Search results for "AMyloid"

showing 10 items of 494 documents

Cerebral microbleeds and vascular cognitive impairment

2010

Abstract MRI manifestations of small vessel diseases including white matter hyperintensities and lacunes have been recognized as potential substrates of vascular cognitive impairment for many years. Cerebral microbleeds (CMBs) – small, perviascular haemorrhages seen as small, well-demarcated, hypointense, rounded lesions on MRI sequences sensitive to magnetic susceptibility effects – are also now recognized as an imaging marker for small vessel pathology, but their clinical impact on cognition remains uncertain. CMBs are present in about a third of patients with ischaemic stroke, and in a high proportion of patients with Alzheimer's disease, cerebral amyloid angiopathy, and vascular dementi…

Pathologymedicine.medical_specialtybusiness.industryVascular diseaseDementia VascularCognitive disordermedicine.diseasecerebral microbleeds vascular cognitive impairmentMagnetic Resonance ImagingHyperintensityCentral nervous system diseaseDegenerative diseaseNeurologyHumansMedicineDementiaNeurology (clinical)Cerebral amyloid angiopathyCognition DisordersbusinessVascular dementiaCerebral Hemorrhage
researchProduct

The selective β1-adrenoceptor antagonist nebivolol is a potential oestrogen receptor agonist with neuroprotective abilities

2010

Background and purpose:  Nebivolol, a selective β1-adrenoceptor antagonist mediating rapid vasodilating effects, is used clinically to treat hypertension. Recently, it was reported that nebivolol also acts as an oestrogen receptor (ER) agonist. To investigate the neuroprotective potential of oestrogens, we assessed the oestrogenic effects of nebivolol in several in vitro neuronal models. Experimental approach:  Human neuroepithelioma SK-N-MC cells stably transfected with human ER α and β, and mouse N2A neuroblastoma cells expressing human APP695SWE[N2Aswe, stably transfected with the Swedish mutation form of the Alzheimer-associated amyloid precursor protein (APPswe, K670M/N671L)] were incu…

PharmacologyAgonistbiologymedicine.drug_classTransfectionPharmacologyNeuroprotectionNebivololCell culturebiology.proteinAmyloid precursor proteinmedicineReceptorAmyloid precursor protein secretasemedicine.drugBritish Journal of Pharmacology
researchProduct

Selective Modulation of Aβ42 Production in Alzheimers Disease: Non-Steroidal Anti-Inflammatory Drugs and Beyond

2006

The amyloid-β (Aβ) peptides and in particular the longer, highly amyloidogenic isoform Aβ42 are believed by many to be the central disease-causing agents in Alzheimers disease (AD). Consequently, academic and pharmaceutical laboratories have focused on elucidating the mechanisms of Aβ production and developing strategies to diminish Aβ formation for treatment or prevention of AD. The most substantial advances have been made with respect to inhibitors of the γ-secretase enzyme, which catalyzes the final step in the generation of Aβ from the amyloid precursor protein (APP). Highly potent γ-secretase inhibitors which suppress production of all Aβ peptides are available today. However, due to t…

Pharmacologychemistry.chemical_classificationGene isoformbiologybusiness.industryNotch signaling pathwayPharmacologymedicine.diseaseSmall moleculePathogenesisEnzymechemistryMechanism of actionDrug DiscoveryImmunologymedicineAmyloid precursor proteinbiology.proteinAlzheimer's diseasemedicine.symptombusinessCurrent Pharmaceutical Design
researchProduct

A Closer Look at α-Secretase

2008

Accumulation of amyloid beta-peptides (Abeta) in the brain is believed to contribute to the development of Alzheimer disease (AD). Abeta, a 40-42 amino acid-comprising proteolytical fragment of the amyloid precursor protein (APP), is released from APP by sequential cleavages via beta- and gamma-secretases. However, the predominant route of APP processing consists of successive cleavages by alpha- and gamma-secretases. Alpha-secretase attacks APP inside the Abeta sequence, and therefore prevents formation of neurotoxic Abeta. After cleavage by alpha-secretase, the soluble N-terminal domain of APP, which possesses neurotrophic and neuroprotective properties, is released. In AD patients, a dec…

Phospholipase CbiologyKinaseChemistryADAM10Cell biologyNeurologyAlpha secretasemental disordersbiology.proteinAmyloid precursor proteinNeurology (clinical)ReceptorAmyloid precursor protein secretaseProtein kinase CCurrent Alzheimer Research
researchProduct

The metalloproteinase-disintegrin ADAM10 is exclusively expressed by type I muscle fibers.

2008

ADAM10 (Kuzbanian) is a member of a recently discovered family of membrane-anchored metalloproteinases with a complex and conserved domain structure. In part, these metalloproteinases have been implicated in muscle formation. Herein the expression pattern of ADAM10 in human skeletal muscle was studied. ADAM10 was found to be present in human myoblasts and to be exclusively expressed in type I fibers, suggesting that it may be critical in muscle fiber differentiation.

PhysiologyADAM10Matrix metalloproteinaseCellular and Molecular NeuroscienceADAM10 ProteinPhysiology (medical)DisintegrinmedicineMyocyteHumansAdenosine TriphosphatasesMetalloproteinasebiologyMyosin Heavy ChainsMyogenesisChemistrySkeletal muscleMembrane ProteinsCell biologyADAM Proteinsmedicine.anatomical_structureMuscle Fibers Slow-TwitchBiochemistrybiology.proteinNeurology (clinical)Amyloid Precursor Protein SecretasesITGA7Musclenerve
researchProduct

Imaging P-Glycoprotein Induction at the Blood–Brain Barrier of a β-Amyloidosis Mouse Model with 11C-Metoclopramide PET

2019

P-glycoprotein (ABC subfamily B member 1, ABCB1) plays an important role at the blood–brain barrier (BBB) in promoting clearance of neurotoxic β-amyloid (Aβ) peptides from the brain into the blood. ABCB1 expression and activity were found to be decreased in the brains of Alzheimer disease patients. Treatment with drugs that induce cerebral ABCB1 activity may be a promising approach to delay the build-up of Aβ deposits in the brain by enhancing clearance of Aβ peptides from the brain. The aim of this study was to investigate whether PET with the weak ABCB1 substrate radiotracer 11C-metoclopramide can measure ABCB1 induction at the BBB in a β-amyloidosis mouse model (APP/PS1-21 mice) and in w…

Pregnane X receptorMetoclopramidebiologybusiness.industryActivator (genetics)AmyloidosisPharmacologyBlood–brain barriermedicine.disease03 medical and health sciences0302 clinical medicinemedicine.anatomical_structure030220 oncology & carcinogenesisbiology.proteinMedicineImmunohistochemistryRadiology Nuclear Medicine and imagingAlzheimer's diseasebusiness030217 neurology & neurosurgerymedicine.drugP-glycoproteinJournal of Nuclear Medicine
researchProduct

Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

2009

Abstract Both the cellular prion protein (PrPc) and the amyloid precursor protein (APP) are physiologically subjected to complex proteolytic processing events. While for APP the proteinases involved – alpha-, beta- and gamma-secretase – have been identified in vitro and in vivo, the cleavage of PrPc by now has been linked only to the shedding activity of the metalloproteinase ADAM10 and/or ADAM17 in cell culture. Here we show that neuronal overexpression of the alpha-secretase ADAM10 in mice reduces all PrPc species detected in the brain instead of leading to enhanced amounts of specific cleavage products of PrPc. Additionally, the incubation time of mice after scrapie infection is signific…

Prionsanimal diseasesADAM10Molecular Sequence DataPrion diseaseScrapieMice Transgeniclcsh:RC321-571ADAM10 ProteinMiceIn vivomental disordersNeurotoxicitymedicineAmyloid precursor proteinAnimalsHumansGliosisAmino Acid Sequencealpha-Secretaselcsh:Neurosciences. Biological psychiatry. NeuropsychiatrySheddingMetalloproteinasebiologyChemistryBrainMembrane ProteinsMolecular biologyIn vitronervous system diseasesMice Inbred C57BLADAM ProteinsNeurologyAlpha secretaseGliosisbiology.proteinCattlemedicine.symptomAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalScrapieNeurobiology of disease
researchProduct

The unsolved relationship of brain aging and late-onset Alzheimer disease.

2009

Late-onset Alzheimer disease is the most common form of dementia and is strongly associated with age. Today, around 24 million people suffer from dementia and with aging of industrial populations this number will significantly increase throughout the next decades. An effective therapy that successfully decelerates or prevents the progressive neurodegeneration does not exist. Histopathologically Alzheimer disease is characterized by extensive extracellular amyloid beta (Abeta) plaques, intracellular neurofibrillary tangles (NFTs), synaptic loss and neuronal cell death in distinct brain regions. The molecular correlation of Abeta or NFTs and development of late-onset Alzheimer disease needs f…

Programmed cell deathAgingAmyloid βFree RadicalsBiophysicsmedicine.disease_causeBiochemistryModels BiologicalAtrophyAlzheimer DiseasemedicineExtracellularDementiaAnimalsHumansMolecular BiologyAmyloid beta-Peptidesbusiness.industryBrainNeurodegenerative Diseasesmedicine.diseaseDementiaAlzheimer's diseasebusinessNeuroscienceOxidative stressIntracellularBiochimica et biophysica acta
researchProduct

Lipids Nutrients in Parkinson and Alzheimer’s Diseases: Cell Death and Cytoprotection

2020

Neurodegenerative diseases, particularly Parkinson’s and Alzheimer’s, have common features: protein accumulation, cell death with mitochondrial involvement and oxidative stress. Patients are treated to cure the symptoms, but the treatments do not target the causes; so, the disease is not stopped. It is interesting to look at the side of nutrition which could help prevent the first signs of the disease or slow its progression in addition to existing therapeutic strategies. Lipids, whether in the form of vegetable or animal oils or in the form of fatty acids, could be incorporated into diets with the aim of preventing neurodegenerative diseases. These different lipids can inhibit the cytotoxi…

Programmed cell deathParkinson's diseaseInflammationReviewDiseasePharmacologyMitochondrionmedicine.disease_causelipids nutrientsCatalysislcsh:ChemistryInorganic ChemistrysynucleinFish OilsAlzheimer DiseaseHumansPlant OilsMedicinePhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopybusiness.industryFatty AcidsOrganic ChemistryapoptosisamyloidParkinson DiseaseNutrientsGeneral Medicinemedicine.diseaseLipidsCytoprotectionComputer Science ApplicationsmitochondriaOxidative Stresslcsh:Biology (General)lcsh:QD1-999CytoprotectionParkinson’s diseaseSynucleinTaumedicine.symptombusinessAlzheimer’s diseaseOxidative stressInternational Journal of Molecular Sciences
researchProduct

Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors.

1996

The extracellular domains of a diverse group of membrane proteins are shed in response to protein kinase C activators such as phorbol 12-myristate 13-acetate (PMA). The lack of sequence similarity in the cleavage sites suggests the involvement of many proteases of diverse specificity in this process. However, a mutant Chinese hamster ovary cell line recently isolated for being defective in PMA-activated shedding of the membrane-anchored growth factor transforming growth factor alpha precursor (proTGF-alpha) is concomitantly defective in the shedding of many other unrelated membrane proteins. Here we show that independent mutagenesis and selection experiments yield shedding mutants having th…

ProteasesCellCHO CellsBiologyHydroxamic AcidsTransfectionBiochemistryAmyloid beta-Protein PrecursorAntigens CDCricetinaemedicineAnimalsProtease InhibitorsL-SelectinProtein PrecursorsCell adhesionMolecular BiologyProtein kinase CMetalloproteinaseChinese hamster ovary cellCell MembraneGenetic Complementation TestMembrane ProteinsMetalloendopeptidasesCell BiologyReceptors InterleukinTransforming Growth Factor alphaReceptors Interleukin-6Cell biologyKineticsmedicine.anatomical_structurePhenotypeEctodomainMembrane proteinMutagenesisTetradecanoylphorbol AcetatePhenanthrolinesThe Journal of biological chemistry
researchProduct