Enzymes of Acetylcholine Metabolism

Foldes, Francis F.

doi:10.1007/978-1-4612-6248-0_8

Cited by 15 publications

(7 citation statements)

References 331 publications

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“…BChE breaks down ester type of neuromuscular blocking agents used in anesthesia [4]. It may also play a role in lipid metabolism [5], and may be affected by dietary fat [6].…”

Section: Discussionmentioning

confidence: 99%

Serum butyrylcholinesterase in type 2 diabetes mellitus: a biochemical and bioinformatics approach

Sridhar¹,

Nirmala²,

Apparao

et al. 2005

Lipids Health Dis

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Background: Butyrylcholinesterase is an enzyme that may serve as a marker of metabolic syndrome. We (a) measured its level in persons with diabetes mellitus, (b) constructed a family tree of the enzyme using nucleotide sequences downloaded from NCBI. Butyrylcholinesterase was estimated colorimetrically using a commercially available kit (Randox Lab, UK). Phylogenetic trees were constructed by distance method (Fitch and Margoliash method) and by maximum parsimony method.Results: There was a negative correlation between serum total cholesterol and butyrylcholinesterase (-0.407; p < 0.05) and between serum LDL cholesterol and butyrylcholinesterase (-0.435; p < 0.05). There was no statistically significant correlation among the other biochemical parameters. In the evolutionary tree construction both methods gave similar trees, except for an inversion in the position of Sus scrofa (M62778) and Oryctolagus cuniculus (M62779) between Fitch and Margoliash, and maximum parsimony methods. Conclusion:The level of butyrylcholinesterase enzyme was inversely related to serum cholesterol; dendrogram showed that the structures from evolutionarily close species were placed near each other.

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“…BChE breaks down ester type of neuromuscular blocking agents used in anesthesia [4]. It may also play a role in lipid metabolism [5], and may be affected by dietary fat [6].…”

Section: Discussionmentioning

confidence: 99%

Serum butyrylcholinesterase in type 2 diabetes mellitus: a biochemical and bioinformatics approach

Sridhar¹,

Nirmala²,

Apparao

et al. 2005

Lipids Health Dis

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show abstract

Section: Discussionmentioning

confidence: 99%

“…Acetylcholine is hydrolyzed by plasma butyrylcholinesterase as well as by tissue acetylcholinesterase [ 10]. Methacholine is not hydrolyzed by mammalian plasma butyrylcholinesterase but can be hydrolyzed by tissue acetylcholinesterase at half the rate of acetylcholine [ 10] . Because both acetylcholine and methacholine are hydrolyzed by acetylcholinesterase, their eÚ ects should be in uenced by the existing levels of tissue acetylcholinesterase and should be enhanced by the prior administration of acetylcholinesterase inhibitors such as neostigmine.…”

Section: Discussionmentioning

confidence: 99%

“…Activities of cholinesterases, which catalyze the hydrolysis of acetylcholine and other cholinergic agonists, are genetically controlled in inbred mouse strains [ 9,10] . Acetylcholinesterase is a membrane-bound enzyme localized to sites of action of acetylcholine release, whereas butyrylcholinesterase or pseudocholinesterase is a soluble plasma enzyme.…”

mentioning

confidence: 99%

“…Acetylcholinesterase is a membrane-bound enzyme localized to sites of action of acetylcholine release, whereas butyrylcholinesterase or pseudocholinesterase is a soluble plasma enzyme. Acetylcholinesterase hydrolyzes acetylcholine and other thiocholine esters in tissues, whereas butyrylcholinesterase hydrolyzes choline esters present in plasma [ 10] . Single genes encode the catalytic subunits of acetylcholinesterase [ 11] and butyrylcholinesterase [ 12] in humans.…”

mentioning

confidence: 99%

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CHOLINESTERASE ACTIVITY IS SIMILAR IN C3H/HeJ AND A/J MICE AND DOES NOT ACCOUNT FOR THEIR DIFFERENT BRONCHOCONSTRICTOR RESPONSIVENESS

Bulut

Kleeberger²,

Hirshman³

1999

Experimental Lung Research

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Significant interstrain variation in airway responsiveness to acetylcholine (ACh) exists in inbred mouse strains. We hypothesized that part of the variation may be due to between-strain differences in cholinesterase activity. We asked if administration of neostigmine (an acetylcholinesterase inhibitor) and/or succinylcholine (an agent which competes for and inhibits butyrylcholinesterase) altered ACh responsiveness in hyporesponsive C3H/HeJ and hyperresponsive A/J mouse strains. Airway responses to ACh were measured by the airway pressure time index in the presence and absence of succinylcholine (10 mg/kg) and/or neostigmine (0.7 mg/kg). In addition, acetylcholinesterase and butyrylcholinesterase activity were directly measured. Acetylcholinesterase and butyrylcholinesterase inhibition increased airway responses to acetylcholine in both strains, but did not eliminate or decrease the differences in airway responsiveness to ACh previously seen in the two strains. Cholinesterase activities in the two strains were not significantly different. We conclude that differences in either acetylcholinesterase or butyrylcholinesterase in the A/J or C3H/HeJ mouse strains are unlikely to contribute to the differences in airway responsiveness to exogenously administered cholinergic agonists.

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2014

Intracellular Calcium

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Enzymes of Acetylcholine Metabolism

Cited by 15 publications

References 331 publications

Serum butyrylcholinesterase in type 2 diabetes mellitus: a biochemical and bioinformatics approach

Serum butyrylcholinesterase in type 2 diabetes mellitus: a biochemical and bioinformatics approach

CHOLINESTERASE ACTIVITY IS SIMILAR IN C3H/HeJ AND A/J MICE AND DOES NOT ACCOUNT FOR THEIR DIFFERENT BRONCHOCONSTRICTOR RESPONSIVENESS

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