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

Journal article

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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Authors: Emmett, SR; Greenfield, S

• Publication status: Published
• Journal: Neuroscience letters
• Volume: 358
• Issue: 3
• Pages: 210-214
• Publication date: 2004-04-01
• DOI: 10.1016/j.neulet.2003.12.078
• EISSN: 1872-7972
• ISSN: 0304-3940
• Language: English
• Keywords: Drug Interactions; Acetylcholine; Molecular Sequence Data; Acetylcholinesterase; Calcium Signaling; N-Methylaspartate; Rats; Extracellular Fluid; Rats, Wistar; Protein Structure, Tertiary; Parkinson Disease; Male; Disease Models, Animal; Substantia Nigra; Neurons; Amino Acid Sequence; Amyloid beta-Protein Precursor; Animals; Peptide Fragments