Abstract

The exact mechanism and progression of Alzheimer's disease (AD) at present is not fully understood. In patients suffering from AD, damage to the hippocampal region and impairment of learning and memory is present. It is also known that a buildup of β-amyloid plaques occur in AD patients and that β-amyloid interacts with some subtypes of neuronal nicotinic acetylcholine receptors (neuronal nAChRs). These receptors are composed of five subunits. The most prevalent nAChR subunit composition through the brain as a whole is α7. Previous data produced from our lab suggests that α7 nAChRs are also one of the most prevalent subunits expressed by interneurons within the hippocampal region, a part of the brain known to be involved in memory and learning. It is hypothesized that one mechanism through which learning and memory becomes impaired in AD is through the interaction of β-amyloid with these nAChRs. It has previously been established that nanomolar amounts of β-amyloid inhibit the peak currents of α7 nAChRs. However, concentrations of β-amyloid in the picomolar range, in some studies show an activation of α7 nAChRs, while other studies no activation is seen. In this experiment we show that human α7 subunit nAChRs are not activated by β-amyloid42 at 1 pM- 30 nM concentrations. We also show that short, seven-second applications of β-amyloid interact with the α7 nAChRs to alter the kinetics of the channel, however, the exact mechanism and pattern by which it effects the channel is still unclear.

Degree

College and Department

Life Sciences; Physiology and Developmental Biology

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