Search results for "Precursor"

showing 10 items of 490 documents

Shedding of the amyloid precursor protein-like protein APLP2 by disintegrin-metalloproteinases

2005

Cleavage of the amyloid precursor protein (APP) within the amyloid-beta (Aβ) sequence by the α-secretase prevents the formation of toxic Aβ peptides. It has been shown that the disintegrin-metalloproteinases ADAM10 and TACE (ADAM17) act as α-secretases and stimulate the generation of a soluble neuroprotective fragment of APP, APPsα. Here we demonstrate that the related APP-like protein 2 (APLP2), which has been shown to be essential for development and survival of mice, is also a substrate for both proteinases. Overexpression of either ADAM10 or TACE in HEK293 cells increased the release of neurotrophic soluble APLP2 severalfold. The strongest inhibition of APLP2 shedding in neuroblastoma c…

ADAM10HEK 293 cellsRetinoic acidP3 peptideCell BiologyBiologyBiochemistryMolecular biologychemistry.chemical_compoundchemistryDownregulation and upregulationbiology.proteinAmyloid precursor proteinMolecular BiologyAPLP2Amyloid precursor protein secretaseFEBS Journal
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Constitutive and regulated α-secretase cleavage of Alzheimer’s amyloid precursor protein by a disintegrin metalloprotease

1999

Amyloid β peptide (Aβ), the principal proteinaceous component of amyloid plaques in brains of Alzheimer’s disease patients, is derived by proteolytic cleavage of the amyloid precursor protein (APP). Proteolytic cleavage of APP by a putative α-secretase within the Aβ sequence precludes the formation of the amyloidogenic peptides and leads to the release of soluble APPsα into the medium. By overexpression ofa disintegrinandmetalloprotease (ADAM), classified as ADAM 10, in HEK 293 cells, basal and protein kinase C-stimulated α-secretase activity was increased severalfold. The proteolytically activated form of ADAM 10 was localized by cell surface biotinylation in the plasma membrane, but the m…

ADAM10Molecular Sequence DataBiologyKidneyTransfectionCell LineSubstrate SpecificityADAM10 ProteinAmyloid beta-Protein PrecursorEndopeptidasesAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansPoint MutationADAM17 ProteinAmino Acid SequenceCloning MolecularProtein kinase AProtein Kinase CSecretory pathwayBinding SitesMultidisciplinaryHEK 293 cellsP3 peptideMembrane ProteinsMetalloendopeptidasesBiological SciencesPeptide FragmentsRecombinant Proteinscarbohydrates (lipids)ADAM ProteinsKineticsZincAlpha secretaseBiochemistryMutagenesis Site-Directedbiology.proteinCattleAmyloid Precursor Protein SecretasesProceedings of the National Academy of Sciences
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Effect of a dominant-negative form of ADAM10 in a mouse model of Alzheimer's disease.

2009

The alpha-secretase cleaves in the non-amyloidogenic pathway the amyloid-beta protein precursor (AbetaPP) within the region of the amyloid-beta peptides to prevent their formation and aggregation in the brain. Members of the ADAM family (a disintegrin and metalloprotease) are the main candidates for physiologically relevant alpha-secretases. We recently demonstrated that overexpression of ADAM10 in mice transgenic for human AbetaPP (ADAM10 x APP[V717I]) alleviated functional deficits related to Alzheimer's disease. To further demonstrate that this is due to the specific activity of alpha-secretase, we characterized mice overexpressing an inactive form of ADAM10 (ADAM10[E384A]; ADAM10-dn). T…

ADAM10Morris water navigation taskGlutamic AcidStimulationMice TransgenicADAM10 ProteinAmyloid beta-Protein PrecursorMiceIn vivoAlzheimer DiseaseDisintegrinReaction TimeAnimalsHumansIsoleucineProtein precursorMaze LearningSwimmingMetalloproteinaseAlaninebiologyBehavior AnimalChemistryGeneral NeuroscienceAge FactorsMembrane ProteinsValineGeneral MedicineCell biologyMice Inbred C57BLPsychiatry and Mental healthClinical PsychologyADAM ProteinsDisease Models Animalbiology.proteinSpecific activityGeriatrics and GerontologyAmyloid Precursor Protein SecretasesJournal of Alzheimer's disease : JAD
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Down-regulation of Endogenous Amyloid Precursor Protein Processing due to Cellular Aging

2005

Processing of amyloid precursor protein (APP) is a well acknowledged central pathogenic mechanism in Alzheimer disease. However, influences of age-associated cellular alterations on the biochemistry of APP processing have not been studied in molecular detail so far. Here, we report that processing of endogenous APP is down-regulated during the aging of normal human fibroblasts (IMR-90). The generation of intracellular APP cleavage products C99, C83, and AICD gradually declines with increasing life span and is accompanied by a reduced secretion of soluble APP (sAPP) and sAPPalpha. Further, the maturation of APP was reduced in senescent cells, which has been shown to be directly mediated by a…

ADAM10NicastrinEndogenyBiochemistryCell LineAmyloid beta-Protein PrecursorMembrane MicrodomainsDownregulation and upregulationEndopeptidasesmental disordersPresenilin-1Amyloid precursor proteinAspartic Acid EndopeptidasesHumansSecretionMolecular BiologyCellular SenescenceMembrane GlycoproteinsbiologyChemistryMembrane ProteinsCell BiologyFibroblastsCholesterolBiochemistrybiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAmyloid precursor protein secretaseIntracellularJournal of Biological Chemistry
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Alpha-secretase as a therapeutic target.

2007

In the non-amyloidogenic pathway the alpha-secretase cleaves the amyloid precursor protein (APP) within the sequence of Abeta-peptides and precludes their formation. In addition, alpha-secretase cleavage releases an N-terminal extracellular domain with neurotrophic and neuroprotective properties. The disintegrin metalloproteinase ADAM10 has been shown to act as alpha-secretase in vivo, to prevent amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model. An increase in alpha-secretase activity therefore is an attractive strategy for treatment of AD and may be achieved by modulating selective signalling pathways. Functional characterization of the human ADAM10 prom…

ADAM10Retinoic acidModels BiologicalReceptors G-Protein-Coupledchemistry.chemical_compoundADAM10 ProteinDownregulation and upregulationAlzheimer DiseaseExtracellularAmyloid precursor proteinAnimalsHumansTranscription factorG protein-coupled receptorbiologyMembrane ProteinsCell biologyEnzyme ActivationADAM ProteinsDisease Models AnimalNeurologychemistryAlpha secretasebiology.proteinNeurology (clinical)Amyloid Precursor Protein SecretasesCurrent Alzheimer research
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Binding mode analysis of ABCA7 for the prediction of novel Alzheimer's disease therapeutics

2021

Graphical abstract

ATP Adenosine-triphosphateNBD nucleotide binding domainGSH reduced glutathionePolypharmacologyAlzheimer’s disease (AD)ATP-binding cassette transporterHTS high-throughput screeningBiochemistryABCA7Structural BiologyPLIF protein ligand interactionMSD membrane spanning domainPDB protein data bankTM transmembrane helixABC ATP-binding cassetteMultitarget modulation (PANABC)RMSD root mean square distanceABC transporter (ABCA1 ABCA4 ABCA7)Computer Science ApplicationsMOE Molecular Operating EnvironmentPharmacophoreSNP single-nucleotide polymorphismBiotechnologyResearch ArticleBBB blood-brain barrierBiophysicsDrug designComputational biologyBiologyAD Alzheimer’s diseasePET positron emission tomographyIC intracellular helixAPP amyloid precursor proteincryo-EM cryogenic-electron microscopyGeneticsHomology modelingBinding siteRational drug design and developmentComputingMethodologies_COMPUTERGRAPHICSNBD-cholesterol 7-nitro-2-13-benzoxadiazol-4-yl-cholesterolTransporterPSO particle swarm optimizationPET tracer (PETABC)ECD extracellular domainR-domain/region regulatory domain/regionABCA1biology.proteinEH extracellular helixTP248.13-248.65BODIPY-cholesterol 44-difluoro-4-bora-3a4a-diaza-s-indacene-cholesterolComputational and Structural Biotechnology Journal
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Abnormal Marker Expression in Acute Leukemia (AL) Characterized by Monoclonal Antibodies and Flow Cytometry

1987

The application of refined immunologic and enzymatic markers to conventional morphologic and cytochemical techniques has revealed an unexpected heterogeneitiy in acute leukemia (AL). Since the development of monoclonal antibodies (MoAbs) to lineage specific differentiation markers, there have been several reports of AL patients whose blast cells represent relatively homogeneous populations with phenotypic features of more than one cell line [1–5] or are characterized by the coexistence of separate cell populations each demonstrating either lymphoid or myeloid features [6–10].

Acute leukemiaMyeloidmedicine.diagnostic_testmedicine.drug_classCellBiologyMonoclonal antibodyMolecular biologyPhenotypeFlow cytometrymedicine.anatomical_structureCell culturePrecursor cellImmunologymedicine
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Topographic heterogeneity of amyloid B-protein epitopes in brains with various forms of neuronal ceroid lipofuscinoses suggesting defective processin…

1990

To verify our hypothesis of defective protease inhibitor domains that are encoded by abnormal processing of amyloid precursor protein (APP) in brains of patients with neuronal ceroid lipofuscinoses (NCL), immunohistochemical and cytochemical studies were performed with monoclonal antibodies (mAbs) directed against various domains of APP. For the studies, 22 autopsy brains were used: 12 with different forms of NCL, and 10 control brains. The staining procedure for the avidin-biotin complex (ABC) technique and the postembedding gold-labelled procedure for electron microscopy (EM) were employed. Of all mAbs used for the study, only mAbs generated against amyloid B-protein bound to neural tissu…

AdultAmyloidPathologymedicine.medical_specialtyBatten diseaseAdolescentAmyloidImmunocytochemistryPathology and Forensic MedicineLipofuscinEpitopes03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineNeuronal Ceroid-LipofuscinosesAmyloid precursor proteinmedicineHumansSenile plaquesChildAged030304 developmental biology0303 health sciencesAmyloid beta-PeptidesbiologyAntibodies MonoclonalBrainInfantMiddle Agedmedicine.diseaseImmunohistochemistryMolecular biology3. Good healthChild Preschoolbiology.proteinNeuronal ceroid lipofuscinosisNeurology (clinical)Protein Processing Post-Translational030217 neurology & neurosurgeryImmunostainingActa Neuropathologica
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Influence of training and a maximal exercise test in analytical variability of muscular, hepatic, and cardiovascular biochemical variables.

2014

Short, middle, and long-term exercise, as well as the relative intensity of the physical effort, may influence a broad array of laboratory results, and it is thereby of pivotal importance to appropriately differentiate the 'physiologic' from the 'pathological' effects of exercise. Therefore, the values of some biomarkers in physically active subjects may be cautiously interpreted since the results may fall outside the conventional reference ranges. It has been demonstrated that middle and long-term endurance and/or strenuous exercise triggers transient elevations of muscular and cardiac biomarkers. However, no data have been published about the effect of short-term maximal exercise test on …

AdultCalcitoninMalemedicine.medical_specialtyCardiac biomarkersCardiovascular biomarkersCalcitonin Gene-Related PeptideClinical BiochemistryPhysical ExertionPhysical medicine and rehabilitationReference ValuesInternal medicineNatriuretic Peptide BrainmedicineCreatine Kinase MB FormHumansAspartate AminotransferasesProtein PrecursorsMuscle SkeletalPathologicalExerciseRelative intensitybiologyL-Lactate Dehydrogenasebusiness.industryC-reactive proteinSkeletal muscleHeartGeneral Medicinegamma-GlutamyltransferaseLaboratory resultsPeptide FragmentsTroponinmedicine.anatomical_structureexercise; laboratory; biomarkersC-Reactive ProteinLiverCardiologybiology.proteinExercise TestPhysical EnduranceMaximal exerciseSedentary BehaviorbusinesslaboratoryBiomarkersScandinavian journal of clinical and laboratory investigation
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A Phase I Study of Intravenous LBH589, a Novel Cinnamic Hydroxamic Acid Analogue Histone Deacetylase Inhibitor, in Patients with Refractory Hematolog…

2006

Abstract Purpose: LBH589 is a novel histone deacetylase inhibitor that inhibits proliferation and induces apoptosis in tumor cell lines. In this phase I study, LBH589 was administered i.v. as a 30-minute infusion on days 1 to 7 of a 21-day cycle. Experimental Design: Fifteen patients (median age, 63 years; range, 42-87 years) with acute myeloid leukemia (13 patients), acute lymphocytic leukemia (1 patient), or myelodysplastic syndrome (1 patient) were treated with LBH589 at the following dose levels (mg/m2): 4.8 (3 patients), 7.2 (3 patients), 9.0 (1 patient), 11.5 (3 patient), and 14.0 (5 patients). The levels of histone acetylation were measured using quantitative flow cytometry and plasm…

AdultCancer ResearchIndolesMaximum Tolerated Dosemedicine.drug_classApoptosisPharmacologyHydroxamic AcidsDrug Administration ScheduleHistonesStructure-Activity Relationshipchemistry.chemical_compoundPredictive Value of TestsPanobinostatAcute lymphocytic leukemiaPanobinostatBiomarkers TumormedicineHumansEnzyme InhibitorsAgedCell ProliferationAged 80 and overDose-Response Relationship Drugbusiness.industryHistone deacetylase inhibitorArea under the curveQTcF ProlongationMyeloid leukemiaMiddle AgedPrecursor Cell Lymphoblastic Leukemia-Lymphomamedicine.diseaseHypokalemiaHistone Deacetylase InhibitorsLeukemiaTreatment OutcomeOncologychemistryCinnamatesLeukemia MyeloidMyelodysplastic SyndromesAcute DiseaseInjections IntravenousImmunologymedicine.symptombusinessFollow-Up StudiesClinical Cancer Research
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