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A peptide derived from the C-terminal region of acetylcholinesterase modulates extracellular concentrations of acetylcholinesterase in the rat substantia nigra.

Abstract:

It is well established that acetylcholinesterase (AChE) has 'non-classical' functions independent of cholinergic transmission. A region of AChE distinct from the catalytic site may be responsible for these actions via a 14-residue peptide located between residues 586-599 at the C-terminus of human AChE. This AChE-peptide possesses a high amino acid sequence homology with a region of amyloid precursor protein and shares many biophysical and physiological characteristics. In this study, the eff...

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Publication status:
Published

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Institution:
University of Oxford
Division:
MSD
Department:
Pharmacology
Role:
Author
Journal:
Neuroscience letters More from this journal
Volume:
358
Issue:
3
Pages:
210-214
Publication date:
2004-04-01
DOI:
EISSN:
1872-7972
ISSN:
0304-3940

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