Search results for "Protein Isoforms"

showing 10 items of 175 documents

Biallelic mutations in neurofascin cause neurodevelopmental impairment and peripheral demyelination

2019

See Karakaya and Wirth (doi:10.1093/brain/awz273) for a scientific commentary on this article. Neurofascin (NFASC) isoforms are immunoglobulin cell adhesion molecules involved in node of Ranvier assembly. Efthymiou et al. identify biallelic NFASC variants in ten unrelated patients with a neurodevelopmental disorder characterized by variable degrees of central and peripheral involvement. Abnormal expression of Nfasc155 is accompanied by severe loss of myelinated fibres.

Male[SDV]Life Sciences [q-bio][SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/NeurobiologyNerve Fibers MyelinatedGene FrequencyNeurodevelopmental Disorder[SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB]Nerve Growth FactorProtein IsoformsChildComputingMilieux_MISCELLANEOUSMyelin Sheathneurofascin; neurodevelopment; peripheral demyelinationAlleleneurodevelopmentDemyelinating DiseaseGenomicsneurodevelopment neurofascin peripheral demyelinationSettore MED/39 - Neuropsichiatria InfantilePedigree[SDV.IMM.IA]Life Sciences [q-bio]/Immunology/Adaptive immunologyChild PreschoolPeripheral Nerve[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Femaleneurodevelopment; neurofascin; peripheral demyelinationNeurogliaHumanAdultAdolescentNervous System MalformationsGuillain-Barre SyndromeAxonNervous System MalformationneurofascinRanvier's NodesHumansNerve Growth FactorsPeripheral NervesAllelesAutoantibodiesperipheral demyelinationInfantProtein IsoformOriginal ArticlesAxonsnervous systemNeurodevelopmental DisordersCell Adhesion MoleculeMutationCell Adhesion MoleculesDemyelinating Diseases
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The neuropeptide calcitonin gene-related peptide differently modulates proliferation and differentiation of smooth muscle cells in culture depending …

2001

Abstract Calcitonin gene-related peptide (CGRP) is a neuropeptide present around vasculature very early during development, when smooth muscle cells (SMC) are still proliferating and not yet totally differentiated. We investigated the effects of CGRP on proliferation and differentiation of SMC in culture; 10 −7 M CGRP added in the medium of cultured smooth muscle cells every 2 days did not significantly changed cells growth rate in 1% FCS. At the opposite, this treatment modulated proliferation of cells grown in 10% FCS medium. Two distinct populations of SMC with different growth rates were obtained from our primary cultures. SMC which proliferated slowly in the presence of 10% fetal calf …

Malemedicine.medical_specialtyCell typePhysiologyAngiogenesisCalcitonin Gene-Related PeptideBlotting WesternClinical BiochemistryNeuropeptideAorta ThoracicCalcitonin gene-related peptideBiologyBiochemistryMuscle Smooth VascularCellular and Molecular NeuroscienceEndocrinologySpecies SpecificityInternal medicineCell AdhesionmedicineAnimalsHumansProtein IsoformsRNA MessengerRats WistarCells CulturedActinCell SizeCell growthCell DifferentiationActinsCulture MediaRatsCell biologyKineticsEndocrinologyCalcitoninBlood VesselsCell DivisionHomeostasisRegulatory Peptides
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Effects of combined strength and sprint training on regulation of muscle contraction at the whole-muscle and single-fibre levels in elite master spri…

2008

The aims of this study were to investigate the mechanisms underlying (1) the ageing-related motor handicap at the whole muscle, cellular, contractile protein and myonuclear levels; and (2) ageing-related differences in muscle adaptability.In vivo muscles function was studied in the knee extensors. Decreases were observed in isokinetic and isometric torque outputs in old age in the sedentary men and women and elite master sprinters. A 20-week long specific sprint and resistance training successfully improved the maximal isometric force and rate of force development in a subgroup of master sprinters.In vitro measurements were performed in muscle biopsies from the vastus lateralis muscle. Immu…

Malemedicine.medical_specialtyPhysiologyVastus lateralis muscleBiopsyMuscle Fibers SkeletalIsometric exerciseBiologyRunningMuscle hypertrophyMyofibrilsIsometric ContractionInternal medicinemedicineHumansProtein IsoformsMuscle StrengthExercise physiologyMuscle SkeletalExerciseAgedAdenosine TriphosphatasesLegMyosin Heavy ChainsElectromyographyAnatomyMiddle Agedmusculoskeletal systemEndocrinologySprintAgeingmedicine.symptomMyofibrilMuscle ContractionMuscle contractionActa Physiologica
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Permissive and suppressive effects of dexamethasone on enzyme induction in hepatocyte co-cultures.

2002

1. Steroids are known to act as permissive factors in hepatocytes. This study shows that dexamethasone (DEX) is a permissive factor for induction of CYP2B1/2, CYP3A1, CYP2A1 and probably also CYP2C11 in cultures with primary rat hepatocytes. 2. The induction factor of phenobarbital (PB)-induced formation of 16beta-hydroxytestosterone (OHT), a testosterone biotransformation product predominantly formed by CYP2B1, is increased 18-fold by the addition of 32 nM DEX to the culture medium. Interestingly, higher concentrations of DEX up to 1000 nM led to a concentration-dependent maximally 5-fold decrease (p = 0.002) of phenobarbital-induced 16beta-OHT formation compared with the effect observed w…

Malemedicine.medical_specialtyTime FactorsHealth Toxicology and MutagenesisAnti-Inflammatory AgentsBiologyToxicologyBiochemistryDexamethasoneRats Sprague-DawleyEnzyme activatorInternal medicinepolycyclic compoundsmedicineCytochrome P-450 CYP1A1AnimalsCytochrome P-450 CYP3AProtein IsoformsPermissiveEnzyme inducerCytochrome P450 Family 2DexamethasoneCells CulturedPharmacologyCryopreservationDose-Response Relationship DrugBiological activityGeneral MedicineIn vitroCoculture TechniquesRatsEnzyme ActivationEndocrinologymedicine.anatomical_structureLiverSteroid 16-alpha-HydroxylaseHepatocytePhenobarbitalCytochrome P-450 CYP2B1Steroid Hydroxylasesbiology.proteinHepatocytesHydroxytestosteronesAryl Hydrocarbon HydroxylasesExcitatory Amino Acid Antagonistshormones hormone substitutes and hormone antagonistsGlucocorticoidmedicine.drugXenobiotica; the fate of foreign compounds in biological systems
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Yeast Translation Elongation Factor eIF5A Expression Is Regulated by Nutrient Availability through Different Signalling Pathways

2020

Translation elongation factor eIF5A binds to ribosomes to promote peptide bonds between problematic amino acids for the reaction like prolines. eIF5A is highly conserved and essential in eukaryotes, which usually contain two similar but differentially expressed paralogue genes. The human eIF5A-1 isoform is abundant and implicated in some cancer types

MitochondrionBiotecnologialcsh:ChemistryPeptide Initiation FactorsGene Expression Regulation Fungalmitochondrial respirationGene expressionExpressió genèticaHap1Protein Isoformshemelcsh:QH301-705.5SpectroscopyChemistryRNA-Binding ProteinsTranslation (biology)Iron DeficienciesGeneral MedicineTORAerobiosisUp-RegulationComputer Science ApplicationsCell biologySnf1EIF5ASignal TransductionGene isoformSaccharomyces cerevisiae ProteinsIronCitric Acid CycleDown-RegulationSaccharomyces cerevisiaeMechanistic Target of Rapamycin Complex 1Models BiologicalArticleCatalysisInorganic ChemistryeIF5APhysical and Theoretical ChemistryMolecular BiologyTranscription factorGeneLysineOrganic ChemistryNutrientsMetabolismCarbonMetabolic Flux AnalysisGlucoselcsh:Biology (General)lcsh:QD1-999Fermentationgene expressionInternational Journal of Molecular Sciences
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Mediation of Elicitin Activity on Tobacco Is Assumed by Elicitin-Sterol Complexes

2001

Elicitins secreted by phytopathogenic Phytophthora spp. are proteinaceous elicitors of plant defense mechanisms and were demonstrated to load, carry, and transfer sterols between membranes. The link between elicitor and sterol-loading properties was assessed with the use of site-directed mutagenesis of the 47 and 87 cryptogein tyrosine residues, postulated to be involved in sterol binding. Mutated cryptogeins were tested for their ability to load sterols, bind to plasma membrane putative receptors, and trigger biological responses. For each mutated elicitin, the chemical characterization of the corresponding complexes with stigmasterol (1:1 stoichiometry) demonstrated their full functionali…

Models MolecularPhytophthora0106 biological sciencesTime FactorsProtein Conformation[SDV]Life Sciences [q-bio]Receptors Cell SurfaceBiologyModels Biological01 natural sciencesArticleHost-Parasite InteractionsFungal Proteins03 medical and health sciencesTobaccoProtein IsoformsBinding siteReceptorMolecular BiologyComputingMilieux_MISCELLANEOUSCells CulturedPlant DiseasesPlant Proteins030304 developmental biology0303 health sciencesBinding SitesAlgal ProteinsCell MembraneProteinsElicitinCell BiologyHydrogen-Ion ConcentrationLigand (biochemistry)Receptor–ligand kineticsSterolElicitor[SDV] Life Sciences [q-bio]SterolsBiochemistryTyrosineCalciumSterol bindingProtein Binding010606 plant biology & botanyMolecular Biology of the Cell
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Ligand-binding domain determines endoplasmic reticulum exit of AMPA receptors.

2010

AMPA receptors (AMPARs) are tetrameric ion channels that mediate rapid glutamate signaling in neurons and many non-neuronal cell types. Endoplasmic reticulum (ER) quality control mechanisms permit only correctly folded functional receptors to be delivered to the cell surface. We analyzed the biosynthetic maturation and transport of all 12 GluA1–4 subunit splice variants as homomeric receptors and observed robust isoform-dependent differences in ER exit competence and surface expression. In contrast to inefficient ER exit of both GluA3 splice forms and the flop variants of GluA1 and GluA4, prominent plasma membrane expression was observed for the other AMPAR isoforms. Surprisingly, deletion …

Models MolecularProtein ConformationImmunoblottingMolecular Sequence DataAMPA receptorBiologymedicine.disease_causeEndoplasmic ReticulumLigandsBiochemistryCell membrane03 medical and health sciences0302 clinical medicineNeurobiologyProtein targetingChlorocebus aethiopsmedicineHomomericAnimalsHumansProtein IsoformsAmino Acid SequenceReceptors AMPAReceptorMolecular BiologyIon channel030304 developmental biology0303 health sciencesBinding SitesSequence Homology Amino AcidEndoplasmic reticulumCell MembraneCell BiologyCell biologyTransport proteinProtein Structure TertiaryAlternative SplicingProtein SubunitsProtein Transportmedicine.anatomical_structureHEK293 CellsMicroscopy FluorescenceCOS CellsProtein Multimerization030217 neurology & neurosurgeryThe Journal of biological chemistry
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Cockroach allergens Per a 3 are oligomers

2009

Allergens from cockroaches cause major asthma-related health problems worldwide. Among them Per a 3 belongs to the most potent allergens. Although the sequences of some members of the Per a 3-family are known, their biochemical and biophysical properties have not been investigated. Here we present for the first time a thorough structural characterization of these allergens, which have recently been tested to induce an increase of allergy specific indicators in blood of Europeans. We isolated two Per a 3 isoforms, which occur freely dissolved in the hemolymph as hexamers with molecular masses of 465+/-25kDa (P II) and 512+/-25kDa (P I). Their sedimentation coefficients (S(20,W)) were determi…

Models MolecularSequence analysismedicine.medical_treatmentProtein subunitMolecular Sequence DataImmunologySequence alignmentRandom hexamermedicine.disease_causeMass SpectrometryAllergenmedicineAnimalsPeriplanetaProtein IsoformsAmino Acid SequencePeptide sequenceBase SequencebiologyCircular DichroismHemocyaninSequence Analysis DNAAllergensbiology.organism_classificationMicroscopy ElectronMicroscopy FluorescenceBiochemistryImmunologyInsect ProteinsElectrophoresis Polyacrylamide GelAmerican cockroachSequence AlignmentUltracentrifugationDevelopmental BiologyDevelopmental & Comparative Immunology
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The Sequence of a Gastropod Hemocyanin (HtH1 from Haliotis tuberculata)

2000

The eight functional units (FUs), a-h, of the hemocyanin isoform HtH1 from Haliotis tuberculata (Prosobranchia, Archaeogastropoda) have been sequenced via cDNA, which provides the first complete primary structure of a gastropod hemocyanin subunit. With 3404 amino acids (392 kDa) it is the largest polypeptide sequence ever obtained for a respiratory protein. The cDNA comprises 10,758 base pairs and includes the coding regions for a short signal peptide, the eight different functional units, a 3'-untranslated region of 478 base pairs, and a poly(A) tail. The predicted protein contains 13 potential sites for N-linked carbohydrates (one for HtH1-a, none for HtH1-c, and two each for the other si…

Models MolecularSignal peptideDNA ComplementaryProtein subunitmedicine.medical_treatmentMolecular Sequence DataOctopodiformesBiologyBiochemistryEvolution MolecularArchaeogastropodaComplementary DNAmedicineAnimalsProtein IsoformsComputer SimulationAmino Acid SequenceMolecular BiologyPeptide sequencePhylogenyGene LibrarySequence Homology Amino AcidProtein primary structureHemocyaninCell BiologyAnatomybiology.organism_classificationRespiratory proteinBiochemistryMolluscaHemocyaninsProtein BindingJournal of Biological Chemistry
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International Union of Basic and Clinical Pharmacology. XCIV. Adhesion G Protein–Coupled Receptors

2015

The Adhesion family forms a large branch of the pharmacologically important superfamily of G protein-coupled receptors (GPCRs). As Adhesion GPCRs increasingly receive attention from a wide spectrum of biomedical fields, the Adhesion GPCR Consortium, together with the International Union of Basic and Clinical Pharmacology Committee on Receptor Nomenclature and Drug Classification, proposes a unified nomenclature for Adhesion GPCRs. The new names have ADGR as common dominator followed by a letter and a number to denote each subfamily and subtype, respectively. The new names, with old and alternative names within parentheses, are: ADGRA1 (GPR123), ADGRA2 (GPR124), ADGRA3 (GPR125), ADGRB1 (BAI1…

Models MolecularSocieties ScientificSubfamilyComputational biologyBiologyGPR110PharmacologyLigandsGPR113Second Messenger SystemsReceptors G-Protein-CoupledCell MovementTerminology as TopicCell AdhesionCyclic AMPAnimalsHumansProtein IsoformsReceptorNomenclatureG protein-coupled receptorPharmacologyCell MembraneInternational AgenciesAdhesionQPGPR56Pharmacology ClinicalIUPHAR Nomenclature ReportsMolecular MedicineQP517Cell Adhesion MoleculesSignal TransductionPharmacological Reviews
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