondrion
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Toward the Standardization of Mitochondrial Proteomics: The Italian Mitochondrial Human Proteome Project Initiative

2017

The Mitochondrial Human Proteome Project aims at understanding the function of the mitochondrial proteome and its crosstalk with the proteome of other organelles. Being able to choose a suitable and validated enrichment protocol of functional mitochondria, based on the specific needs of the downstream proteomics analysis, would greatly help the researchers in the field. Mitochondrial fractions from ten model cell lines were prepared using three enrichment protocols and analyzed on seven different LC-MS/MS platforms. All data were processed using neXtProt as reference database. The data are available for the Human Proteome Project purposes through the ProteomeXchange Consortium with the iden…

Proteomics0301 basic medicineProteomeStandardizationComputational biologyBiologyMitochondrionProteomicsBioinformaticsBiochemistryenrichment protocol; mitochondria; Mitochondrial Human Proteome Project; standardization;Cell LineMitochondrial Proteins03 medical and health sciences0302 clinical medicineTandem Mass SpectrometryHuman proteome projectHumansProtein Interaction MapsSettore BIO/10 - BIOCHIMICAMitochondrial proteinstandardizationChromatographyLiquidNeXtProtChemistry (all)General Chemistrymitochondria030104 developmental biologyItalyenrichment protocolProteomeReference databaseMitochondrial Human Proteome Projectenrichment protocol; mitochondria; Mitochondrial Human Proteome Project; standardization; Cell Line; Chromatography Liquid; Humans; Italy; Mitochondria; Mitochondrial Proteins; Protein Interaction Maps; Proteome; Proteomics; Tandem Mass Spectrometry; Biochemistry; Chemistry (all)030217 neurology & neurosurgeryChromatography Liquid
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Protein modulation in mouse heart under acute and chronic hypoxia

2011

Exploring cellular mechanisms underlying beneficial and detrimental responses to hypoxia represents the object of the present study. Signaling molecules controlling adaptation to hypoxia (HIF-1α), energy balance (AMPK), mitochondrial biogenesis (PGC-1α), autophagic/apoptotic processes regulation and proteomic dysregulation were assessed. Responses to acute hypoxia (AH) and chronic hypoxia (CH) in mouse heart proteome were detected by 2-D DIGE, mass spectrometry and antigen-antibody reactions. Both in AH and CH, the results indicated a deregulation of proteins related to sarcomere stabilization and muscle contraction. Neither in AH nor in CH the HIF-1α stabilization was observed. In AH, the …

ProteomicsCell signalingProteomeImmunoblottingApoptosisBiologyProtein degradationBiochemistryTwo-Dimensional Difference Gel ElectrophoresisMiceContractile ProteinsHeat shock proteinmedicineAnimalsHypoxiaMolecular BiologyHeat-Shock ProteinsAnimalMyocardiumAutophagyAMPK / Animal proteomics / Apoptosis / Autophagy / Heart / HypoxiaApoptosiProteomicAMPKHeat-Shock ProteinHypoxia (medical)Hypoxia-Inducible Factor 1 alpha SubunitCell biologyGene Expression RegulationMitochondrial biogenesisBiochemistrySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationAdenosylhomocysteinaseContractile Proteinmedicine.symptomEnergy MetabolismPROTEOMICS
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Mitochondrial proteomics profile points oxidative phosphorylation as main target for beauvericin and enniatin B mixture

2020

Abstract Beauvericin (BEA) and enniatin B (EN B) are non-legislated Fusarium mycotoxins usually found in cereal and cereal-based products all around the world. By the proteomic analysis of mitochondria enriched extracts from Jurkat cells exposed for 24 h to three concentrations of BEA:EN B (0.01–0.1–0.5 μM), a number of 1821 proteins (202 mitochondrial) were identified and relatively quantified. 340 proteins (59 mitochondrial) were statistically significant altered in our samples (Anova p-value ≤ 0.05 and fold change (FC) ≥1.5). The protein mitochondrial translational release factor 1 like (MTRF1L) was the most abundant protein in the three mycotoxin exposures studied. The mycotoxins mixtur…

ProteomicsTranscription GeneticOxidative phosphorylationMitochondrionToxicologyProteomicsRibosomeJurkat cellsOxidative PhosphorylationElectron TransportMitochondrial ProteinsJurkat Cells03 medical and health scienceschemistry.chemical_compound0404 agricultural biotechnologyDepsipeptidesHumans030304 developmental biology0303 health sciencesfood and beverages04 agricultural and veterinary sciencesGeneral Medicine040401 food scienceBeauvericinFold changeMitochondriachemistryBiochemistryBacterial outer membraneFood ScienceFood and Chemical Toxicology
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