Search results for "BETA-PROTEIN"

showing 10 items of 73 documents

Brothers in arms: proBDNF/BDNF and sAPPα/Aβ-signaling and their common interplay with ADAM10, TrkB, p75NTR, sortilin, and sorLA in the progression of…

2021

Abstract Brain-derived neurotrophic factor (BDNF) is an important modulator for a variety of functions in the central nervous system (CNS). A wealth of evidence, such as reduced mRNA and protein level in the brain, cerebrospinal fluid (CSF), and blood samples of Alzheimer’s disease (AD) patients implicates a crucial role of BDNF in the progression of this disease. Especially, processing and subcellular localization of BDNF and its receptors TrkB and p75 are critical determinants for survival and death in neuronal cells. Similarly, the amyloid precursor protein (APP), a key player in Alzheimer’s disease, and its cleavage fragments sAPPα and Aβ are known for their respective roles in neuropro…

ADAM10Clinical BiochemistryNerve Tissue ProteinsTropomyosin receptor kinase BReceptors Nerve Growth FactorBiochemistryNeuroprotectionADAM10 ProteinAmyloid beta-Protein PrecursorNeurotrophic factorsAlzheimer DiseaseAmyloid precursor proteinHumansReceptor trkBMolecular BiologyLDL-Receptor Related ProteinsAmyloid beta-PeptidesMembrane GlycoproteinsbiologyBrain-Derived Neurotrophic FactorMembrane ProteinsMembrane Transport ProteinsAdaptor Proteins Vesicular Transportnervous systembiology.proteinSignal transductionAmyloid Precursor Protein SecretasesNeuroscienceAmyloid precursor protein secretaseNeurotrophinBiological chemistryReferences
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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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Pure Progressive Amnesia and the APPV717G Mutation

2009

We report an isolated, slowly progressive, pure amnestic phenotype in a 59-year-old member of a family affected by autosomal dominant familial Alzheimer disease. Early-onset Alzheimer disease in this family was associated with a V717G mutation in the amyloid precursor protein gene (APP). Subjective impairment of episodic memory began in our subject at the age of 44 years and subsequent, longitudinal neuropsychologic assessment confirmed progressive, severe, global impairment of memory functions over a period of 14 years with preservation of other cognitive domains. The mean annual hippocampal atrophy rate, determined by volumetric magnetic resonance imaging was intermediate between values p…

AdultMaleAgingPathologymedicine.medical_specialtyGlycineAmnesiaHippocampusAmyloid beta-Protein PrecursorAtrophyAlzheimer DiseasemedicineHumansDementiaMemory disorderEpisodic memoryAgedSettore M-PSI/02 - Psicobiologia E Psicologia FisiologicaCognitive disorderValineMiddle Agedmedicine.diseaseAPPV717G mutation.PedigreePsychiatry and Mental healthClinical PsychologyPhenotypeMutationDisease ProgressionPure progressive amnesiaFemaleAmnesiaAtrophyGeriatrics and Gerontologymedicine.symptomAlzheimer's diseasePsychologyGerontologyFrontotemporal dementia
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Brain aging and late-onset Alzheimer's disease: many open questions.

2012

ABSTRACTDespite decades of research in the field of Alzheimer's disease (AD), a real understanding of its molecular pathophysiology and treatments relevant to the day-to-day lives of patients remain out of reach. Research has, with good reason, focused on certain key pathways and potential mechanisms, but sometimes this has been at the expense of work on other theories, which may be slowing down progress in this field. Interesting theories at present include oxidative stress and caloric restriction. Work on the Aβ cascade should continue but with a shift in focus to its intracellular effects and an awareness that additional pathogenetic factors and processes must be involved – most importan…

AgingHyperphosphorylationLate onsettau ProteinsDiseaseEpigenesis GeneticAmyloid beta-Protein PrecursorAlzheimer DiseaseIntervention (counseling)MedicineDementiaAnimalsHumansEpigeneticsCaloric Restrictionbusiness.industryNeurodegenerationBrainmedicine.diseasePsychiatry and Mental healthClinical PsychologyOxidative StressGeriatrics and GerontologyAlzheimer's diseasebusinessGerontologyNeuroscienceInternational psychogeriatrics
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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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Functional Role of Lipoprotein Receptors in Alzheimers Disease

2008

The LDL receptor gene family constitutes a class of structurally closely related cell surface receptors fulfilling diverse functions in different organs, tissues, and cell types. The LDL receptor is the prototype of this family, which also includes the VLDLR, ApoER2/LRP8, LRP1 and LRP1B, as well as Megalin/GP330, SorLA/LR11, LRP5, LRP6 and MEGF7. Recently several lines of evidence have positioned the LDL receptor gene family as one of the key players in Alzheimer's disease (AD) research. Initially this receptor family was of high interest due to its key function in cholesterol/apolipoprotein E (ApoE) uptake, with the epsilon4 allele of ApoE as the strongest genetic risk factor for late-onse…

Apolipoprotein EAmyloid beta-PeptidesbiologyChemistryEndosomeLRP1BLRP1Cell biologyAmyloid beta-Protein PrecursorApolipoproteins ECholesterolReceptors LDLNeurologyAlzheimer DiseaseCell surface receptormental disordersLDL receptorAmyloid precursor proteinbiology.proteinAnimalsHumansNeurology (clinical)ReceptorCurrent Alzheimer Research
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Functional role of the low-density lipoprotein receptor-related protein in Alzheimer's disease.

2006

Alzheimer’s disease (AD) is the most common age-related neurodegenerative disorder, characterized by neuronal loss, neurofibrillary tangle formation and the extracellular deposition of amyloid-β (Aβ) plaques. The amyloid precursor protein (APP) and the enzymes responsible for Aβ generation seem to be the base elements triggering the destructive processes. Initially, the low-density lipoprotein receptor-related protein (LRP) was genetically linked to AD and later it emerged to impact on many fundamental events related to this disease. LRP is not only involved in Aβ clearance but is also the major receptor of several AD-associated ligands, e.g. apolipoprotein E and α<sub>2</sub>-m…

Apolipoprotein EFunctional rolemedicine.medical_specialtyPathologybiologyChemistryDiseaseLRP1Amyloid beta-Protein PrecursorEndocrinologyNeurologyAlzheimer DiseaseInternal medicineLDL receptormedicineExtracellularAmyloid precursor proteinbiology.proteinNeurofibrillary tangle formationAnimalsHumansNeurology (clinical)LDL-Receptor Related ProteinsNeuro-degenerative diseases
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Haptoglobin interacts with apolipoprotein E and beta-amyloid and influences their crosstalk.

2014

Beta-amyloid accumulation in brain is a driving force for Alzheimer's disease pathogenesis. Apolipoprotein E (ApoE) represents a critical player in beta-amyloid homeostasis, but its role in disease progression is controversial. We previously reported that the acute-phase protein haptoglobin binds ApoE and impairs its function in cholesterol homeostasis. The major aims of this study were to characterize the binding of haptoglobin to beta-amyloid, and to evaluate whether haptoglobin affects ApoE binding to beta-amyloid. Haptoglobin is here reported to form a complex with beta-amyloid as shown by immunoblotting experiments with purified proteins, or by its immunoprecipitation in brain tissues …

Apolipoprotein EMalePhysiologyDiseaseBeta-amyloidBiochemistryAmyloid beta-Protein PrecursorAlzheimer' diseasepolycyclic compoundsskin and connective tissue diseasesapolipoprotein EbiologyChemistryMedicine (all)Haptoglobinfood and beveragesBrainApoE/A? complexGeneral MedicineMiddle AgedhaptoglobinCrosstalk (biology)ApoE/Aβ complexSettore MED/26 - Neurologialipids (amino acids peptides and proteins)FemaleAlzheimer's diseaseProtein BindingAdultmedicine.medical_specialtyImmunoprecipitationCognitive NeuroscienceEnzyme-Linked Immunosorbent AssayCHO CellsTransfectionAlzheimer' disease; ApoE/Aβ complex; Apolipoprotein E; Beta-amyloid; Haptoglobin; Human brain tissue; Adult; Aged; Alzheimer Disease; Amyloid beta-Peptides; Amyloid beta-Protein Precursor; Analysis of Variance; Animals; Apolipoproteins E; Brain; CHO Cells; Cricetulus; Enzyme-Linked Immunosorbent Assay; Female; Haptoglobins; Humans; Immunoprecipitation; Male; Middle Aged; Mutation; Protein Binding; Transfection; Biochemistry; Cell Biology; Physiology; Cognitive Neuroscience; Medicine (all)NOApolipoproteins ECricetulusAlzheimer DiseaseInternal medicinemental disordersmedicineAnimalsHumansImmunoprecipitationAgedAnalysis of VarianceAmyloid beta-PeptidesHaptoglobinsNeurotoxicityAlzheimer’diseaseCell Biologymedicine.diseasehuman brain tissueEndocrinologyMutationbiology.proteinAlzheimer'diseaseHomeostasisACS chemical neuroscience
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