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article, tau, muscarinic, phosphorylation, privacy, cookies, content, journal, agonists, gskβ, access, information, publish, search, alzheimers, data, log, research, neural, nonneuronal, cells, inhibition, neurons, forlenza, spink, dayanandan, disease, kinase, receptor, discover, springer, optional, personal, parties, policy, find, track, transmission, reduce, cite, anderton, olesen, lovestone, explore, metabolism, protein, compounds, process, impairment, glycogen,

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month download article/chapter reduced tau phosphorylation gsk-3β phosphorylation gsk-3β inhibition neural transmission aims ampk ameliorates alzheimer privacy choices/manage cookies muscarinic agonists alter full article pdf related subjects stably phosphorylated tau m1 receptor disease-modifying properties specific muscarinic agonist tau phosphorylation european economic area scope submit manuscript α-secretase cleavage early event correlating microtubule-binding properties muscarinic receptor conditions privacy policy glycogen synthase kinase-3 amyloid precursor protein accepting optional cookies gsk-3β journal finder publish neuronal cells expressing pkcε activation article journal cognitive impairment article log neural transm 107 article forlenza article cite 1007/s007020070034 keywords phosphorylates tau disease process check access instant access privacy policy personal data lovestone department books a muscarinic receptors tau pathology protein kinase optional cookies manage preferences journal publish

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         description: Muscarinic agonists alter the metabolism of amyloid precursor protein, leading to an increase in α-secretase cleavage and a decreased production of amyloidogenic peptides; suggesting that these compounds might modify the Alzheimer's disease process. A second therapeutic target in AD is the accumulation of stably phosphorylated tau into neurofibrillary tangles; an early event correlating with cognitive impairment. Glycogen synthase kinase-3 (GSK-3β) phosphorylates tau and is inhibited via protein kinase C (PKC). As certain muscarinic receptors are linked to PKC, we examined the effect of a range of agonists on GSK-3β phosphorylation of tau. In neurons a non-specific muscarinic agonist, carbachol, reduced tau phosphorylation. In non-neuronal cells expressing the m1 receptor a range of m1 agonists reduced transiently-expressed tau phosphorylation and altered its microtubule-binding properties. These findings link the two pathological process of AD – APP metabolism and tau phosphorylation – and suggest that muscarinic and other cholinergic compounds might have disease-modifying properties.
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