Amyloid beta-peptide inhibits high-affinity choline uptake and acetylcholine release in rat hippocampal slices

J Neurochem. 1998 May;70(5):2179-87. doi: 10.1046/j.1471-4159.1998.70052179.x.

Abstract

The characteristic pathological features of the postmortem brain of Alzheimer's disease (AD) patients include, among other features, the presence of neuritic plaques composed of amyloid beta-peptide (A beta) and the loss of basal forebrain cholinergic neurons, which innervate the hippocampus and the cortex. Studies of the pathological changes that characterize AD and several other lines of evidence indicate that A beta accumulation in vivo may initiate and/or contribute to the process of neurodegeneration and thereby the development of AD. However, the mechanisms by which A beta peptide influences/causes degeneration of the basal forebrain cholinergic neurons and/or the cognitive impairment characteristic of AD remain obscure. Using in vitro slice preparations, we have recently reported that A beta-related peptides, under acute conditions, potently inhibit K+-evoked endogenous acetylcholine (ACh) release from hippocampus and cortex but not from striatum. In the present study, we have further characterized A beta-mediated inhibition of ACh release and also measured the effects of these peptides on choline acetyltransferase (ChAT) activity and high-affinity choline uptake (HACU) in hippocampal, cortical, and striatal regions of the rat brain. A beta(1-40) (10(-8) M) potently inhibited veratridine-evoked endogenous ACh release from rat hippocampal slices and also decreased the K+-evoked release potentiated by the nitric oxide-generating agent, sodium nitroprusside (SNP). It is interesting that the endogenous cyclic GMP level induced by SNP was found to be unaltered in the presence of A beta(1-40). The activity of the enzyme ChAT was not altered by A beta peptides in hippocampus, cortex, or striatum. HACU was reduced significantly by various A beta peptides (10(-14) to 10(-6) M) in hippocampal and cortical synaptosomes. However, the uptake of choline by striatal synaptosomes was altered only at high concentration of A beta (10(-6) M). Taken together, these results indicate that A beta peptides, under acute conditions, can decrease endogenous ACh release and the uptake of choline but exhibit no effect on ChAT activity. In addition, the evidence that A beta peptides target primarily the hippocampus and cortex provides a potential mechanistic framework suggesting that the preferential vulnerability of basal forebrain cholinergic neurons and their projections in AD could relate, at least in part, to their sensitivity to A beta peptides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholine / metabolism*
  • Amyloid beta-Peptides / pharmacology*
  • Animals
  • Binding, Competitive / drug effects
  • Choline / antagonists & inhibitors*
  • Choline / pharmacokinetics
  • Choline O-Acetyltransferase / metabolism
  • Cyclic GMP / metabolism
  • Hippocampus / metabolism*
  • In Vitro Techniques
  • Male
  • Nitroprusside / pharmacology
  • Peptide Fragments / pharmacology
  • Rats
  • Rats, Sprague-Dawley

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • Nitroprusside
  • Choline O-Acetyltransferase
  • Cyclic GMP
  • Choline
  • Acetylcholine