Search results for "alpha-crystallin"

showing 10 items of 13 documents

αB-crystallin response to a pro-oxidant non-cytotoxic environment in murine cardiac cells: An "in vitro" and "in vivo" study.

2020

The αB-crystallin (HSPB5) protein is modulated in response to a wide variety of stressors generated by multiple physio-pathological conditions, sustained by reactive oxygen species (ROS) production. In cardiac muscle tissue, this protein regulates various cellular processes, such as protein degradation, apoptosis and the stabilization of cytoskeletal elements. In this work, we studied the role of HSPB5 expression, activation and localization in HL-1 murine cardiomyocytes exposed to pro-oxidant and non-cytotoxic H2O2 concentration, as well as in cardiac tissue isolated from mice following an acute, non-damaging endurance exercise. Our results demonstrated that HSPB5 is the most abundant HSP …

0301 basic medicineOxidative eustressOxidative phosphorylationProtein degradationBiochemistry03 medical and health sciencesMice0302 clinical medicineIn vivoPhysiology (medical)medicineAnimalsCardiac musclePhosphorylationchemistry.chemical_classificationReactive oxygen speciesHSPB5ChemistryCardiac musclealpha-Crystallin B ChainHydrogen PeroxidePro-oxidantEndurance exerciseHSPA1ACell biology030104 developmental biologymedicine.anatomical_structureProteolysisCardiac muscle tissueReactive Oxygen SpeciesOxidation-Reduction030217 neurology & neurosurgeryFree radical biologymedicine
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The Small Heat Shock Protein α-Crystallin B Shows Neuroprotective Properties in a Glaucoma Animal Model

2017

Glaucoma is a neurodegenerative disease that leads to irreversible retinal ganglion cell (RGC) loss and is one of the main causes of blindness worldwide. The pathogenesis of glaucoma remains unclear, and novel approaches for neuroprotective treatments are urgently needed. Previous studies have revealed significant down-regulation of α-crystallin B as an initial reaction to elevated intraocular pressure (IOP), followed by a clear but delayed up-regulation, suggesting that this small heat-shock protein plays a pathophysiological role in the disease. This study analyzed the neuroprotective effect of α-crystallin B in an experimental animal model of glaucoma. Significant IOP elevation induced b…

0301 basic medicineProteomicsRetinal Ganglion Cellsgenetic structuresNerve fiber layerGlaucomaCell CountMass Spectrometrylcsh:ChemistryPathogenesischemistry.chemical_compound0302 clinical medicineexperimental glaucoma; α-crystallin B; neuroprotection; proteomicsProtein Interaction Mapslcsh:QH301-705.5Spectroscopyα-crystallin BGeneral MedicineComputer Science ApplicationsUp-Regulationmedicine.anatomical_structureNeuroprotective AgentsRetinal ganglion cellneuroprotectionRetinal Neuronsmedicine.medical_specialtyDown-RegulationBiologyNeuroprotectionCatalysisArticleInorganic Chemistry03 medical and health sciencesCrystallinOphthalmologyHeat shock proteinmedicineElectroretinographyAnimalsPhysical and Theoretical ChemistryMolecular BiologyIntraocular Pressureexperimental glaucomaOrganic Chemistryalpha-Crystallin B ChainRetinalGlaucomamedicine.diseaseeye diseasesDisease Models Animal030104 developmental biologylcsh:Biology (General)lcsh:QD1-999chemistry030221 ophthalmology & optometrysense organsInternational Journal of Molecular Sciences; Volume 18; Issue 11; Pages: 2418
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Trehalose effects on α-crystallin aggregates

2007

alpha-Crystallin in its native state is a large, heterogeneous, low-molecular weight (LMW) aggregate that under certain conditions may progressively became part of insoluble high-molecular weight (HMW) systems. These systems are supposed to play a relevant role in eye lens opacification and vision impairment. In this paper, we report the effects of trehalose on alpha-crystallin aggregates. The role of trehalose in alpha-crystallin stress tolerance, chaperone activity and thermal stability is studied. The results show that trehalose stabilizes the alpha-crystallin native structure, inhibits alpha-crystallin aggregation, and disaggregates preformed LMW systems not affecting its chaperone acti…

BiophysicsMicroscopy Atomic ForceBiochemistrythermal stabilitychemistry.chemical_compoundCrystallinNative stateThermal stabilityBenzothiazolesalpha-Crystallinsalpha-crystallinChaperone activityProtein Structure QuaternaryEye lensMolecular BiologyNative structureCircular DichroismTrehalosefood and beveragesCell BiologyTrehaloseeye diseaseschaperone activityThiazolesSpectrometry FluorescencechemistryBiochemistryaggregatesα-Crystallin Trehalose Aggregates Chaperone activity Thermal stabilitysense organsBiochemical and Biophysical Research Communications
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Protective Effects of L- and D-Carnosine on R-Crystallin Amyloid Fibril Formation: Implications for Cataract Disease

2009

Mildly denaturing conditions induce bovine ?-crystallin, the major structural lens protein, to self-assemble into fibrillar structures in vitro. The natural dipeptide L-carnosine has been shown to have potential protective and therapeutic significance in many diseases. Carnosine derivatives have been proposed as potent agents for ophthalmic therapies of senile cataracts and diabetic ocular complications. Here we report the inhibitory effect induced by the peptide (L- and D-enantiomeric form) on ?-crystallin fibrillation and the almost complete restoration of the chaperone activity lost after denaturant and/or heat stress. Scanning force microscopy (SFM), thioflavin T, and a turbidimetry ass…

CrystallinCircular dichroismAmyloidCarnosinePeptideMicroscopy Atomic ForceBiochemistryCataractLens proteinRats Sprague-Dawleychemistry.chemical_compoundOrgan Culture TechniquesCrystallinChaperone activityAnimalsalpha-CrystallinsSFM Scanning Force Microscopychemistry.chemical_classificationDipeptideCD Circular DichroismThT Thioflavin TCalorimetry Differential ScanningDSC Differential Scanning CalorimetryCircular DichroismCarnosineStereoisomerismIn vitroeye diseasesRatsSpectrometry FluorescencechemistryBiochemistryHEPES 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acidThioflavinCattleFemaleSpectrophotometry Ultravioletsense organsAmyloid fibrilMolecular Chaperones
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Intermediate Filament Diseases: Desminopathy

2008

Desminopathy is one of the most common intermediate filament human disorders associated with mutations in closely interacting proteins, desmin and alphaB-crystallin. The inheritance pattern in familial desminopathy is characterized as autosomal dominant or autosomal recessive, but many cases have no family history. At least some and likely most sporadic desminopathy cases are associated with de novo DES mutations. The age of disease onset and rate of progression may vary depending on the type of inheritance and location of the causative mutation. Typically, the illness presents with lower and later upper limb muscle weakness slowly spreading to involve truncal, neck-flexor, facial and bulba…

GeneticsPathologymedicine.medical_specialtyPoint mutationMutantCardiomyopathyIntermediate Filamentsalpha-Crystallin B ChainGene mutationBiologymedicine.diseaseSudden deathPolymorphism Single NucleotideArticleUpper limb muscle weaknessDesminMuscular DiseasesmedicineDisease ProgressionAnimalsHumansDesminIntermediate filament
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Characterization of small HSPs from Anemonia viridis reveals insights into molecular evolution of alpha crystallin genes among cnidarians.

2014

Gene family encoding small Heat-Shock Proteins (sHSPs containing α-crystallin domain) are found both in prokaryotic and eukaryotic organisms; however, there is limited knowledge of their evolution. In this study, two small HSP genes termed AvHSP28.6 and AvHSP27, both organized in one intron and two exons, were characterised in the Mediterranean snakelocks anemone Anemonia viridis. The release of the genome sequence of Hydra magnipapillata and Nematostella vectensis enabled a comprehensive study of the molecular evolution of α-crystallin gene family among cnidarians. Most of the H. magnipapillata sHSP genes share the same gene organization described for AvHSP28.6 and AvHSP27, differing from …

LipopolysaccharidesMarine and Aquatic SciencesGene ExpressionCnidarianSea anemoneGenomeAnemoniaGene duplicationProtein Isoformsalpha-CrystallinsPhylogenyGenomic organizationGeneticsMultidisciplinarybiologyReverse Transcriptase Polymerase Chain ReactionQTemperatureRMedicineAnemonia viridiSmall HSP; Anemonia viridis; Cnidarians; molecular evolutionResearch ArticleScienceMolecular Sequence DataMarine BiologySmall HSPEvolution MolecularCnidariaSpecies SpecificityMolecular evolutionMetals HeavySequence Homology Nucleic AcidAnimalsGene familyAmino Acid SequenceMolecular BiologyGeneEvolutionary BiologyBase SequenceSequence Homology Amino Acidmolecular evolutionGene Expression ProfilingEcology and Environmental SciencesBiology and Life SciencesAquatic EnvironmentsCell Biologybiology.organism_classificationHeat-Shock Proteins SmallSea AnemonesEarth SciencesPLoS ONE
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The early response of αB-crystallin to a single bout of aerobic exercise in mouse skeletal muscles depends upon fiber oxidative features

2019

Besides its substantial role in eye lens, αB-crystallin (HSPB5) retains fundamental function in striated muscle during physiological or pathological modifications. In this study, we aimed to analyse the cellular and molecular factors driving the functional response of HSPB5 protein in different muscles from mice subjected to an acute bout of non-damaging endurance exercise or in C2C12 myocytes upon exposure to pro-oxidant environment, chosen as “in vivo” and “in vitro” models of a physiological stressing conditions, respectively.To this end, red (GR) and white gastrocnemius (GW), as sources of slow-oxidative and fast-glycolytic/oxidative fibers, as well as the soleus (SOL), mainly composed …

Male0301 basic medicineMuscle Fibers SkeletalClinical BiochemistrySkeletal muscleFluorescent Antibody TechniqueOxidative phosphorylationFilaminBiochemistryMice03 medical and health sciences0302 clinical medicineSettore BIO/10 - BiochimicaPhysical Conditioning AnimalmedicineAnimalsMyocytePhosphorylationlcsh:QH301-705.5Actinlcsh:R5-920Settore BIO/16 - Anatomia UmanaMyogenesisChemistryOrganic ChemistryαB-crystallin phosphorylationalpha-Crystallin B ChainSkeletal muscleImmunohistochemistryEndurance exerciseCell biologyOxidative Stress030104 developmental biologymedicine.anatomical_structurelcsh:Biology (General)Oxidative streDesminMyofibrillcsh:Medicine (General)Oxidation-ReductionBiomarkers030217 neurology & neurosurgeryResearch PaperSignal TransductionRedox Biology
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Prevention of the post-chemotherapy relapse of tuberculous infection by combined immunotherapy

2008

Summary We report that a recently developed combined immunotherapy (CIT) has the capacity to prevent a spontaneous relapse of replicating Mycobacterium tuberculosis bacilli in the lungs of BALB/c, C57Bl/6 or C3H/HeJ strains of mice, following 4 weeks of non-sterilising treatment with isoniazid and rifampicin. The CIT regimen, represented by recombinant IFNγ, anti-α crystalline monoclonal IgA antibody and IL-4 neutralizing polyclonal antibody, reduced the 8-week relapse of viable bacterial counts in the lungs most significantly, when CIT was inoculated during the 5th week post infection, i.e. during the 3rd week of chemotherapy. Although CIT enhanced lung granuloma area, nitric oxide, cytoki…

MaleMicrobiology (medical)TuberculosisTuberculosiAntibodiemedicine.medical_treatmentImmunologyAntitubercular AgentsColony Count MicrobialMicrobiologyAntibodiesMycobacterium tuberculosisInterferon-gammaMiceAdjuvants ImmunologicRecurrencemedicineAnimalsalpha-CrystallinsRelapseTuberculosis PulmonaryCytokineMice Inbred BALB CMice Inbred C3HChemotherapyLungbiologybusiness.industryTuberculosis; Cytokines; Antibodies; Immunotherapy; RelapseIsoniazidMycobacterium tuberculosisImmunotherapybiology.organism_classificationmedicine.diseaseCombined Modality TherapyRecombinant ProteinsImmunoglobulin AMice Inbred C57BLRegimenInfectious Diseasesmedicine.anatomical_structureModels AnimalImmunologyInterleukin-4ImmunotherapybusinessRifampicinmedicine.drugTuberculosis
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Proteome analysis of myocardial tissue following ischemia and reperfusion--effects of complement inhibition.

2006

Myocardial ischemia-reperfusion injury can be related to complement activation with generation of chemotactic mediators, release of cytokines, leukocyte accumulation, and subsequent severe tissue injury. In this regard, activation of transcription factors (i.e., NFkappaB) and de novo protein synthesis or inflammatory protein degradation seems to play an important role. In the present study, we analyzed the cardiac protein expression following myocardial ischemia (60 min) and reperfusion (180 min) in a rabbit model utilizing two-dimensional electrophoresis and nanoHPLC/ESI-MS/MS for biochemical protein identification. To achieve cardioprotective effects, we used a novel highly selective smal…

MaleProteomeG proteinNeutrophilsMolecular Sequence DataBiophysicsIschemiaMyocardial IschemiaMyocardial Reperfusion InjuryProtein degradationComplement C1 Inactivator ProteinsBiochemistryAnalytical ChemistrySuperoxide dismutaseClassical complement pathwayElectrocardiographyNecrosismedicineProtein biosynthesisAnimalsAmino Acid SequenceMolecular BiologyCreatine KinasebiologySuperoxide DismutaseMyocardiumalpha-Crystallin B ChainComplement System Proteinsmedicine.diseaseMolecular biologyComplement systembiology.proteinCreatine kinaseRabbitsMicrotubule-Associated ProteinsBiomarkersBiochimica et biophysica acta
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Two‐dimensional analysis of myocardial protein expression following myocardial ischemia and reperfusion in rabbits

2002

Myocardial ischemia and reperfusion injury (MI/R) can be related to leukocyte activation with subsequent release of cytokines and oxygen derived free radicals. Activation of the complement system has been implicated in the pathogenesis of myocardial ischemia and reperfusion injury. Inflammatory injury will subsequently result in cellular activation and protein synthesis. In the present study we analyzed the myocardial protein expression and its pattern following myocardial ischemia and reperfusion, with and without complement inhibition with the synthetic serine protease inhibitor Futhan/nafamstat mesilate (FUT-175) known to inhibit classical and alternative complement pathway in a rabbit m…

MaleSerine Proteinase InhibitorsNecrosisProteomeNeutrophilsMyocardial IschemiaIschemiaMyocardial Reperfusion InjuryPharmacologyGuanidinesBiochemistrySuperoxide dismutaseNecrosisRandom AllocationComplement inhibitormedicineAnimalsElectrophoresis Gel Two-DimensionalCreatine KinaseMolecular BiologybiologySuperoxide DismutaseChemistryGene Expression ProfilingMyocardiumHemodynamicsProteinsalpha-Crystallin B Chainmedicine.diseaseBenzamidinesComplement systemBiochemistrybiology.proteinAlternative complement pathwayCreatine kinaseRabbitsmedicine.symptomReperfusion injuryPROTEOMICS
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