Search results for " Fragment."

showing 10 items of 1142 documents

Pharmacological intervention in age-associated brain disorders by Flupirtine: Alzheimer’s and Prion diseases

1998

Alzheimer's disease, a major form of dementia in the elderly has become an increasingly important health problem in developed countries. In vitro studies on primary neurons demonstrate that Flupirtine (Katadolon) at a concentration of 1 microg/ml, significantly reduces the neurotoxic (apoptotic) effect displayed by A beta25-35, a segment of the amyloid beta-protein precursor the etiologic agent of Alzheimer's disease. Flupirtine, which has been in clinical use since 10 years ago, prevents the toxic effect of PrP, the presumed etiologic agent of the Creutzfeldt-Jakob disease as well as the excitatory amino acid glutamate on cortical neurons. Flupirtine displays a bimodal activity. Its strong…

AgingTime FactorsCell SurvivalPrionsMolecular Sequence DataAminopyridinesApoptosisPharmacologyBiologyNeuroprotectionPrion Diseaseschemistry.chemical_compoundGlutamatesAlzheimer DiseasemedicineAnimalsAmino Acid SequenceRats WistarCells CulturedNeuronsAmyloid beta-PeptidesGlutamate receptorNeurotoxicityBiological activityGlutathionemedicine.diseasePeptide FragmentsRatsNeuroprotective Agentsmedicine.anatomical_structureProto-Oncogene Proteins c-bcl-2BiochemistrychemistryCalciumNeuronAlzheimer's diseaseFlupirtineDevelopmental Biologymedicine.drugMechanisms of Ageing and Development
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Cannabinoid receptor 1 deficiency in a mouse model of Alzheimer's disease leads to enhanced cognitive impairment despite of a reduction in amyloid de…

2012

Alzheimer's disease (AD) is characterized by amyloid-beta deposition in amyloid plaques, neurofibrillary tangles, inflammation, neuronal loss, and cognitive deficits. Cannabinoids display neuromodulatory and neuroprotective effects and affect memory acquisition. Here, we studied the impact of cannabinoid receptor type 1 (CB1) deficiency on the development of AD pathology by breeding amyloid precursor protein (APP) Swedish mutant mice (APP23), an AD animal model, with CB1-deficient mice. In addition to the lower body weight of APP23/CB1(-/-) mice, most of these mice died at an age before typical AD-associated changes become apparent. The surviving mice showed a reduced amount of APP and its …

Agingmedicine.medical_specialtyPathologyCannabinoid receptormedicine.medical_treatmentMutantMice TransgenicInflammationDiseaseNeuroprotectionAmyloid beta-Protein PrecursorMiceReceptor Cannabinoid CB1Alzheimer DiseaseCell Line TumorInternal medicinemental disordersmedicineAmyloid precursor proteinAnimalsHumansMaze LearningCognitive impairmentAmyloid beta-Peptidesbiologybusiness.industryGeneral NeuroscienceBody WeightAge FactorsBrainPeptide FragmentsDisease Models AnimalEndocrinologyGene Expression RegulationMutationbiology.proteinlipids (amino acids peptides and proteins)MicrogliaNeurology (clinical)CannabinoidGeriatrics and Gerontologymedicine.symptomCognition DisordersbusinessDevelopmental BiologyNeurobiology of Aging
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Induction of apoptosis in cardiac myocytes by an A3 adenosine receptor agonist.

1998

The effects of the selective adenosine (ADO) A3 receptor agonist IB-MECA (N6-(3-iodobenzyl)adenosine-5'-N-methylcarboxamide) on cultured newborn rat cardiomyocytes were examined in comparison with ADO, the ADO A1 receptor-selective agonist R-PIA (N6-R-phenylisopropyladenosine), or the ADO A3 selective antagonist MRS 1191 (3-ethyl-5-benzyl-2-methyl-6-phenyl-4-phenylethynyl-1, 4-(+/-)-dihydropyridine-3,5 dicarboxylate), using digital image analysis of Feulgen-stained nuclei. At high concentration, IB-MECA (/=10 microM ) and ADO (200 microM) induced apoptosis; however, R-PIA or MRS 1191 did not have any detectable effects on cardiac cells. In addition, DNA breaks in cardiomyocytes undergoing a…

AgonistContraction (grammar)TUNEL assayAdenosinemedicine.drug_classMyocardiumReceptor Adenosine A3ApoptosisHeartCell BiologyDNA FragmentationBiologyAdenosine receptorMolecular biologyAdenosineRatsApoptosismedicinePurinergic P1 Receptor AgonistsMyocyteAnimalsCalciumReceptorCells Culturedmedicine.drugExperimental cell research
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Tachykinin NK(2) receptors facilitate acetylcholine release from guinea-pig isolated trachea.

2000

The release of newly synthesised [3H]acetylcholine was evoked by electrical field stimulation (5 Hz, 600 pulses) of epithelium-deprived guinea-pig trachea strips after sensory neuropeptides depletion with 3 microM capsaicin. The selective tachykinin NK(2) receptor agonist [betaAla(8)]neurokinin A-(4-10) increased in a concentration-dependent manner the electrically-induced release of [3H]acetylcholine. The facilitatory effect was antagonised by the selective non-peptide tachykinin NK(2) receptor antagonist, SR 48968 (apparent pK(B) 8.9). The tachykinin NK(1) and NK(3) receptor agonists substance P methyl ester and senktide (both 10 and 100 nM), respectively, did not affect the evoked releas…

AgonistMalemedicine.medical_specialtymedicine.drug_classNeurokinin AGuinea PigsSubstance PIn Vitro TechniquesCholinechemistry.chemical_compoundPiperidinesInternal medicinemedicineAnimalsReceptorPharmacologyNeuronsReceptors Neurokinin-2Receptor antagonistAcetylcholineElectric StimulationPeptide FragmentsTracheaEndocrinologychemistryCapsaicinBenzamidesNeurokinin ACapsaicinTachykinin receptorAcetylcholinemedicine.drugEuropean journal of pharmacology
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Extracellular Domains of the Bradykinin B2 Receptor Involved in Ligand Binding and Agonist Sensing Defined by Anti-peptide Antibodies

1996

Many of the physiological functions of bradykinin are mediated via the B2 receptor. Little is known about binding sites for bradykinin on the receptor. Therefore, antisera against peptides derived from the putative extracellular domains of the B2 receptor were raised. The antibodies strongly reacted with their corresponding antigens and cross-reacted both with the denatured and the native B2 receptor. Affinity-purified antibodies to the various extracellular domains were used to probe the contact sites between the receptor and its agonist, bradykinin or its antagonist HOE140. Antibodies to extracellular domain 3 (second loop) efficiently interfered, in a concentration-dependent manner, with…

AgonistReceptor Bradykinin B2medicine.drug_classMolecular Sequence DataFluorescent Antibody TechniqueCHO CellsSpodopteraBradykininTransfectionBiochemistryAntibodiesProtein Structure SecondaryCell LineCricetinaeExtracellularmedicineAnimalsHumansAmino Acid SequenceBradykinin receptorBinding siteReceptorMolecular BiologyChemistryReceptors BradykininCell MembraneCell BiologyMolecular biologyPeptide FragmentsRecombinant ProteinsRatsCell biologyModels StructuralEctodomainCompetitive antagonistIntracellularJournal of Biological Chemistry
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Selection and characterization of a novel agonistic human recombinant anti-Trail-R2 minibody with anti-leukemic activity

2009

Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is a promising natural anticancer therapeutic agent because through its “death receptors”, TRAIL-R1 and TRAIL-R2, it induces apoptosis in many transformed tumor cells, but not in the majority of normal cells. Hence, agonistic compounds directed against TRAIL death receptors have the potential of being excellent cancer therapeutic agents, with minimal cytotoxicity in normal tissues. Here, we report the selection and characterization of a new single-chain fragment variable (scFv) to TRAIL-R2 receptor isolated from a human phage-display library, produced as minibody (MB), and characterized for the in vitro anti-leukemic tumoricid…

Agonistmedicine.drug_classTRAIL; TRAIL-R2; minibody; anticancer therapyImmunologylymphoma; therapy; recombinant antibodyTRAILApoptosislymphomaCHO CellsCricetulusPeptide LibraryTRAIL-R2CricetinaeImmunoglobulin FragmentmedicineAnimalsHumansImmunology and Allergyrecombinant antibodyanticancer therapyReceptorCytotoxicityImmunoglobulin FragmentsPharmacologytherapyLeukemiaChemistryAnimalChinese hamster ovary cellAntibody-Dependent Cell CytotoxicityminibodyApoptosiIn vitroRecombinant ProteinsReceptors TNF-Related Apoptosis-Inducing LigandCHO CellCell cultureApoptosisImmunologyCancer researchTumor necrosis factor alphaCricetuluHuman
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Cellular Prion Protein Participates in Amyloid-β Transcytosis across the Blood—Brain Barrier

2012

The blood—brain barrier (BBB) facilitates amyloid-β (Aβ) exchange between the blood and the brain. Here, we found that the cellular prion protein (PrPc), a putative receptor implicated in mediating Aβ neurotoxicity in Alzheimer's disease (AD), participates in Aβ transcytosis across the BBB. Using an in vitro BBB model, [125I]-Aβ1–40 transcytosis was reduced by genetic knockout of PrPc or after addition of a competing PrPc-specific antibody. Furthermore, we provide evidence that PrPc is expressed in endothelial cells and, that monomeric Aβ1–40 binds to PrPc. These observations provide new mechanistic insights into the role of PrPc in AD.

Amyloid βanimal diseasesBiologyBrief CommunicationBlood–brain barrierModels BiologicalMiceAlzheimer Diseasemental disordersmedicineAnimalsPrPC ProteinsPrion proteinReceptorCells CulturedAmyloid beta-PeptidesNeurotoxicitymedicine.diseaseMolecular biologyPeptide FragmentsIn vitronervous system diseasesCell biologymedicine.anatomical_structureNeurologyTranscytosisBlood-Brain BarrierGene Knockdown Techniquesbiology.proteinNeurology (clinical)AntibodyTranscytosisCardiology and Cardiovascular MedicineProtein BindingJournal of Cerebral Blood Flow & Metabolism
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The sea urchin embryo: a model to study Alzheimer's beta amyloid induced toxicity.

2009

Abstract Alzheimer’s disease (AD) is the most common form of dementia. The cause of AD is closely related to the accumulation of amyloid beta peptide in the neuritic plaques. The use of animal model systems represents a good strategy to elucidate the molecular mechanism behind the development of this pathology. Here we use the Paracentrotus lividus embryo to identify molecules and pathways that can be involved in the degenerative process. As a first step, we identified the presence of an antigen related to the human APP, called Pl APP. This antigen, after gastrula stage, is processed producing a polypeptide of about 10 kDa. By immunohistochemistry we localized the Pl APP antigen in some ser…

AmyloidAmyloid betaBiophysicsApoptosisBiochemistryNervous SystemParacentrotus lividusAlzheimer Diseasebiology.animalAnimalsHumansSenile plaquesAntigensMolecular BiologySea urchinCaspaseTUNEL assayAmyloid beta-Peptidesbiologybiology.organism_classificationPeptide FragmentsRecombinant ProteinsCell biologyBiochemistryApoptosisCaspasesModels Animalbiology.proteinParacentrotusParacentrotus lividusAmyloid-betaOligomers Fibrillar aggregatesApoptosisAnimal modelArchives of biochemistry and biophysics
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Structural analysis of copper(I) interaction with amyloid β peptide

2019

Abstract The N-terminal fragment of Aβ (β = beta) peptide is able to bind essential transition metal ions like, copper, zinc and iron. Metal binding usually occurs via the imidazole nitrogens of the three His residues which play a key role in the coordination chemistry. Among all the investigated systems, the interaction between copper and Amyloid β assume a biological relevance because of the interplay between the two copper oxidation states, Cu(II) and Cu(I), and their involvement in redox reactions. Both copper ions share the ability to bind Amyloid β. A huge number of investigations have demonstrated that Cu(II) anchors to the N-terminal amino and His6, His13/14 imidazole groups, while …

AmyloidSilverCoordination spherechemistry.chemical_elementPeptide010402 general chemistrySilver(I)01 natural sciencesBiochemistryRedoxCoordination complexInorganic ChemistryMetalchemistry.chemical_compoundCoordination ComplexesImidazoleHistidineAmino Acid SequenceHistidinechemistry.chemical_classificationAmyloid beta-Peptides010405 organic chemistryChemistryStructureCopperPeptide Fragments0104 chemical sciencesCrystallographyCoordinationvisual_artvisual_art.visual_art_mediumCopper(I)CopperProtein BindingJournal of Inorganic Biochemistry
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I Vaticana fragmenta a due secoli dalla riscoperta

2022

Two centuries have passed since the palimpsest that transmits a Roman legal work known as the Vaticana fragmenta was rediscovered by Angelo Mai in the Vatican Apostolic Library in Rome. This paper reviews the main issues relating to this work and suggests some reasons why a new edition of the text is desirable. 1820 hat Angelo Mai in der Vatikanischen Apostolischen Bibliothek in Rom ein Palimpsest wiederentdeckt, welches ein römisches Rechtswerk – die so genannte Vaticana Fragmenta – überliefert. 200 Jahre sind seitdem genau vergangen. Dieser Beitrag gibt einen Überblick über die wichtigsten Aspekte dieses Werks und zeigt Gründe auf, warum eine neue Ausgabe dieses Textes wünschenswert ist.

Angelo MaiVaticana fragmentaSettore IUS/18 - Diritto Romano E Diritti Dell'Antichita'Vat. Lat. 5766Palimpsestforschung.
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