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

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

Journal Name: Protein & Peptide Letters

Volume 19 , Issue 2 , 2012

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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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Article Details

VOLUME: 19
ISSUE: 2
Year: 2012
Page: [165 - 172]
Pages: 8
DOI: 10.2174/092986612799080149
Price: $65

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