Abstract
We used acetylcholine and butyrylcholine to competitively inhibit the cleavage of acetylthiocholine or butyrylthiocholine in plaques and tangles of Alzheimer's disease. Butyrylcholine was much more effective than acetylcholine in reducing the histochemical reaction for acetylcholinesterase not only in neuronal fibers, but also in plaques and tangles. This is in keeping with biochemical data on acetylcholinesterase and supports the existence of true acetylcholinesterase activity within plaques and tangles. However, 2-4 times higher acetylcholine and buturylcholine concentrations were necessary to inhibit the plaque and tangle bound enzyme. Together with the previously reported different pH optima, this suggests that the plaque- and tangle-bound acetylcholinesterase may represent an altered form of this enzyme.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 56-61 |
| Number of pages | 6 |
| Journal | Neuroscience Letters |
| Volume | 117 |
| Issue number | 1-2 |
| DOIs | |
| State | Published - Sep 4 1990 |
Funding
We would like to thank Kristin Loud and Annmarie Dineen for expert technical assistance. We are grateful to Drs. Bruce Price and James Morris for providing brain tissue. This work was partly supported by NRSA award (AG 05455), an Alzheimer's Disease Research Center Grant (AG 05134), Javits Neuroscience Investigator Award (NS 20285) and the Alzheimer's Disease and Related Disorders Association; Ch.R.S. holds a grant from the Deutsche Forschungsgemeinschaft (DFG).
Keywords
- Alzheimer's disease
- Cholinesterase histochemistry
- Competitive substrate inhibition
- Plaque
- Tangle
ASJC Scopus subject areas
- General Neuroscience