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Alzheimer's disease (AD) is a neurodegenerative disease, one of whose major pathological hallmarks is the accumulation of amyloid plaques comprised of aggregated   β  -amyloid (A  β  ) peptides. It is now recognized that soluble A  β   oligomers may lead to synaptic dysfunctions early in AD pathology preceding plaque deposition. A  β   is produced by a sequential cleavage of amyloid precursor protein (APP) by the activity of   β  - and   γ  -secretases, which have been identified as major candidate therapeutic targets of AD. This paper focuses on how A  β   alters synaptic function and the functional consequences of inhibiting the activity of the two secretases responsible for A  β   generation. Abnormalities in synaptic function resulting from the absence or inhibition of the A  β  -producing enzymes suggest that A  β   itself may have normal physiological functions which are disrupted by abnormal accumulation of A  β   during AD pathology. This interpretation suggests that AD therapeutics targeting the   β  - and   γ  -secretases should be developed to restore normal levels of A  β   or combined with measures to circumvent the associated synaptic dysfunction(s) in order to have minimal impact on normal synaptic function.

Consequences of Inhibiting Amyloid Precursor Protein Processing Enzymes on Synaptic Function and Plasticity