Search results for "alpha-Crystallins"

showing 4 items of 4 documents

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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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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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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