Plasma cholinesterase activity in patients during therapy with dexamethasone or prednisone

Bradamante, Vlasta; Kunec-Vajić, E.; Lisić, Miroslav; Dobrić, Ivan; Beus, I

doi:10.1007/bf00558156

Cited by 9 publications

(2 citation statements)

References 22 publications

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“…Analysts should, however, be aware of in vivo interferences, notably that of toxic inhibition either from the presence of anticholinesterase medications or the presence of OP insecticides. As with all analyses, the possible presence of drug interference should be considered; there is, for example, at least one report of arti¢cially low activity seen in patients on long-term steroid therapy 38 and we have seen interference in the benzoylcholine assay due to antibiotics with a high absorbance in the UV region. Readers are referred to suitable texts such as Young 39 for reviews of drug interferences.…”

Section: Assay Interferencementioning

confidence: 99%

Cholinesterase: phenotyping and genotyping

Goodall

2004

Ann Clin Biochem

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The plasma enzyme butyrylcholinesterase (BChE) is of clinical interest because of the occurrence of genetic variants with decreased ability to hydrolyse, and therefore inactivate, muscle-relaxant drugs such as suxamethonium. Analysis of BChE involves the determination of both enzyme activity and biochemical phenotypes which are used to determine the risk of so-called 'scoline apnoea'. Problems in analysis arise from both the lack of a universally accepted reference method and the variety of substrates and conditions employed for the determination of activity and phenotypes. Phenotype is determined by the use of speci c enzyme inhibitors that produce phenotype-speci c patterns of 'inhibitor numbers'. DNA analysis is now possible, and true genotypes can be obtained. The nomenclature in use for cholinesterase studies can cause problems in interpretation and reporting as there is poor understanding of the difference between phenotype and genotype, and terms are often, inappropriately, transposed. Techniques for both biochemical and molecular analysis of the enzyme are discussed.

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Section: Assay Interferencementioning

confidence: 99%

Cholinesterase: phenotyping and genotyping

Goodall

2004

Ann Clin Biochem

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“…Different drugs may either decrease or increase the activity of BuChE and AChE. Inhibition of plasma BuChE in rats and humans may be caused by organophosphorus herbicides such as glyphosate (8), reversible cholinesterase inhibitors (9), glucocorticoids (10,11), or some beta blockers (12). In humans, low plasma BuChE activity may reduce succinylcholine hydrolysis and prolong respiratory depression (13).…”

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confidence: 99%

Effects of simvastatin and fenofibrate on butyrylcholinesterase activity in the brain, plasma, and liver of normolipidemic and hyperlipidemic rats

Vukšić

Lovrić

Konjevoda

et al. 2019

Archives of Industrial Hygiene and Toxicology

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The study objective was to test the hypothesis that simvastatin and fenofibrate should cause an increase in butyrylcholinesterase (BuChE) activity not only in the plasma and liver but also in the brain of normolipidemic and hyperlipidemic rats. Catalytic enzyme activity was measured using acetylthiocholine (ATCh) and butyrylthiocholine (BTCh) as substrates. Normolipidemic and hyperlipidemic rats were divided in four groups receiving 50 mg/kg of simvastatin a day or 30 mg/kg of fenofibrate a day for three weeks and three control groups receiving saline. Simvastatin and fenofibrate caused an increase in brain BuChE activity in both normo- and hyperlipidemic rats regardless of the substrate. The increase with BTCh as substrate was significant and practically the same in normolipidemic and hyperlipidemic rats after simvastatin treatment (14–17% vs controls). Simvastatin and fenofibrate also increased liver and plasma BuChE activity in both normolipidemic and hyperlipidemic rats regardless of the substrate. In most cases the increase was significant. Considering the important role of BuChE in cholinergic transmission as well as its pharmacological function, it is necessary to continue investigations of the effects of lipid-lowering drugs on BuChE activity.

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A color‐reaction‐based rapid screening for null activity of butyrylcholinesterase: A step toward point‐of‐care screening for succinylcholine apnea

Nagpal

Chowdhary

Bhattacharyya

et al. 2015

Biotech and App Biochem

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Succinylcholine apnea happens in cases of null butyrylcholinesterase activity after administration of preintubation succinylcholine. So far, there is no such popular test that can rapidly screen null butyrylcholinesterase activity from plasma. Development of a novel method for rapid screening of null butyrylcholinesterase activity of plasma samples was the objective of the current work. Dichromate reagent was added to 1-naphthol, 2-naphthol, phenol, and para-nitrophenol in separate aliquots and watched for the color formation. Plasma samples preincubated with and without selective butyrylcholinesterase inhibitor were mixed with 1-naphthylacetate and watched for color development after addition of dichromate reagent. Fitting of 1-naphthylacetate at the active site of butyrylcholinesterase was analyzed by using tools of computational biology. It was seen that 1-naphthol formed color with dichromate reagent in a concentration-dependent manner. Other phenols did not form color with dichromate reagent even at 500-µm concentrations. Plasma sample with and without selective butyrylcholinesterase inhibitor (tetra isopropyl pyrophosphoramide) was distinguishable by color formation when incubated with 1-naphthylacetate, followed by the addition of dichromate reagent. In silico analysis also showed that 1-naphthylacetate fitted well at the active site of butyrylcholinesterase. The developed method may be used for rapid screening for null butyrylcholinesterase activity at point of care.

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Plasma cholinesterase activity in patients during therapy with dexamethasone or prednisone

Cited by 9 publications

References 22 publications

Cholinesterase: phenotyping and genotyping

Cholinesterase: phenotyping and genotyping

Effects of simvastatin and fenofibrate on butyrylcholinesterase activity in the brain, plasma, and liver of normolipidemic and hyperlipidemic rats

A color‐reaction‐based rapid screening for null activity of butyrylcholinesterase: A step toward point‐of‐care screening for succinylcholine apnea

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