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

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

Volume: 19 Issue: 2

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

Affiliation:

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

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.

Cite this article as:

C. Halliday Amy and A. Greenfield Susan, From Protein to Peptides: a Spectrum of Non-Hydrolytic Functions of Acetylcholinesterase, Protein & Peptide Letters 2012; 19 (2) . https://dx.doi.org/10.2174/092986612799080149

DOI https://dx.doi.org/10.2174/092986612799080149	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305