Proline‐Rich Chaperones Are Compared Computationally and Experimentally for Their Abilities to Facilitate Recombinant Butyrylcholinesterase Tetramerization in CHO Cells

Proline‐Rich Chaperones Are Compared Computationally and Experimentally for Their Abilities to... IntroductionButyrylcholinesterase (BChE) is a serine hydrolase, which can hydrolyze cocaine, heroin, aspirin, bambuterol, and succinylcholine and can also scavenge various organophosphorus pesticides and chemical warfare agents, making it an organophosphorus bioscavenger. Organophosphorus agents are acutely neurotoxic because they can inhibit acetylcholinesterase (AChE), which is essential for the control of transmitter acetylcholine (ACh) of nervous impulses. Inhibition of AChE results in excessive ACh accumulation at synapses, leading to overstimulation that can cause headaches, insomnia, muscle twitches and even convulsions, coma, or respiratory failure depending on the organophosphorus agent type and the dosage. Although BChE's exact physiological role is unclear, its substrate and inhibitor selectivity are similar to the AChE. As a result, BChE can scavenge and further act to counter administered or inhaled poisons that target AChE and other physiological targets in mammals.The BChE enzyme isolated from human plasma is a tetrameric glycoprotein with each subunit comprising 574 residues (MW: 85 kDa per subunit) and nine N‐linked carbohydrates with no indication of O‐linked carbohydrates. Pharmacokinetic properties of expressed recombinant BChE have been observed to be affected by a number of factors including the size of the recombinant protein and its glycosylation characteristics, including sialic acid content. Especially important to the pharmacokinetic http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biotechnology Journal Wiley

Proline‐Rich Chaperones Are Compared Computationally and Experimentally for Their Abilities to Facilitate Recombinant Butyrylcholinesterase Tetramerization in CHO Cells

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Publisher
Wiley Subscription Services, Inc., A Wiley Company
Copyright
© 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
ISSN
1860-6768
eISSN
1860-7314
D.O.I.
10.1002/biot.201700479
Publisher site
See Article on Publisher Site

Abstract

IntroductionButyrylcholinesterase (BChE) is a serine hydrolase, which can hydrolyze cocaine, heroin, aspirin, bambuterol, and succinylcholine and can also scavenge various organophosphorus pesticides and chemical warfare agents, making it an organophosphorus bioscavenger. Organophosphorus agents are acutely neurotoxic because they can inhibit acetylcholinesterase (AChE), which is essential for the control of transmitter acetylcholine (ACh) of nervous impulses. Inhibition of AChE results in excessive ACh accumulation at synapses, leading to overstimulation that can cause headaches, insomnia, muscle twitches and even convulsions, coma, or respiratory failure depending on the organophosphorus agent type and the dosage. Although BChE's exact physiological role is unclear, its substrate and inhibitor selectivity are similar to the AChE. As a result, BChE can scavenge and further act to counter administered or inhaled poisons that target AChE and other physiological targets in mammals.The BChE enzyme isolated from human plasma is a tetrameric glycoprotein with each subunit comprising 574 residues (MW: 85 kDa per subunit) and nine N‐linked carbohydrates with no indication of O‐linked carbohydrates. Pharmacokinetic properties of expressed recombinant BChE have been observed to be affected by a number of factors including the size of the recombinant protein and its glycosylation characteristics, including sialic acid content. Especially important to the pharmacokinetic

Journal

Biotechnology JournalWiley

Published: Jan 1, 2018

Keywords: ; ; ; ;

References

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