Search results for "Cellular localization"

showing 10 items of 93 documents

Immunohistochemical marker for Na+ CP type Vα (C-20) and heterozygous nonsense SCN5A mutation W822X in a sudden cardiac death induced by mild anaphyl…

2009

A sudden death likely due to mild anaphylactic reaction in a young man is described. Autoptic, histologic, immunohistochemical, and laboratory findings were strongly consistent with the diagnosis of a mild anaphylactic reaction. Genetic molecular analysis, performed on formalin-fixed, paraffin-embedded tissues, showed a mutation described as W822X in a family with electrocardiographic pattern typical of Brugada Syndrome. It results in a nonsense mutation generating a truncated form of the channel protein. The mutation is due to a point substitution of a guanine with an adenine residue (G2466A). Immunohistochemistry and laser scanning confocal microscopy on sections from heart formalin-fixed…

MaleChannellopathies; Confocal laser scanning microscopy; Immunohistochemistry; Na+ CP type Vα (C-20); Sodium channel; Sudden cardiac death; W822X; Adult; Anaphylaxis; Brugada Syndrome; Fatal Outcome; Humans; Male; Muscle Proteins; Myocardium; Myocytes Cardiac; NAV1.5 Voltage-Gated Sodium Channel; Peanut Hypersensitivity; Sodium Channels; Death Sudden Cardiac; Mutation Missense; 2734; Medical Laboratory Technology; HistologyMuscle Proteinsmedicine.disease_causeSodium ChannelsSudden cardiac deathNAV1.5 Voltage-Gated Sodium ChannelNa+ CP type V[alpha] (C-20)Fatal OutcomeMissense mutationMyocytes CardiacConfocal laser scanning microscopyCP type Vα (C-20)Cellular localizationBrugada syndromeBrugada SyndromeMutationChemistrySodium channelChannellopathiesImmunohistochemistryChannellopathies; Confocal laser scanning microscopy; Immunohistochemistry; Na; +; CP type Vα (C-20); Sodium channel; Sudden cardiac death; W822XDeathMedical Laboratory TechnologyCardiologyCardiacAdultmedicine.medical_specialtyHistologyNa+ CP type V[alpha] (C-20) confocal laser scanning microscopy immunohistochemistry sodium channel channellopathies W822X sudden cardiac deathNonsense mutation2734Mutation MissenseSocio-culturaleNa+ CP type Vα (C-20)+Sudden deathPathology and Forensic MedicineInternal medicinemedicineHumansPeanut HypersensitivityNacardiovascular diseasesW822XAnaphylaxisMyocytesSodium channelMyocardiummedicine.diseaseMolecular biologySuddenSudden cardiac deathDeath Sudden CardiacMutationMissenseNa+ CP type V[alpha] (C-20); confocal laser scanning microscopy; immunohistochemistry; sodium channel; channellopathies; W822X; sudden cardiac death
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Immunocytochemistry of M-cadherin in mature and regenerating rat muscle

1994

Background: Cadherins are transmembrane proteins mediating calcium-dependent cell–cell adhesion in a cell type-specific manner by means of homophilic binding. M(muscle)-cadherin is a recently detected member of the cadherin family. Methods: We have investigated the localization of M-cadherin innormal and aneurally regenerating skeletal muscle of rat by means of pre-embedding immunocytochemistry. The antibody was directed against the extra-cellular domain of M-cadherin. Results: Myoblasts and myotubes in regenerating muscles tended to be arranged in clusters enclosed by a common basal lamina. Satellite cells of mature muscle fibers were attached to the underlying fiber without separating bas…

MaleImmunocytochemistryBiologyMuscle DevelopmentReference ValuesExtracellularmedicineAnimalsRegenerationMyocyteTissue DistributionRats WistarCellular localizationMyogenesisCadherinMusclesSkeletal muscleCadherinsImmunohistochemistryAgricultural and Biological Sciences (miscellaneous)Molecular biologyRatsCell biologyMicroscopy Electronmedicine.anatomical_structureBasal laminaAnatomyThe Anatomical Record
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Heterozygous nonsense SCN5A mutation W822X explains a simultaneous sudden infant death syndrome.

2008

The sudden, unexpected, and unexplained death of both members of a set of healthy twins (simultaneous sudden infant death syndrome (SSIDS)) is defined as a case in which both infants meet the definition of sudden infant death syndrome individually. A search of the world medical literature resulted in only 42 reported cases of SSIDS. We report the case of a pair of identical, male, monozygotic twins, 138 days old, who suddenly died, meeting the full criteria of SSIDS and where a genetic screen was performed, resulting in a heterozygous nonsense SCN5A mutation (W822X) in both twins. Immunohistochemistry was performed on cardiac tissue samples utilizing polyclonal antibodies anti-Na+ CP type V…

MalePathologymedicine.medical_specialtyNav1.5 protein functionv1.5 protein functionmedia_common.quotation_subject2734Nonsense mutationNonsenseNa+ channel functionMuscle ProteinsSocio-culturaleBiology+Nav1.5 protein function; Na+ channel function; SCN5A gene mutation; Simultaneous sudden infant death syndrome; W822X mutation; Codon Nonsense; Diseases in Twins; Humans; Infant; Male; Muscle Proteins; NAV1.5 Voltage-Gated Sodium Channel; Sodium Channels; Sudden Infant Death; 2734Sudden deathSodium ChannelsNAV1.5 Voltage-Gated Sodium ChannelPathology and Forensic MedicinePathogenesisSCN5A gene mutationDiseases in TwinsmedicineHumansSimultaneous sudden infant death syndromeSCN5A gene mutationW822X mutationNa+ channel functionNav1.5 protein functionNaSimultaneous sudden infant death syndrome SCN5A gene mutation W822X mutation Na+ channel function Nav1.5 protein function CodonMolecular BiologyCellular localizationmedia_commonSimultaneous sudden infant death syndromeSettore BIO/16 - Anatomia UmanaSimultaneous sudden infant death syndrome SCN5A gene mutation W822X mutation Na+ channel function Nav1.5 protein functionW822X mutationInfantCell BiologyGeneral MedicineSudden infant death syndromeNonsenseTerminal deoxynucleotidyl transferaseCodon NonsenseImmunohistochemistryNa; v; 1.5 protein function; Na; +; channel function; SCN5A gene mutation; Simultaneous sudden infant death syndrome; W822X mutationchannel functionSudden Infant Death
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Inactivation of electrophilic metabolites by glutathione S-transferases and limitation of the system due to subcellular localization

1977

Benzo(a)pyrene was activated to metabolites mutagenic for Salmonella typhimurium TA 98 by liver microsomes from control and phenobarbital treated mice. Under these conditions benzo(a)pyrene 4,5-oxide accounts for most of the mutagenicity. We have therefore investigated (1) the conjugation of benzo(a)pyrene 4,5-oxide with glutathione and (2) the effect of glutathione on the mutagenicity of benzo(a)pyrene.

MaleSalmonella typhimuriumendocrine systemHealth Toxicology and MutagenesisMutagenToxicologymedicine.disease_causeMicechemistry.chemical_compoundCytosolBiotransformationpolycyclic compoundsmedicineAnimalsBenzopyrenesBiotransformationGlutathione Transferasebiologyfungifood and beveragesGeneral MedicineGlutathioneSubcellular localizationGlutathioneCytosolGlutathione S-transferaseBenzo(a)pyrenechemistryBiochemistryMicrosomes Liverbiology.proteinPyreneMutagensArchives of Toxicology
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Time-dependent contribution of non neuronal cells to BDNF production after ischemic stroke in rats.

2010

International audience; Although brain-derived neurotrophic factor (BDNF) plays a central role in recovery after cerebral ischemia, little is known about cells involved in BDNF production after stroke. The present study testes the hypothesis that neurons are not the unique source of neosynthesized BDNF after stroke and that non neuronal-BDNF producing cells differ according to the delay after stroke induction. For this purpose, cellular localization of BDNF and BDNF content of each hemisphere were analysed in parallel before and after (4h, 24h and 8d) ischemic stroke in rats. Stroke of different severities was induced by embolization of the brain with variable number of calibrated microsphe…

MaleTime Factorsmedicine.medical_treatmentCentral nervous systemIschemiaBDNF productionFunctional LateralityBrain IschemiaBrain ischemia03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineNeurotrophic factorsGlial Fibrillary Acidic ProteinmedicineAnimalsRats WistarStrokeCellular localization030304 developmental biologyBrain-derived neurotrophic factorBrain ChemistryNeurons0303 health sciencesbusiness.industryBDNF localization[SCCO.NEUR]Cognitive science/NeuroscienceBrain-Derived Neurotrophic Factor[SCCO.NEUR] Cognitive science/NeuroscienceBrainCell BiologyCerebral Infarctionmedicine.diseaseRatsStrokemedicine.anatomical_structurenervous systemIntracranial Embolism[ SCCO.NEUR ] Cognitive science/NeurosciencebusinessStroke recoveryNeuroscience030217 neurology & neurosurgeryNeurochemistry international
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Brain metabolism of ethanol and alcoholism: an update.

2007

It has long been suggested that some of the neuropharmacological, neurochemical and behavioural effects of ethanol are mediated by its first metabolite, acetaldehyde. In spite of the well documented psychoactivity of acetaldehyde, the precise role of this compound in alcohol abuse remains a matter of intense debate among scientists devoted to the study of alcoholism. Very frequently, the main drawback has been related to the presence of adequate levels of acetaldehyde or its derivatives inside the brain after ethanol ingestion. Since penetration into the central nervous system from blood of peripherically derived acetaldehyde is very low due to the high aldehyde dehydrogenase activity at th…

MetaboliteClinical BiochemistryCentral nervous systemAcetaldehydePharmacologychemistry.chemical_compoundNeurochemicalmedicineAnimalsHumansEthanol metabolismCellular localizationPharmacologyEthanolEthanolDopaminergicAcetaldehydeBrainCentral Nervous System DepressantsCytochrome P-450 CYP2E1CatalaseAlcoholismmedicine.anatomical_structurechemistryEnzyme InductionOxidation-ReductionCurrent drug metabolism
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Tetraspan vesicle membrane proteins: Synthesis, subcellular localization, and functional properties

2002

Tetraspan vesicle membrane proteins (TVPs) are characterized by four transmembrane regions and cytoplasmically located end domains. They are ubiquitous and abundant components of vesicles in most, if not all, cells of multicellular organisms. TVP-containing vesicles shuttle between various membranous compartments and are localized in biosynthetic and endocytotic pathways. Based on gene organization and amino acid sequence similarities TVPs can be grouped into three distinct families that are referred to as physins, gyrins, and secretory carrier-associated membrane proteins (SCAMPs). In mammals synaptophysin, synaptoporin, pantophysin, and mitsugumin29 constitute the physins, synaptogyrin 1-…

Multicellular organismBiochemistryMembrane proteinVesicleSynaptoporinBiologySubcellular localizationPeptide sequenceTransmembrane proteinExocytosisCell biology
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Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell…

2005

AbstractThe movement protein (MP) of Prunus necrotic ringspot virus (PNRSV) is required for cell-to-cell movement. MP subcellular localization studies using a GFP fusion protein revealed highly punctate structures between neighboring cells, believed to represent plasmodesmata. Deletion of the RNA-binding domain (RBD) of PNRSV MP abolishes the cell-to-cell movement. A mutational analysis on this RBD was performed in order to identify in vivo the features that govern viral transport. Loss of positive charges prevented the cell-to-cell movement even though all mutants showed a similar accumulation level in protoplasts to those observed with the wild-type (wt) MP. Synthetic peptides representin…

MutantMolecular Sequence DataPlasmodesmaBiologyCircular dichroismIlarvirusGFPViral ProteinsVirologyMovement proteinTobaccoAmino Acid SequenceMovement proteinRNA binding domainProtein secondary structureProtoplastsRNABiological Transportbiology.organism_classificationSubcellular localizationSubcellular locationMolecular biologyVirusProtein Structure TertiaryPlant LeavesPlant Viral Movement ProteinsPrunus necrotic ringspot virusRNA ViralCell-to-cell movementPeptidesProteïnesPrunus necrotic ringspot virusBinding domainVirology
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p75NTRin the spleen: Age-dependent changes, effect of NGF and 4-methylcatechol treatment, and structural changes in p75NTR-deficient mice

2003

In addition to their well-known actions within the nervous system, neurotrophins and their receptors are involved in immune system functioning, as demonstrated by their wide distribution in lymphoid tissues and their in vitro actions on immunocompetent cells. Nevertheless, the in vivo roles of neurotrophin-receptor systems in lymphoid tissues, as well as the scope of their influence throughout development and adulthood, are yet to be clarified. In the present study, we used combined morphological and immunohistochemical techniques to investigate the presence and cellular localization of p75NTR, the pan-neurotrophin receptor protein, in rat spleen from newborns to aging individuals, and the …

Nervous systemWhite pulpmedicine.medical_specialtyPathologybiologySpleenAgricultural and Biological Sciences (miscellaneous)medicine.anatomical_structureImmune systemNerve growth factorEndocrinologyInternal medicinemedicinebiology.proteinsense organsAnatomyReceptorCellular localizationNeurotrophinThe Anatomical Record Part A: Discoveries in Molecular, Cellular, and Evolutionary Biology
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Post-translational modifications on RNA-binding proteins: accelerators, brakes, or passengers in neurodegeneration?

2021

RNA-binding proteins (RBPs) are critical players in RNA expression and metabolism, thus, the proper regulation of this class of proteins is critical for cellular health. Regulation of RBPs often occurs through post-translational modifications (PTMs), which allow the cell to quickly and efficiently respond to cellular and environmental stimuli. PTMs have recently emerged as important regulators of RBPs implicated in neurodegenerative disorders, in particular amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Here, we summarize how disease-associated PTMs influence the biophysical properties, molecular interactions, subcellular localization, and function of ALS/FTD-linked …

NeurodegenerationCellAmyotrophic Lateral SclerosisRNA-Binding ProteinsRNA-binding proteinBiologymedicine.diseaseSubcellular localizationBiochemistrymedicine.anatomical_structureFrontotemporal Dementiamental disordersmedicinePosttranslational modificationHumansRNA-Binding Protein FUSAmyotrophic lateral sclerosisMolecular BiologyNeuroscienceProtein Processing Post-TranslationalFunction (biology)Frontotemporal dementiaTrends in biochemical sciences
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