Search results for "ALPHA"

showing 10 items of 3228 documents

Cold Atmospheric Plasma Promotes Regeneration-Associated Cell Functions of Murine Cementoblasts In Vitro

2021

The aim of the study was to examine the efficacy of cold atmospheric plasma (CAP) on the mineralization and cell proliferation of murine dental cementoblasts. Cells were treated with CAP and enamel matrix derivates (EMD). Gene expression of alkaline phosphatase (ALP), bone gamma-carboxyglutamate protein (BGLAP), periostin (POSTN), osteopontin (OPN), osterix (OSX), collagen type I alpha 1 chain (COL1A1), dentin matrix acidic phosphoprotein (DMP)1, RUNX family transcription factor (RUNX)2, and marker of proliferation Ki-67 (KI67) was quantified by real-time PCR. Protein expression was analyzed by immunocytochemistry and ELISA. ALP activity was determined by ALP assay. Von Kossa and alizarin r…

0301 basic medicinePlasma GasesGene Expressioncold atmospheric plasmaMice0302 clinical medicineCell MovementmineralizationOsteopontinBiology (General)CementogenesisSpectroscopyDental CementumbiologyChemistryCell DifferentiationGeneral Medicinetraumatic dental injuriesdental hard tissue regeneration therapyComputer Science ApplicationsChemistryAlkaline phosphatasecementoblastsemdogainQH301-705.5Cell SurvivalproliferationCementoblastOsteocalcinPeriostinArticleCatalysisCell LineInorganic Chemistry03 medical and health sciencesCalcification Physiologicstomatognathic systemAnimalsViability assayPhysical and Theoretical ChemistryQD1-999Molecular BiologyCell ProliferationCell growthOrganic Chemistry030206 dentistryMolecular biologyDMP1Collagen type I alpha 1030104 developmental biologyGene Expression Regulationbiology.proteinOsteopontinTranscriptomeInternational Journal of Molecular Sciences
researchProduct

Mutations in the GLA Gene and LysoGb3: Is It Really Anderson-Fabry Disease?

2018

Anderson-Fabry disease (FD) is a rare, progressive, multisystem storage disorder caused by the partial or total deficit of the lysosomal enzyme &alpha

0301 basic medicineProbandMaleDiseasemedicine.disease_causeSphingolipidCatalysilcsh:Chemistry0302 clinical medicineGla geneFabry disease; GLA gene; LysoGb3MedicineChildlcsh:QH301-705.5Spectroscopychemistry.chemical_classificationGeneticsAlleleAged 80 and overMutationComputer Science Applications1707 Computer Vision and Pattern RecognitionGeneral MedicineMiddle AgedPhenotype3. Good healthComputer Science ApplicationsPhenotypeChild PreschoolFemaleHumanAdultAdolescentGenotypeGlycolipidCatalysisArticleInorganic Chemistry03 medical and health sciencesYoung Adultotorhinolaryngologic diseasesHumansPhysical and Theoretical ChemistryMolecular BiologyGeneGLA geneAllelesAgedFabry diseaseSphingolipidsbusiness.industryOrganic ChemistryInfant NewbornLysoGb3InfantBiomarkerFabry disease; gla gene; lysogb3; adolescent; adult; aged; aged 80 and over; alleles; amino acid substitution; biomarkers; child; child preschool; fabry disease; female; genotype; glycolipids; humans; infant; infant newborn; male; middle aged; phenotype; sphingolipids; young adult; alpha-galactosidase; mutationmedicine.diseaseFabry disease030104 developmental biologyEnzymechemistrylcsh:Biology (General)lcsh:QD1-999Amino Acid Substitutionalpha-GalactosidaseMutationGlycolipidsbusiness030217 neurology & neurosurgeryBiomarkersInternational Journal of Molecular Sciences
researchProduct

Peroxisome proliferator-activated receptor-γ coactivator-1α mediates neuroprotection against excitotoxic brain injury in transgenic mice: role of mit…

2016

Peroxisome proliferator-activated receptor gamma coactivator-1α (PGC-1α) is a transcriptional coactivator involved in the regulation of mitochondrial biogenesis and cell defense. The functions of PGC-1α in physiology of brain mitochondria are, however, not fully understood. To address this we have studied wild-type and transgenic mice with a two-fold overexpression of PGC-1α in brain neurons. Data showed that the relative number and basal respiration of brain mitochondria were increased in PGC-1α transgenic mice compared with wild-type mitochondria. These changes occurred concomitantly with altered levels of proteins involved in oxidative phosphorylation (OXPHOS) as studied by proteomi…

0301 basic medicineProgrammed cell deathKainic acidTransgenebcl-X ProteinPeroxisome proliferator-activated receptorBiologyInhibitor of apoptosisSettore BIO/09 - FisiologiaNeuroprotectionOxidative PhosphorylationInhibitor of Apoptosis ProteinsMice03 medical and health scienceschemistry.chemical_compoundXIAP0302 clinical medicineBrain InjurieInhibitor of Apoptosis ProteinAnimalsCA1 Region HippocampalCells CulturedNeuronschemistry.chemical_classificationNeuroscience (all)Kainic AcidCell DeathAnimalNeuron survivalGeneral NeuroscienceProteomicXIAP; Kainic acid; Mitochondria; Neuron survival; PGC-1α; Proteomics; Animals; Brain Injuries; CA1 Region Hippocampal; Cell Death; Cells Cultured; Inhibitor of Apoptosis Proteins; Kainic Acid; Mice; Mitochondria; Neurons; Oxidative Phosphorylation; Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha; Proto-Oncogene Proteins c-bcl-2; bcl-X Protein; Neuroscience (all)NeuronPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaMitochondriaCell biologyXIAP030104 developmental biologyProto-Oncogene Proteins c-bcl-2chemistryMitochondrial biogenesisBrain InjuriesImmunologyPGC-1α030217 neurology & neurosurgeryEuropean Journal of Neuroscience
researchProduct

Mammalian plasma fetuin-B is a selective inhibitor of ovastacin and meprin metalloproteinases

2019

AbstractVertebrate fetuins are multi-domain plasma-proteins of the cystatin-superfamily. Human fetuin-A is also known as AHSG, α2-Heremans-Schmid-glycoprotein. Gene-knockout in mice identified fetuin-A as essential for calcified-matrix-metabolism and bone-mineralization. Fetuin-B deficient mice, on the other hand, are female infertile due to zona pellucida ‘hardening’ caused by the metalloproteinase ovastacin in unfertilized oocytes. In wildtype mice fetuin-B inhibits the activity of ovastacin thus maintaining oocytes fertilizable. Here we asked, if fetuins affect further proteases as might be expected from their evolutionary relation to single-domain-cystatins, known as proteinase-inhibito…

0301 basic medicineProteasesGlycosylationalpha-2-HS-Glycoproteinmedicine.medical_treatmentProteolysislcsh:MedicineAstacoideaMatrix metalloproteinaseArticle03 medical and health sciencesMicePlasma0302 clinical medicinemedicineAnimalsHumansFibrinolysinZona pellucidalcsh:ScienceMammalsMetalloproteinaseMultidisciplinaryProteasemedicine.diagnostic_testChemistrylcsh:RWild typeMetalloendopeptidasesFetuinFetuin-BRecombinant ProteinsCell biology030104 developmental biologymedicine.anatomical_structureMatrix Metalloproteinase 9FertilizationProteolysisMetalloproteasesCattlelcsh:Q030217 neurology & neurosurgery
researchProduct

Insights into the Structure of the Vip3Aa Insecticidal Protein by Protease Digestion Analysis

2017

Vip3 proteins are secretable proteins from Bacillus thuringiensis whose mode of action is still poorly understood. In this study, the activation process for Vip3 proteins was closely examined in order to better understand the Vip3Aa protein stability and to shed light on its structure. The Vip3Aa protoxin (of 89 kDa) was treated with trypsin at concentrations from 1:100 to 120:100 (trypsin:Vip3A, w:w). If the action of trypsin was not properly neutralized, the results of SDS-PAGE analysis (as well as those with Agrotis ipsilon midgut juice) equivocally indicated that the protoxin could be completely processed. However, when the proteolytic reaction was efficiently stopped, it was revealed t…

0301 basic medicineProteasesHealth Toxicology and MutagenesisSize-exclusion chromatographyBeta sheetBacillus thuringiensislcsh:MedicineBiologyToxicologyCleavage (embryo)ArticleProtein Structure Secondary03 medical and health sciencestrypsin inhibitorsBacterial ProteinsSDS-PAGE artefactprotease stabilitymedicinebacterial secreted proteinsAnimalsTrypsinMode of actionProtein secondary structureVip proteinsIntestinal Secretionslcsh:Rtoxin activationVip proteins; bacterial secreted proteins; toxin activation; proteolytic activation; trypsin inhibitors; <i>Bacillus thuringiensis</i>; SDS-PAGE artefact; protease stabilityTrypsinMolecular biologyLepidoptera030104 developmental biologyBiochemistryproteolytic activationLarvaProteolysisPeptidesAlpha helixmedicine.drugToxins
researchProduct

Discovery and validation of 2-styryl substituted benzoxazin-4-ones as a novel scaffold for rhomboid protease inhibitors

2017

Abstract Rhomboids are intramembrane serine proteases with diverse physiological functions in organisms ranging from archaea to humans. Crystal structure analysis has provided a detailed understanding of the catalytic mechanism, and rhomboids have been implicated in various disease contexts. Unfortunately, the design of specific rhomboid inhibitors has lagged behind, and previously described small molecule inhibitors displayed insufficient potency and/or selectivity. Using a computer-aided approach, we focused on the discovery of novel scaffolds with reduced liabilities and the possibility for broad structural variations. Docking studies with the E. coli rhomboid GlpG indicated that 2-styry…

0301 basic medicineProteasesSerine Proteinase InhibitorsStereochemistrymedicine.medical_treatmentClinical BiochemistryPharmaceutical ScienceBiochemistryStyrenesSerine03 medical and health sciencesCatalytic DomainEndopeptidasesDrug DiscoveryEscherichia coliSerinemedicineAnimalsChymotrypsinDrosophila ProteinsHumansMolecular BiologyEnzyme AssaysSerine proteaseProtease030102 biochemistry & molecular biologybiologyBenzoxazinonesChemistryEscherichia coli ProteinsRhomboid proteaseRhomboidOrganic ChemistryMembrane ProteinsTransforming Growth Factor alphaBenzoxazinesDNA-Binding ProteinsMolecular Docking Simulation030104 developmental biologyDocking (molecular)Mutationbiology.proteinMolecular MedicineCattleDrosophilaBioorganic &amp; Medicinal Chemistry Letters
researchProduct

Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions.

2016

Lunasin is a 43 amino acid peptide with anti-cancer, antioxidant, anti-inflammatory and cholesterol-lowering properties. Although the mechanism of action of lunasin has been characterized to some extent, its exact three-dimensional structure as well as the function of the N-terminal sequence remains unknown. We established a novel method for the production of recombinant lunasin that allows efficient isotope labeling for NMR studies. Initial studies showed that lunasin can exist in a reduced or oxidized state with an intramolecular disulfide bond depending on solution conditions. The structure of both forms of the peptide at pH 3.5 and 6.5 was characterized by CD spectroscopy and multidimen…

0301 basic medicineProtein Conformation alpha-HelicalCircular dichroismPhysiologyBeta sheetPeptideIntrinsically disordered proteinsBiochemistryLunasinAntioxidantsHistones03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineEndocrinologyNeoplasmsAnticarcinogenic AgentsHumansAmino Acid SequenceDisulfidesProtein secondary structureNuclear Magnetic Resonance BiomolecularPlant Proteinschemistry.chemical_classificationChemistryAcetylationNuclear magnetic resonance spectroscopyIntrinsically Disordered Proteins030104 developmental biologyBiochemistry030220 oncology & carcinogenesisBiophysicsSoybean ProteinsPeptidesOxidation-ReductionFunction (biology)Peptides
researchProduct

In vivo selection of heterotypically interacting transmembrane helices: Complementary helix surfaces, rather than conserved interaction motifs, drive…

2017

Single pass transmembrane proteins make up almost half of the whole transmembrane proteome. Contacts between such bitopic transmembrane proteins are common, and oligomerization of their single transmembrane helix is involved in triggering and regulation of signal transduction across cell membranes. In several recent analyses the distribution of amino acids at helix-helix contact sides has been analyzed, and e.g. a preference of amino acids with small side chains has been identified. Here we select amino acids, amino acid pairings and amino acid motifs, which mediate strong interactions of single-span transmembrane α-helices. Our analysis illustrates an architecture of TM helix dimers that i…

0301 basic medicineProtein Conformation alpha-HelicalDimerAmino Acid MotifsBiophysicsBiologyBiochemistryBordetella pertussisProtein Structure Secondary03 medical and health scienceschemistry.chemical_compoundAmino Acid SequenceAmino Acidschemistry.chemical_classificationCell MembraneMembrane ProteinsCell BiologyTransmembrane proteinAmino acidCrystallographyTransmembrane domain030104 developmental biologyMembrane proteinchemistryProteomeHelixBiophysicsProtein foldingDimerizationBiochimica et biophysica acta. Biomembranes
researchProduct

Phosphorylation of meprin β controls its cell surface abundance and subsequently diminishes ectodomain shedding

2021

Meprin β is a zinc-dependent metalloprotease exhibiting a unique cleavage specificity with strong preference for acidic amino acids at the cleavage site. Proteomic studies revealed a diverse substrate pool of meprin β including the interleukin-6 receptor (IL-6R) and the amyloid precursor protein (APP). Dysregulation of meprin β is often associated with pathological conditions such as chronic inflammation, fibrosis, or Alzheimer's disease (AD). The extracellular regulation of meprin β including interactors, sheddases, and activators has been intensively investigated while intracellular regulation has been barely addressed in the literature. This study aimed to analyze C-terminal phosphorylat…

0301 basic medicineProtein Kinase C-alphaImmunoprecipitationmedia_common.quotation_subjectBiochemistry03 medical and health sciences0302 clinical medicineProtein Kinase C betaTumor Cells CulturedGeneticsAmyloid precursor proteinHumansPhosphorylationInternalizationMolecular BiologyProtein kinase Cmedia_commonbiologyChemistryCell MembraneMetalloendopeptidasesSheddaseCell biology030104 developmental biologyGene Expression RegulationEctodomainColonic NeoplasmsProteolysisbiology.proteinPhosphorylationExtracellular Space030217 neurology & neurosurgeryIntracellularBiotechnologyThe FASEB Journal
researchProduct

Human R1441C LRRK2 regulates the synaptic vesicle proteome and phosphoproteome in a Drosophila model of Parkinson's disease

2016

International audience; Mutations in leucine-rich repeat kinase 2 (LRRK2) cause late-onset, autosomal dominant familial Parkinsons disease (PD) and variation at the LRRK2 locus contributes to the risk for idiopathic PD. LRRK2 can function as a protein kinase and mutations lead to increased kinase activity. To elucidate the pathophysiological mechanism of the R1441C mutation in the GTPase domain of LRRK2, we expressed human wild-type or R1441C LRRK2 in dopaminergic neurons of Drosophila and observe reduced locomotor activity, impaired survival and an age-dependent degeneration of dopaminergic neurons thereby creating a new PD-like model. To explore the function of LRRK2 variants in vivo, we …

0301 basic medicineProteomerab3 GTP-Binding Proteinsalpha-synucleindomainSyntaxin 1Interactomedopaminergic-neuronsAnimals Genetically Modifiedchemistry.chemical_compound0302 clinical medicinemicrotubule stabilityDrosophila ProteinsProtein Interaction MapsGenetics (clinical)LRRK2 GeneKinasephosphorylationBrainParkinson DiseaseArticlesGeneral Medicineautosomal-dominant parkinsonismLRRK2Drosophila melanogasterSynaptotagmin IProteomePhosphorylationSynaptic VesiclesNerve Tissue ProteinsBiologyLeucine-Rich Repeat Serine-Threonine Protein Kinase-203 medical and health sciencesGeneticsAnimalsHumansKinase activitygeneMolecular BiologyAlpha-synucleingtp-bindingDopaminergic Neuronsrepeat kinase 2Molecular biologyPhosphoric Monoester Hydrolasesnervous system diseasesDisease Models Animal030104 developmental biologyGene Expression Regulationchemistrymutation030217 neurology & neurosurgery[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
researchProduct