Search results for "BETA-PROTEIN"

showing 10 items of 73 documents

Membrane topology of gp41 and amyloid precursor protein: Interfering transmembrane interactions as potential targets for HIV and Alzheimer treatment

2009

AbstractThe amyloid precursor protein (APP), that plays a critical role in the development of senile plaques in Alzheimer disease (AD), and the gp41 envelope protein of the human immunodeficiency virus (HIV), the causative agent of the acquired immunodeficiency syndrome (AIDS), are single-spanning type-1 transmembrane (TM) glycoproteins with the ability to form homo-oligomers. In this review we describe similarities, both in structural terms and sequence determinants of their TM and juxtamembrane regions. The TM domains are essential not only for anchoring the proteins in membranes but also have functional roles. Both TM segments contain GxxxG motifs that drive TM associations within the li…

BiophysicsHIV InfectionsBiologyGp41BiochemistryArticleTransmembrane segmentAmyloid beta-Protein PrecursorMembranes (Biologia)Alzheimer DiseaseAmyloid precursor proteinAnimalsHumansSenile plaqueschemistry.chemical_classificationCell MembraneMembraneHIVCell Biologygp41HIV Envelope Protein gp41Transmembrane proteinVirusCell biologyTransmembrane domainchemistryBiochemistryAmyloid precursor proteinMembrane topologyAlzheimerHIV-1biology.proteinGlycoproteinSequence motifBiochimica et Biophysica Acta (BBA) - Biomembranes
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Amyloid precursor protein in platelets: A peripheral marker for the diagnosis of sporadic AD

2001

BACKGROUND: An altered pattern of amyloid precursor protein (APP) forms consisting in a reduced ratio between the upper (130 kDa) and the lower (106 to 110 kDa) immunoreactivity bands has been described in platelets of patients with AD. OBJECTIVE: To evaluate the sensitivity and the specificity of platelet APP forms' ratio (APPr) as a marker for AD. METHODS: Eighty-five patients with probable AD and 95 control subjects (CON), including healthy individuals and neurologic patients, entered the study. Platelet APPr was evaluated by means of Western Blot analysis and immunostaining in the whole platelet homogenate, and calculated by the ratio between the optical density (OD) of the upper (130 k…

Blood PlateletsMalePathologymedicine.medical_specialtyBlood cellCentral nervous system diseaseAmyloid beta-Protein PrecursorDegenerative diseaseWestern blotAlzheimer DiseasemedicineAmyloid precursor proteinHumansPlateletAgedPsychiatric Status Rating Scalesmedicine.diagnostic_testbiologybusiness.industryMiddle Agedmedicine.diseaseAbnormalities in the pattern of platelet amyloid precursor protein forms in patients with mild cognitive impairment and Alzheimer diseasemedicine.anatomical_structureAmyloid precursor proteinbiology.proteinFemaleSettore MED/26 - NeurologiaNeurology (clinical)Alzheimer's diseasebusinessImmunostainingBiomarkers
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Amyloid precursor protein in platelets of patients with Alzheimer disease: effect of acetylcholinesterase inhibitor treatment.

2001

BACKGROUND:Amyloid precursor protein (APP) forms with apparent molecular weights of 130, 110, and 106 kd are present in human platelets. It has been demonstrated that Alzheimer disease (AD) is specifically associated with a decreased APP forms ratio in platelets. OBJECTIVE:To investigate whether acetylcholinesterase (AChE) inhibitor treatment modifies the ratio of platelet APP forms in patients with AD. PATIENTS AND METHODS:From a large sample of patients with probable AD, 30 with mild to moderate AD were selected. Each patient underwent a clinical evaluation including the Mini-Mental State Examination (MMSE) and platelet APP forms analysis at baseline and after 30 days. During this interva…

Blood PlateletsMalemedicine.medical_specialtyIsoformmedicine.drug_classBlotting WesternAlzheimer disease; biomarker; platelet; Amyloid Precursor Protein; Isoformchemistry.chemical_compoundAmyloid beta-Protein PrecursorArts and Humanities (miscellaneous)PiperidinesDonepezil HydrochlorideInternal medicinemental disordersAmyloid precursor proteinMedicineHumansPlateletDonepezilLongitudinal StudiesDonepezilCholinesteraseAgedamyloid alzheimer diseaseplateletbiologybusiness.industryMiddle AgedAcetylcholinesteraseEndocrinologychemistryAcetylcholinesterase inhibitorEnzyme inhibitorIndansAmyloid Precursor Proteinbiology.proteinbiomarkerSettore MED/26 - NeurologiaFemaleNeurology (clinical)Cholinesterase InhibitorsAlzheimer diseasebusinessmedicine.drugFollow-Up Studies
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Inflammatory Chemokines Expression Variations and Their Receptors in APP/PS1 Mice

2021

Background: In Alzheimer’s disease (AD), an increase in inflammation is distinctive. Amyloid precursor protein plus presenilin-1 (APP/PS1 mice) is a model for this illness. Chemokines secreted by central nervous system (CNS) cells could play multiple important roles in AD. Data looking for the chemokines involved in inflammatory mechanisms are lacking. To understand the changes that occur in the inflammation process in AD, it is necessary to improve strategies to act on specific inflammatory targets. Objective: Chemokines and their receptors involved in phagocytosis, demyelination, chemotaxis, and coagulation were the objective of our study. Methods: Female APPswe/PS1 double-transgenic mice…

CCR1CCR2ChemokineCCR3CCR4Mice TransgenicCCL7Amyloid beta-Protein PrecursorMiceChemokine receptorAlzheimer Diseasemental disordersAnimalsInflammationAmyloid beta-PeptidesbiologyGeneral NeuroscienceBrainChemotaxisGeneral MedicineDisease Models AnimalPsychiatry and Mental healthClinical PsychologyImmunologybiology.proteinFemaleReceptors ChemokineChemokinesGeriatrics and GerontologyJournal of Alzheimer's Disease
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Holo-APP and G-protein-mediated signaling are required for sAPPa-induced activation of the Akt survival pathway

2014

International audience; Accumulating evidence indicates that loss of physiologic amyloid precursor protein (APP) function leads to reduced neuronal plasticity, diminished synaptic signaling and enhanced susceptibility of neurons to cellular stress during brain aging. Here we investigated the neuroprotective function of the soluble APP ectodomain sAPPa (soluble APPa), which is generated by cleavage of APP by a-secretase along the non-amyloidogenic pathway. Recombinant sAPPa protected primary hippocampal neurons and SH-SY5Y neuroblastoma cells from cell death induced by trophic factor deprivation. We show that this protective effect is abrogated in neurons from APP-knockout animals and APP-de…

Cancer ResearchCell SurvivalADAM10Amino Acid MotifsImmunology[SDV.BC]Life Sciences [q-bio]/Cellular BiologyIn Vitro TechniquesHydroxamic AcidsHippocampusNeuroprotectionCell LineADAM10 ProteinAmyloid beta-Protein PrecursorMicePhosphatidylinositol 3-Kinases03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicinemental disordersAmyloid precursor proteinAnimalsHumansProtein kinase BPI3K/AKT/mTOR pathwayPhosphoinositide-3 Kinase Inhibitors030304 developmental biologyMice Knockout0303 health sciencesbiologyBiochemistry and Molecular BiologyMembrane ProteinsDipeptidesCell BiologyMolecular biologyRecombinant ProteinsMice Inbred C57BLADAM ProteinsPertussis Toxinbiology.proteinOriginal ArticleSynaptic signalingAmyloid Precursor Protein SecretasesNeuron deathProto-Oncogene Proteins c-aktAmyloid precursor protein secretase030217 neurology & neurosurgeryBiokemi och molekylärbiologiSignal Transduction
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Inhibitors of Rho-kinase modulate amyloid-β (Aβ) secretion but lack selectivity for Aβ42

2005

Certain non-steroidal anti-inflammatory drugs (NSAIDs) preferentially inhibit production of the amyloidogenic Abeta42 peptide, presumably by direct modulation of gamma-secretase activity. A recent report indicated that NSAIDs could reduce Abeta42 by inhibition of the small GTPase Rho, and a single inhibitor of Rho kinase (ROCK) mimicked the effects of Abeta42-lowering NSAIDs. To investigate whether Abeta42 reduction is a common property of ROCK inhibitors, we tested commercially available compounds in cell lines that were previously used to demonstrate the Abeta42-lowering activity of NSAIDs. Surprisingly, we found that two ROCK inhibitors reduced total Abeta secretion in a dose-dependent m…

Cell SurvivalMutantPeptideCHO CellsProtein Serine-Threonine KinasesPharmacologyBiochemistryAmyloid beta-Protein PrecursorCellular and Molecular NeuroscienceCricetulusCricetinaeEndopeptidasesmental disordersAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesSecretionSmall GTPaseEnzyme InhibitorsRho-associated protein kinasechemistry.chemical_classificationrho-Associated KinasesAmyloid beta-PeptidesbiologyAnti-Inflammatory Agents Non-SteroidalIntracellular Signaling Peptides and ProteinsIn vitro toxicologyProtein-Tyrosine KinasesPeptide Fragmentsnervous system diseasesBiochemistrychemistrybiology.proteinAmyloid Precursor Protein SecretasesSelectivityProtein Processing Post-TranslationalJournal of Neurochemistry
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α-Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure

2001

Disintegrin metalloproteases from different organisms form the ADAM (a disintegrin and metalloprotease) family. All members display a common domain organization and possess four potential functions: proteolysis, cell adhesion, cell fusion, and cell signaling. Members of the ADAM family are responsible for the proteolytic cleavage of transmembrane proteins and release of their extracellular domain. The proteolytic process is referred to as ectodomain shedding, which is activated by phorbol esters and inhibited by hydroxamic acid-based inhibitors. We have shown that the disintegrin metalloprotease ADAM 10 has both constitutive and regulated alpha-secretase activity. Expression of a dominant n…

Cell signalingDisintegrinsMolecular Sequence DataProtein domainBiologyGeneral Biochemistry Genetics and Molecular BiologyADAM10 ProteinAmyloid beta-Protein PrecursorHistory and Philosophy of ScienceEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansProtease InhibitorsAmino Acid SequenceCell adhesionMetalloproteinaseGeneral NeuroscienceHEK 293 cellsMembrane ProteinsMetalloendopeptidasesRecombinant ProteinsTransmembrane proteincarbohydrates (lipids)ADAM ProteinsBiochemistryEctodomainbiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAnnals of the New York Academy of Sciences
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Estrogen-induced cell signalling in a cellular model of Alzheimer's disease.

2003

Alzheimer's disease (AD) is characterised by deposition of a 4 kDa amyloid-beta peptide (Abeta) into senile plaques of the affected brain. Abeta is a proteolytic product of the membrane protein, amyloid precursor protein (APP). An alternative cleavage pathway involves alpha-secretase activity and results in secretion of a 100 kDa non-amyloidogenic APP (sAPPalpha) and therefore a potential reduction in Abeta secretion. We have shown that estrogen induces alpha-cleavage and therefore results in the secretion of sAPPalpha. This secretion is signalled via MAP-kinase and PI-3 kinase signal-transduction pathways. These pathways also have the potential to inhibit the activation of glycogen synthas…

Cell signalingMAP Kinase Signaling SystemEndocrinology Diabetes and MetabolismClinical BiochemistryBiologyBiochemistryModels BiologicalAmyloid beta-Protein PrecursorGlycogen Synthase Kinase 3Phosphatidylinositol 3-KinasesEndocrinologyGSK-3Alzheimer DiseaseAmyloid precursor proteinAnimalsHumansSecretionSenile plaquesMolecular BiologyGSK3BAmyloid beta-PeptidesGlycogen Synthase Kinase 3 betaCell DeathKinaseBrainEstrogensCell BiologyCell biologybiology.proteinMolecular MedicineSignal transductionLithium ChloridePeptidesSignal TransductionThe Journal of steroid biochemistry and molecular biology
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Oxidative stress resistance in hippocampal cells is associated with altered membrane fluidity and enhanced nonamyloidogenic cleavage of endogenous am…

2010

Reactive oxygen species (ROS) have important roles as signaling molecules in the regulation of a variety of biological processes. On the other hand, chronic oxidative stress exerted by ROS is widely considered a causative factor in aging. Therefore, cells need to be able to adapt to a chronic oxidative challenge and do so to a certain cell-type-specific extent. Recently, we have shown in oxidative-stress-resistant cell lines, HT22(H2O2) and HT22(Glu), derived from the neuronal cell line HT22 by chronic exposure to sublethal concentrations of H(2)O(2) and glutamate, that, in addition to the known antioxidant defense mechanisms, e.g., activation of antioxidant enzymes or up-regulation of heat…

Cell signalingMembrane FluidityBlotting WesternOxidative phosphorylationmedicine.disease_causeHippocampusBiochemistryNeuroprotectionCell LineAmyloid beta-Protein PrecursorMembrane MicrodomainsPhysiology (medical)Membrane fluidityAmyloid precursor proteinmedicineHumansCellular SenescenceNeuronschemistry.chemical_classificationReactive oxygen speciesbiologyChemistryCell MembraneMembrane ProteinsCell biologyOxidative Stressbiology.proteinSphingomyelinOxidative stressFree Radical Biology and Medicine
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Entrapment of A Beta 1-40 peptide in unstructured aggregates

2012

Recognizing the complexity of the fibrillogenesis process provides a solid ground for the development of therapeutic strategies aimed at preventing or inhibiting protein-protein aggregation. Under this perspective, it is meaningful to identify the possible aggregation pathways and their relative products. We found that Aβ-peptide dissolved in a pH 7.4 solution at small peptide concentration and low ionic strength forms globular aggregates without typical amyloid β-conformation. ThT binding kinetics was used to monitor aggregate formation. Circular dichroism spectroscopy, AFM imaging, static and dynamic light scattering were used for structural and morphological characterization of the aggre…

Circular dichroismAmyloidKineticsPeptideProtein Structure SecondaryFIBRIL FORMATIONDynamic light scatteringMEMBRANE DISRUPTIONGeneral Materials ScienceFiberATOMIC-FORCE MICROSCOPYchemistry.chemical_classificationAmyloid beta-PeptidesChemistryProtein StabilityOsmolar ConcentrationTemperatureFibrillogenesisCondensed Matter PhysicsReceptor–ligand kineticsPeptide FragmentsAMYLOID-BETA-PROTEINALZHEIMERS-DISEASECrystallographyKineticsSpectrometry FluorescenceBiophysicsProtein Multimerization
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