Affiliations: Unitat d'Histologia i Neurobiologia (UHN), Facultat de Medicina i Ciències de la Salut, Universitat Rovira i Virgili, Reus, Spain
Correspondence:
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Corresponding author: Dr. Manel M. Santafé, Unitat d'Histologia i Neurobiologia (UHN), Facultat de Medicina i Ciències de la Salut, Universitat Rovira i Virgili, carrer St Lloren\c{c} num 21, 43201-Reus, Spain. Tel.: +54 11 977 759351; Fax: +54 11 977 759322; E-mail: msm@fmcs.urv.es.
Note: [1] These authors contributed equally to this work.
Abstract: Using intracellular recording of the diaphragm muscle of adult rats, we have investigated the short-term functional effects of amyloid-β (Aβ)25-35 peptide aggregates on the modulation of acetylcholine (ACh) release and the involvement of protein kinase C (PKC). The non-aggregated form of this peptide does not change the evoked and spontaneous transmitter release parameters on the neuromuscular synapse. However, the aggregated form of Aβ25-35 acutely interferes with evoked quantal ACh release (∼40% reduction) when synaptic activity in the ex vivo neuromuscular preparation is maintained by low frequency (1 Hz) electrical stimulation. This effect is partially dependent on the activity of PKC that may have a permissive action. The end result of Aβ25-35 is in opposition to the PKC-dependent maintenance effect on ACh release manifested in active synapses.
Keywords: Acetylcholine release, amyloid-β, amyloid-β protein precursor, motor nerve terminals, protein kinase C
