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Current Protein & Peptide Science

Editor-in-Chief

ISSN (Print): 1389-2037
ISSN (Online): 1875-5550

Review Article

Butyrylcholinesterase: A Multifaceted Pharmacological Target and Tool

Author(s): Zhe Ying Ha, Shintu Mathew and Keng Yoon Yeong*

Volume 21, Issue 1, 2020

Page: [99 - 109] Pages: 11

DOI: 10.2174/1389203720666191107094949

Price: $65

Abstract

Butyrylcholinesterase is a serine hydrolase that catalyzes the hydrolysis of esters in the body. Unlike its sister enzyme acetylcholinesterase, butyrylcholinesterase has a broad substrate scope and lower acetylcholine catalytic efficiency. The difference in tissue distribution and inhibitor sensitivity also points to its involvement external to cholinergic neurotransmission. Initial studies on butyrylcholinesterase showed that the inhibition of the enzyme led to the increment of brain acetylcholine levels. Further gene knockout studies suggested its involvement in the regulation of amyloid-beta, a brain pathogenic protein. Thus, it is an interesting target for neurological disorders such as Alzheimer’s disease. The substrate scope of butyrylcholinesterase was recently found to include cocaine, as well as ghrelin, the “hunger hormone”. These findings led to the development of recombinant butyrylcholinesterase mutants and viral gene therapy to combat cocaine addiction, along with in-depth studies on the significance of butyrylcholinesterase in obesity. It is observed that the pharmacological impact of butyrylcholinesterase increased in tandem with each reported finding. Not only is the enzyme now considered an important pharmacological target, it is also becoming an important tool to study the biological pathways in various diseases. Here, we review and summarize the biochemical properties of butyrylcholinesterase and its roles, as a cholinergic neurotransmitter, in various diseases, particularly neurodegenerative disorders.

Keywords: Butyrylcholinesterase, Alzheimer's disease, Parkinson’s disease, obesity, cocaine addiction, inflammation.

Graphical Abstract
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