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• W2091571160 abstract "Prion diseases are neurodegenerative disorders that are characterized by the presence of the misfolded prion protein (PrP). Neurotoxicity in these diseases may result from prion-induced modulation of ion channel function, changes in neuronal excitability, and consequent disruption of cellular homeostasis. We therefore examined PrP effects on a suite of potassium (K+) conductances that govern excitability of basal forebrain neurons. Our study examined the effects of a PrP fragment [PrP(106–126), 50 nM] on rat neurons using the patch clamp technique. In this paradigm, PrP(106–126) peptide, but not the “scrambled” sequence of PrP(106–126), evoked a reduction of whole-cell outward currents in a voltage range between –30 and +30 mV. Reduction of whole-cell outward currents was significantly attenuated in Ca2+-free external media and also in the presence of iberiotoxin, a blocker of calcium-activated potassium conductance. PrP(106–126) application also evoked a depression of the delayed rectifier (IK) and transient outward (IA) potassium currents. By using single cell RT-PCR, we identified the presence of two neuronal chemical phenotypes, GABAergic and cholinergic, in cells from which we recorded. Furthermore, cholinergic and GABAergic neurons were shown to express Kv4.2 channels. Our data establish that the central region of PrP, defined by the PrP(106–126) peptide used at nanomolar concentrations, induces a reduction of specific K+ channel conductances in basal forebrain neurons. These findings suggest novel links between PrP signalling partners inferred from genetic experiments, K+ channels, and PrP-mediated neurotoxicity. © 2010 Wiley-Liss, Inc." @default.
• W2091571160 created "2016-06-24" @default.
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• W2091571160 date "2010-02-19" @default.
• W2091571160 modified "2023-09-23" @default.
• W2091571160 title "Ionic mechanisms of action of prion protein fragment PrP(106-126) in rat basal forebrain neurons" @default.
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• W2091571160 doi "https://doi.org/10.1002/jnr.22372" @default.
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