Search results for "Molecular sequence"

showing 10 items of 1972 documents

Activation of alpha-1A adrenoceptors mobilizes calcium from the intracellular stores in myocytes from rat portal vein.

1994

International audience; Intracellular free Ca++ concentration ([Ca++]i) was monitored using the fluorescence from the dye fura-2-acetoxymethylester in single myocytes from rat portal vein. In the presence of oxodipine (a L-type Ca++ channel inhibitor), norepinephrine (10 microM) evoked transient increases in [Ca++]i which were related to release of Ca++ from intracellular stores. The alpha-1 adrenoceptors mediating intracellular Ca++ release and inositol phosphate accumulation were identified by using subtype-selective agonists and antagonists. Pretreatment with chloroethylclonidine had little effect on the norepinephrine-induced increase in [Ca++]i and inositol phosphate accumulation. In c…

Portal VeinInositol Phosphates[SDV]Life Sciences [q-bio]Molecular Sequence Data[SDV.BC]Life Sciences [q-bio]/Cellular Biology[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]In Vitro TechniquesAntibodiesMuscle Smooth VascularRats[SDV] Life Sciences [q-bio]NorepinephrineChloride ChannelsReceptors Adrenergic alpha-1[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]AnimalsCalciumAmino Acid SequenceRats Wistar[SDV.BC] Life Sciences [q-bio]/Cellular BiologyAdrenergic alpha-AntagonistsCells CulturedSignal Transduction
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Demonstration of an endocrine signaling circuit for insulin in the sponge Geodia cydonium.

1989

Abstract The existence of an insulin-mediated cell-to-cell signaling in the sponge Geodia cydonium is demonstrated in this study by molecular biological and immunological techniques. The sequence of a sponge cDNA clone encoding preproinsulin was analyzed for the first time and determined to comprise a high homology to human preproinsulin (60-80% homology). The predicted polypeptide of preproinsulin from sponge contains two disulfide bridges which link the A- to the B-chain. The intra-A chain disulfide bridge is absent. Applying immunological and electron microscopical techniques it is shown that insulin is produced in specialized cells (spherulous cells). Experimental evidence is presented …

PreproinsulinAnnexinsCellular differentiationBlotting WesternMolecular Sequence DataBiologyGeneral Biochemistry Genetics and Molecular BiologySequence Homology Nucleic AcidAnimalsHumansInsulinAmino Acid SequenceProtein PrecursorsReceptorMolecular BiologyPancreatic hormoneProinsulinGeneral Immunology and MicrobiologyBase SequenceGeneral NeuroscienceCalcium-Binding ProteinsDNAImmunohistochemistryReceptor InsulinPoriferaMicroscopy ElectronBiochemistryGene Expression RegulationHormone receptorSignal transductionHormoneResearch ArticleProinsulinSignal Transduction
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Sequence evolution, processing, and posttranslational modification of zonadhesin D domains in primates, as inferred from cDNA data

2005

Zonadhesin is a mammalian transmembrane sperm ligand. Precursor zonadhesin essentially consists of MAM (meprin/A5 antigen/mu receptor tyrosine phosphatase) domains, a mucin-like repeat, and D domains (homologous to von Willebrand D). Recent immunovisualization and binding assays indicate that zonadhesin D domains 1–3 bind postacrosomally to the zona pellucida. This feature has attracted considerable interest in the evolution of zonadhesin and its possible biological and biomedical implications. Previous molecular evolutionary analyses, however, were confined to cDNA sequences of only few distantly related species. Moreover, except for rabbit and pig, little is known about zonadhesin’s proce…

PrimatesDNA ComplementaryBase pairMolecular Sequence DataBiologyPROSITEEvolution MolecularComplementary DNAGeneticsmedicineAnimalsAmino Acid SequenceSelection GeneticZona pellucidaPhylogenyGeneticsComputational BiologyMembrane ProteinsGeneral MedicineLigand (biochemistry)Transmembrane proteinProtein Structure Tertiarymedicine.anatomical_structureEvolutionary biologyGenBankDimerizationProtein Processing Post-TranslationalSequence AlignmentFunction (biology)Protein Modification TranslationalGene
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Interaction of 68–kDa TAR RNA-binding protein and other cellular proteins with rpion protein-RNA stem-loop

1995

The RNA stem-loop structure of the trans-activating region TAR sequence of human immunodeficiency virus-1 mRNA is the binding site for a number of host cell proteins. A virtually identical set of proteins from HeLa nuclear extracts was found to bind to the predicted RNA hairpin element of prion protein (PrP) mRNA, as demonstrated in UV cross-linking/RNase protection and Northwestern assays. We show that the cellular TAR loop-binding protein, p68, is among those proteins which associate with PrP RNA. Competition experiments with various TAR RNA mutants revealed that binding of partially purified p68 to PrP RNA stem-loop occurs sequence-specifically. The 100-kDa 2-5A synthetase which is invol…

PrionsBlotting WesternMolecular Sequence DataRNA-dependent RNA polymeraseReceptors Cell SurfaceRNA-binding proteinBiologyBinding CompetitiveCellular and Molecular NeuroscienceVirology2'5'-Oligoadenylate SynthetaseHumansLymphocytesHIV Long Terminal RepeatBase SequenceRNA-Binding ProteinsRNABlotting NorthernNon-coding RNAMolecular biologyRNA silencingNeurologyMutagenesisRNA editingeIF4ANucleic Acid ConformationNeurology (clinical)Small nuclear RNAHeLa CellsJournal of Neurovirology
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Effect of flupirtine on Bcl-2 and glutathione level in neuronal cells treated in vitro with the prion protein fragment (PrP106-126).

1997

Flupirtine, trade name Katadolon, is a centrally acting nonopioid analgesic that has recently been found to display cytoprotective activity in vitro and in vivo on neurons induced to undergo apoptosis. This report shows that the PrP106-126 fragment of the prion protein, which is the likely etiological agent for a series of encephalopathies, is toxic to cortical neurons in vitro. Simultaneously, PrP106-126 influences the molecular GSH content and the bcl-2 expression in neurons. Significant toxicity (32% reduction in cell viability) was observed at a concentration of 50 microM of the peptide after 9 days of incubation, while at higher concentrations toxicity increased to 70%. Neurotoxicity w…

PrionsMolecular Sequence DataAminopyridinesApoptosisPharmacologyBiologychemistry.chemical_compoundDevelopmental NeurosciencemedicineAnimalsAmino Acid SequenceRats WistarCytotoxicityCells CulturedNeuronsNeurotoxicityGlutathioneAnalgesics Non-Narcoticmedicine.diseaseGlutathioneIn vitroPeptide FragmentsGenes bcl-2RatsOxidative StressNeuroprotective AgentsNeurologychemistryGene Expression RegulationProto-Oncogene Proteins c-bcl-2ApoptosisCell cultureImmunologyToxicityFlupirtineOxidation-Reductionmedicine.drugExperimental neurology
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Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

2009

Abstract Both the cellular prion protein (PrPc) and the amyloid precursor protein (APP) are physiologically subjected to complex proteolytic processing events. While for APP the proteinases involved – alpha-, beta- and gamma-secretase – have been identified in vitro and in vivo, the cleavage of PrPc by now has been linked only to the shedding activity of the metalloproteinase ADAM10 and/or ADAM17 in cell culture. Here we show that neuronal overexpression of the alpha-secretase ADAM10 in mice reduces all PrPc species detected in the brain instead of leading to enhanced amounts of specific cleavage products of PrPc. Additionally, the incubation time of mice after scrapie infection is signific…

Prionsanimal diseasesADAM10Molecular Sequence DataPrion diseaseScrapieMice Transgeniclcsh:RC321-571ADAM10 ProteinMiceIn vivomental disordersNeurotoxicitymedicineAmyloid precursor proteinAnimalsHumansGliosisAmino Acid Sequencealpha-Secretaselcsh:Neurosciences. Biological psychiatry. NeuropsychiatrySheddingMetalloproteinasebiologyChemistryBrainMembrane ProteinsMolecular biologyIn vitronervous system diseasesMice Inbred C57BLADAM ProteinsNeurologyAlpha secretaseGliosisbiology.proteinCattlemedicine.symptomAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalScrapieNeurobiology of disease
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Functional characterization of two melanocortin (MC) receptors in lamprey showing orthology to the MC1 and MC4 receptor subtypes

2007

Abstract Background The melanocortin (MC) receptors have a key role in regulating body weight and pigmentation. They belong to the rhodopsin family of G protein-coupled receptors (GPCRs). The purpose of this study was to identify ancestral MC receptors in agnathan, river lamprey. Results We report cloning of two MC receptors from river lamprey. The lamprey receptors, designated MCa and MCb, showed orthology to the MC1 and MC4 receptor subtypes, respectively. The molecular clock analysis suggested that lamprey MC receptor genes were not duplicated recently and diverged from each other more than 400 MYR ago. Expression and pharmacological characterization showed that the lamprey MCa receptor …

Pro-OpiomelanocortinSecond Messenger SystemsGene DuplicationProtein Interaction MappingCyclic AMPPetromyzonReceptorPhylogenyCell Line TransformedSkinGeneticsbiologyReceptors MelanocortinMelanocortin 3 receptorCell biologyOrgan SpecificityRhodopsinReceptor Melanocortin Type 4HagfishesMelanocortinReceptor Melanocortin Type 1Protein BindingResearch ArticleEvolutionRecombinant Fusion ProteinsMolecular Sequence DataBinding CompetitivePeptides CyclicEvolution Moleculargamma-MSHAdrenocorticotropic HormoneSpecies SpecificityMelanocortin receptorbeta-MSHQH359-425AnimalsHumansAmino Acid SequenceEcology Evolution Behavior and SystematicsGene LibraryG protein-coupled receptorBinding SitesSequence Homology Amino AcidFuguLampreybiology.organism_classificationPeptide FragmentsVisceraalpha-MSHbiology.proteinCosyntropinSequence Alignmenthuman activitiesBMC Evolutionary Biology
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A family with various symptomatology suggestive of Anderson-Fabry disease and a genetic polymorphism of alpha galactosidase A gene.

2014

Background: Anderson/Fabry disease expresses a wide range of clinical variability in patients that it is possible to explain referring to a genetic variability with numerous mutations described in the literature (more than 600). Methods: We report some clinical cases of some members of a Sicilian family to express phenotypical variability of this disease in subjects with the same genetic mutation. Results: The first case was a 59-year-old female. Brain MRI revealed right frontal periventricular white matter of likely vascular-degenerative origin. The proband's alpha galactosidase A activity was 3.7. nmol/mL/h. Molecular genetics revealed a polymorphism: - 10 C. >. T; IVS 2-76_80del5; IVS…

ProbandAdultMalemedicine.medical_specialtyPathologySettore MED/09 - Medicina InternaAdolescentClinical BiochemistryMolecular Sequence DataBiologyAnderson-Fabry diseaseNucleic Acid DenaturationGastroenterologyPolymorphism (computer science)Internal medicineMolecular geneticsmedicineHaplotypeHumansFamilyGenetic Predisposition to DiseaseGenetic variabilitySymptomatologyChildPolymorphism GeneticBase SequenceHaplotypeHeterozygote advantageGeneral MedicineMiddle Agedmedicine.diseaseFabry diseaseMagnetic Resonance ImagingPedigreealpha-GalactosidaseFabry DiseaseMicroalbuminuriaFemaleHumanClinical biochemistry
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ATP1A2 mutations in 11 families with familial hemiplegic migraine.

2005

Abstract Familial hemiplegic migraine (FHM) is an autosomal dominant form of migraine with aura. The disease is caused by mutations of at least three genes among which two have been identified, CACNA1A and ATP1A2. Very few mutations have been identified so far in ATP1A2. We screened the coding sequence of ATP1A2 in 26 unrelated FHM probands in whom CACNA1A screening was negative. A total of eight different mutations were identified in 11 of the probands (41%), including six missense mutations, one small deletion leading to a frameshift, and one in frame deletion. All were novel mutations. Two mutations were recurrent, in three and two families, respectively. Genotyping of 94 relatives of th…

ProbandMaleMigraine with AuraMolecular Sequence DataMutation MissenseBiologymedicine.disease_causeFrameshift mutationATP1A2GeneticsmedicineMissense mutationAnimalsHumansAmino Acid SequenceGenotypingGenetics (clinical)Familial hemiplegic migraineGeneticsFamily HealthMutationPolymorphism GeneticSequence Homology Amino AcidExonsmedicine.diseaseMigraine with auraPedigreeMutationFemalemedicine.symptomSodium-Potassium-Exchanging ATPase
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Poriferan survivin exhibits a conserved regulatory role in the interconnected pathways of cell cycle and apoptosis

2010

Survivin orchestrates intracellular pathways during cell division and apoptosis. Its central function as mitotic regulator and inhibitor of cell death has major implications for tumor cell proliferation. Analyses in early-branching Metazoa so far propose an exclusive role of survivin as a chromosomal passenger protein, whereas only later during evolution a complementary antiapoptotic function might have arisen, concurrent with increased organismal complexity. To lift the veil on the ancestral function(s) of this key regulator, a survivin-like protein (SURVL) of one of the earliest-branching metazoan taxa was identified and functionally characterized. SURVL of the sponge Suberites domuncula …

Programmed cell deathCell divisionRecombinant Fusion ProteinsMolecular Sequence DataApoptosisTransfectionCell LineInhibitor of Apoptosis ProteinsLipopeptidesSurvivinAnimalsHumansAmino Acid SequenceMolecular BiologyMitosisGeneticsOriginal PaperBase SequencebiologyCell CycleCell BiologyCell cyclebiology.organism_classificationCell biologySuberites domunculaCell cultureCaspasesSuberitesSequence AlignmentCell DivisionIntracellularCadmiumCell Death & Differentiation
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