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• W2322609186 abstract "Alzheimer's disease is associated with the accumulation within the brain of amyloid-β (Aβ) peptides that damage synapses and affect memory. Our recent study examined Alzheimer’s-related neurodegeneration by incubating cultured neurons with Aβ and measuring synaptic density. We showed that glimepiride, a sulphonylurea used for the treatment of diabetes, protected neurons against Aβ-induced synapse damage by changing the responsiveness of neurons to Aβ. Although glimepiride-treated neurons bound similar amounts of Aβto control neurons less Aβaccumulated within lipid rafts. More specifically, glimepiride reduced the Aβ-inducedactivation of cytoplasmic phospholipase A 2 (cPLA 2 ), aberrant activation of which causes synapse damage. Glimepiride also reduced the Aβ-induced increase in cholesterol that was required for the activation of cPLA 2 suggesting that drug-induced modifications of membrane micro-environments alter the Aβ-induced signalling pathways that lead to synapse damage. Therapeutic strategies in Alzheimer’s disease often include neutralising toxic forms of Aβ. Although several monoclonal antibodies (mAbs) targeting Aβ are currently in clinical trials, there remain concerns over their side effects, their ability to cross the blood brain barrier and their effectiveness. Here we offer an alternative mechanism for neutralising Aβ. Glimepiride caused the release of soluble cellular prion proteins (PrP C ), a receptor for toxic forms of Aβ. The soluble PrP C bound to and neutralised Aβ thus preventing synapse damage. Such observations raise the possibility that glimepiride could induce soluble PrP C within the brain that will neutralise toxic Aβ, reduce synapse damage and hence delay the progression of cognitive decline in Alzheimer’s disease." @default.
• W2322609186 created "2016-06-24" @default.
• W2322609186 creator A5060254479 @default.
• W2322609186 date "2016-03-01" @default.
• W2322609186 modified "2023-09-27" @default.
• W2322609186 title "Does glimepiride provide a novel mechanism of neutralising toxic amyloid-β?" @default.
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• W2322609186 doi "https://doi.org/10.14800/nc.1197" @default.
• W2322609186 hasPublicationYear "2016" @default.
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