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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

From Protein to Peptides: a Spectrum of Non-Hydrolytic Functions of Acetylcholinesterase

Author(s): Amy C. Halliday and Susan A. Greenfield

Volume 19, Issue 2, 2012

Page: [165 - 172] Pages: 8

DOI: 10.2174/092986612799080149

Price: $65

Abstract

Acetylcholinesterase (AChE), a member of the α/β-hydrolase fold superfamily of proteins, is a serine hydrolase responsible for the hydrolysis of the well studied neurotransmitter acetylcholine (ACh). However, it is becoming clear that AChE has a range of actions other than this ‘classical’ role. Non-classical AChE functions have been identified in apoptosis, stress-responses, neuritogenesis, and neurodegeneration. Furthermore, these non-classical roles are attributable not only to the native protein, which appears to act as a mediary binding protein under a number of circumstances, but also to peptides cleaved from the parent protein. Peptides cleaved from AChE can act as independent signalling molecules. Here we discuss the implications of non-hydrolytic functions of this multi-tasking protein.

Keywords: Acetylcholinesterase, adhesion, apoptosis, neurogenesis, non-hydrolytic function, signalling peptide, synaptic, exons, Tetramers, 3D X-ray structure, glycophosphatidylinositol (GPI)


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