Search results for "Dop"

showing 10 items of 4870 documents

BAG3 regulates total MAP1LC3B protein levels through a translational but not transcriptional mechanism

2015

Autophagy is mainly regulated by post-translational and lipid modifications of ATG proteins. In some scenarios, the induction of autophagy is accompanied by increased levels of certain ATG mRNAs such as MAP1LC3B/LC3B, ATG5 or ATG12. However, little is known about the regulation of ATG protein synthesis at the translational level. The cochaperone of the HSP70 system BAG3 (BCL2-associated athanogene 3) has been associated to LC3B lipidation through an unknown mechanism. In the present work, we studied how BAG3 controls autophagy in HeLa and HEK293 cells. Our results showed that BAG3 regulates the basal amount of total cellular LC3B protein by controlling its mRNA translation. This effect was …

0301 basic medicineProteasome Endopeptidase ComplexTranscription GeneticATG8ATG5BiologyBAG3ATG1203 medical and health sciences0302 clinical medicineProtein biosynthesisHumansRNA MessengerMolecular BiologyAdaptor Proteins Signal TransducingGeneticsGene knockdownAutophagyCell BiologyLipidsBasic Research PaperCell biologyHEK293 Cells030104 developmental biologyProtein BiosynthesisProteolysisApoptosis Regulatory ProteinsLysosomesMicrotubule-Associated ProteinsMAP1LC3B030217 neurology & neurosurgeryHeLa Cells
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Allopurinol partially prevents disuse muscle atrophy in mice and humans

2018

AbstractDisuse muscle wasting will likely affect everyone in his or her lifetime in response to pathologies such as joint immobilization, inactivity or bed rest. There are no good therapies to treat it. We previously found that allopurinol, a drug widely used to treat gout, protects muscle damage after exhaustive exercise and results in functional gains in old individuals. Thus, we decided to test its effect in the prevention of soleus muscle atrophy after two weeks of hindlimb unloading in mice, and lower leg immobilization following ankle sprain in humans (EudraCT: 2011-003541-17). Our results show that allopurinol partially protects against muscle atrophy in both mice and humans. The pro…

0301 basic medicineProteasome Endopeptidase Complexmedicine.medical_specialtyScience[SDV]Life Sciences [q-bio]Allopurinolmedicine.medical_treatmentAllopurinolHindlimbBed restArticleMice03 medical and health sciences0302 clinical medicineAtrophyPhysical Conditioning AnimalInternal medicineAnimalsHumansMedicineAnkle InjuriesMuscle SkeletalWastingSoleus muscleMultidisciplinaryUbiquitinbusiness.industryQRmedicine.diseaseMuscular Disorders AtrophicMuscle atrophy3. Good healthGoutMuscular Atrophy030104 developmental biologyEndocrinologyHindlimb SuspensionMedicinemedicine.symptombusiness030217 neurology & neurosurgerymedicine.drugScientific Reports
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Ephestia kuehniella tolerance to Bacillus thuringiensis Cry1Aa is associated with reduced oligomer formation

2016

The basis of the different susceptibility of Ephestia kuehniella to the Cry1Aa and Cry1Ac δ-endotoxins from Bacillus thuringiensis kurstaki BNS3 was studied. Both toxins bound specifically to the BBMV of E. kuehniella. The result of the ligand blot showed that Cry1Ac bound to three putative receptors of about 100, 65 and 80 kDa and Cry1Aa interacted only with a 100 kDa protein. Pronase digestion of the BBMV-bound toxins was used to analyze the toxin insertion. Both toxins inserted into the BBMV as monomers however, a 14 kDa peptide of α4-α5 which correspond to the oligomeric form of this peptide was detected in case of Cry1Ac only. Analysis of the in vitro oligomerisation of these toxins in…

0301 basic medicineProtein ConformationBacillus thuringiensisBiophysicsPeptidemedicine.disease_causeBiochemistryOligomerHemolysin Proteins03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsBacillus thuringiensismedicineAnimalsReceptorMolecular Biologychemistry.chemical_classificationBacillus thuringiensis Toxins030102 biochemistry & molecular biologybiologyToxinfungiCell BiologyLigand (biochemistry)biology.organism_classificationEndotoxinsLepidopteraBlot030104 developmental biologyBiochemistryCry1AcchemistryProtein MultimerizationBiochemical and Biophysical Research Communications
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Phosphorylation of meprin β controls its cell surface abundance and subsequently diminishes ectodomain shedding

2021

Meprin β is a zinc-dependent metalloprotease exhibiting a unique cleavage specificity with strong preference for acidic amino acids at the cleavage site. Proteomic studies revealed a diverse substrate pool of meprin β including the interleukin-6 receptor (IL-6R) and the amyloid precursor protein (APP). Dysregulation of meprin β is often associated with pathological conditions such as chronic inflammation, fibrosis, or Alzheimer's disease (AD). The extracellular regulation of meprin β including interactors, sheddases, and activators has been intensively investigated while intracellular regulation has been barely addressed in the literature. This study aimed to analyze C-terminal phosphorylat…

0301 basic medicineProtein Kinase C-alphaImmunoprecipitationmedia_common.quotation_subjectBiochemistry03 medical and health sciences0302 clinical medicineProtein Kinase C betaTumor Cells CulturedGeneticsAmyloid precursor proteinHumansPhosphorylationInternalizationMolecular BiologyProtein kinase Cmedia_commonbiologyChemistryCell MembraneMetalloendopeptidasesSheddaseCell biology030104 developmental biologyGene Expression RegulationEctodomainColonic NeoplasmsProteolysisbiology.proteinPhosphorylationExtracellular Space030217 neurology & neurosurgeryIntracellularBiotechnologyThe FASEB Journal
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Mcl-1 and Bok transmembrane domains : Unexpected players in the modulation of apoptosis

2020

The Bcl-2 protein family comprises both proand antiapoptotic members that control the permeabilization of the mitochondrial outer membrane, a crucial step in the modulation of apoptosis. Recent research has demonstrated that the carboxyl-terminal transmembrane domain (TMD) of some Bcl-2 protein family mem-bers can modulate apoptosis; however, the transmembrane interactome of the antiapoptotic protein Mcl-1 remains largely unexplored. Here, we demonstrate that the Mcl-1 TMD forms homooligomers in the mitochondrial membrane, competes with full-length Mcl-1 protein with regards to its antiapoptotic function, and induces cell death in a Bok-dependent manner. While the Bok TMD oligomers locate p…

0301 basic medicineProtein familyMitochondrionBCL-X(L)Endoplasmic ReticulumInteractome114 Physical sciences03 medical and health sciencesBok0302 clinical medicineProtein DomainsMITOCHONDRIAhemic and lymphatic diseasesAnimalsHumansBcl-2Inner mitochondrial membraneMultidisciplinaryCell DeathChemistryEndoplasmic reticulumapoptosisMcl-1PATHWAYSLOCALIZATIONBiological SciencesTransmembrane protein3. Good healthCell biologytransmembraneTransmembrane domainstomatognathic diseasesGLYCOPHORIN-A DIMERIZATION030104 developmental biologyHELIX PACKINGProto-Oncogene Proteins c-bcl-2BAX030220 oncology & carcinogenesisMitochondrial MembranesPROSURVIVAL BCL-2 PROTEINSMOTIFSURVIVALMyeloid Cell Leukemia Sequence 1 Protein1182 Biochemistry cell and molecular biologyBacterial outer membraneHeLa Cells
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Human R1441C LRRK2 regulates the synaptic vesicle proteome and phosphoproteome in a Drosophila model of Parkinson's disease

2016

International audience; Mutations in leucine-rich repeat kinase 2 (LRRK2) cause late-onset, autosomal dominant familial Parkinsons disease (PD) and variation at the LRRK2 locus contributes to the risk for idiopathic PD. LRRK2 can function as a protein kinase and mutations lead to increased kinase activity. To elucidate the pathophysiological mechanism of the R1441C mutation in the GTPase domain of LRRK2, we expressed human wild-type or R1441C LRRK2 in dopaminergic neurons of Drosophila and observe reduced locomotor activity, impaired survival and an age-dependent degeneration of dopaminergic neurons thereby creating a new PD-like model. To explore the function of LRRK2 variants in vivo, we …

0301 basic medicineProteomerab3 GTP-Binding Proteinsalpha-synucleindomainSyntaxin 1Interactomedopaminergic-neuronsAnimals Genetically Modifiedchemistry.chemical_compound0302 clinical medicinemicrotubule stabilityDrosophila ProteinsProtein Interaction MapsGenetics (clinical)LRRK2 GeneKinasephosphorylationBrainParkinson DiseaseArticlesGeneral Medicineautosomal-dominant parkinsonismLRRK2Drosophila melanogasterSynaptotagmin IProteomePhosphorylationSynaptic VesiclesNerve Tissue ProteinsBiologyLeucine-Rich Repeat Serine-Threonine Protein Kinase-203 medical and health sciencesGeneticsAnimalsHumansKinase activitygeneMolecular BiologyAlpha-synucleingtp-bindingDopaminergic Neuronsrepeat kinase 2Molecular biologyPhosphoric Monoester Hydrolasesnervous system diseasesDisease Models Animal030104 developmental biologyGene Expression Regulationchemistrymutation030217 neurology & neurosurgery[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
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Ethnopharmacology of Love

2018

Background: Elixirs conferring eternal youth or inducing amatory and erotic attraction have been searched for without success. Lovesickness is a widespread affliction resulting from unrequited love and/or the impossibility for physical and emotional union. The symptoms are reflections of altered dopamine, serotonin, noradrenaline, testosterone and cortisol levels and range from frenzy and intrusive thinking to despair and depression, sharing traits with the neurochemistry of addiction and compulsive behavior disorder. Although it can seriously impact the quality of life, lovesickness is currently not considered in official disease classification systems. Consequently, no official therapeuti…

0301 basic medicinePsychotherapistmedia_common.quotation_subjectethnomedicineReviewaphrodisiacs03 medical and health sciences0302 clinical medicinemedicinesexPharmacology (medical)LovesicknessFalling in lovemedia_commonPharmacologybeta-caryophylleneInfatuationinfatuationAddictionlcsh:RM1-950RomanceserotoninVentral tegmental area030104 developmental biologymedicine.anatomical_structurelcsh:Therapeutics. PharmacologylovesicknessCompulsive behaviormedicine.symptomdopaminePsychology030217 neurology & neurosurgeryUnrequited loveFrontiers in Pharmacology
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Metabolic and inflammatory reprogramming of macrophages by ONC201 translates in a pro-inflammatory environment even in presence of glioblastoma cells

2020

Tumor-associated macrophages facilitate tumor progression and resistance to therapy. Their capacity for metabolic and inflammatory reprogramming represents an attractive therapeutic target. ONC201/TIC10 is an anticancer molecule that antagonizes the dopamine receptor D2 and affects mitochondria integrity in tumor cells. We examined whether ONC201 induces a metabolic and pro-inflammatory switch in primary human monocyte-derived macrophages that reactivates their antitumor activities, thus enhancing the onco-toxicity of ONC201. Contrary to glioblastoma cells, macrophages exhibited a low ratio of dopamine receptors D2/D5 gene expression and were resistant to ONC201 cytotoxicity. Macrophages re…

0301 basic medicinePyridinesImmunology610 MedizinGlutamic AcidAntineoplastic AgentsMitochondrionBiology570 Life sciences03 medical and health sciences0302 clinical medicineImmune systemCell Line TumorDopamine receptor D2610 Medical sciencesTumor MicroenvironmentHumansImmunology and AllergyMacrophageReceptors Dopamine D5Tumor microenvironmentReceptors Dopamine D2MacrophagesImidazolesMitochondriaCell biologyGene Expression Regulation NeoplasticPyrimidines030104 developmental biologyDrug Resistance NeoplasmTumor progressionDopamine receptorEnergy MetabolismGlioblastomaReprogrammingTranscription Factor CHOPSignal Transduction030215 immunology570 Biowissenschaften
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RPGR protein complex regulates proteasome activity and mediates store-operated calcium entry

2018

Ciliopathies are a group of genetically heterogeneous disorders, characterized by defects in cilia genesis or maintenance. Mutations in the RPGR gene and its interacting partners, RPGRIP1 and RPGRIP1L, cause ciliopathies, but the function of their proteins remains unclear. Here we show that knockdown (KD) of RPGR, RPGRIP1 or RPGRIP1L in hTERT-RPE1 cells results in abnormal actin cytoskeleton organization. The actin cytoskeleton rearrangement is regulated by the small GTPase RhoA via the planar cell polarity (PCP) pathway. RhoA activity was upregulated in the absence of RPGR, RPGRIP1 or RPGRIP1L proteins. In RPGR, RPGRIP1 or RPGRIP1L KD cells, we observed increased levels of DVl2 and DVl3 pr…

0301 basic medicineRMRHOAactin cytoskeletonbiologyChemistryEndoplasmic reticulumCiliumSTIM1RPGR complex030105 genetics & heredityActin cytoskeletonStore-operated calcium entryActin cytoskeleton organizationeye diseasesCell biology03 medical and health sciencesendoplasmic reticulum030104 developmental biologyciliopathyOncologybiology.proteinSmall GTPasestore-operated Ca2+ entryResearch PaperOncotarget
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A FRAP-Based Method for Monitoring Molecular Transport in Ciliary Photoreceptor Cells In Vivo

2016

The outer segment of rod and cone photoreceptor cells represents a highly modified primary sensory cilium. It renews on a daily basis throughout lifetime and effective vectorial transport to the cilium is essential for the maintenance of the photoreceptor cell function. Defects in molecules of transport modules lead to severe retinal ciliopathies. We have recently established a fluorescence recovery after photobleaching (FRAP)-based method to monitor molecular trafficking in living rodent photoreceptor cells. We irreversibly bleach the fluorescence of tagged molecules (e.g. eGFP-Rhodopsin) in photoreceptor cells of native vibratome sections through the retina by high laser intensity. In the…

0301 basic medicineRetinagenetic structuresbiologyChemistryCiliumFluorescence recovery after photobleachingRetinalRod Cell Outer SegmentPhotoreceptor cellTransport protein03 medical and health scienceschemistry.chemical_compound030104 developmental biologymedicine.anatomical_structureRhodopsinmedicineBiophysicsbiology.proteinsense organs
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