Synaptic TransmissionBlock of LTP in rat hippocampus in vivo by β-amyloid precursor protein fragmentsCullen, William K.1; Suh, Yoo-Hun2; Anwyl, Roger3; Rowan, Michael J.1,4Author Information 1Departments of Pharmacology and Therapeutics, Trinity College, Dublin 2, Ireland 2Department of Pharmacology, Seoul National University, College of Medicine, 28 Yongon-dong, Chongo Gu, Seoul 110-799, Korea 3Departments of Physiology, Trinity College, Dublin 2, Ireland 4Corresponding Author: Michael J. Rowan ACKNOWLEDGEMENTS: Supported by the Health Research Board of Ireland, the Wellcome Trust and the European Commission. We thank S-H Kim for synthesizing CT-105 and Dr Charles Large for the gift of Aβ 1–42. Website publication 24 September 1997 Received 8 July 1997; accepted 5 August 1997 NeuroReport: October 20th, 1997 - Volume 8 - Issue 15 - p 3213-3217 Buy Abstract THE effects of β-amyloid precursor protein (β-APP) fragments on plasticity of glutamtatergic synaptic transmission were examined in the hippocampus of urethane anaesthetized rats. I.c.v. injection of β-amyloid (Aβ) 1–40 and 1–42 and the C-terminal fragment CT105 greatly shortened the duration of high frequency stimulation-induced long-term potentiation (LTP) of field excitatory postsynaptic potentials in the CA1 area. Whereas in vehicle injected animals LTP was stable over a 5 h recording period, doses of these peptides (Aβ1–40, 0.4 and 3.5 nmol; Aβ1–42, 0.01 nmol; CT105, 0.05 nmol) which did not affect baseline synaptic transmission abolished LTP within 3–5 h. The reduced duration of this form of synaptic plasticity may contribute to the cognitive deficits in Alzheimer's disease. © Lippincott-Raven Publishers.