The significance of blood cholinesterase activity measurements

Gage, J. C.

doi:10.1007/978-1-4615-8422-3_5

Cited by 27 publications

(19 citation statements)

References 13 publications

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“…Limperos Although there is generally good agreement in the literature as to the magnitude of interindividual RBC-ChE variation, the extent of intraindividual RBC-ChE variability remains controversial. Reports in the literature can be found showing that within a given individual RBC-ChE activities increase (7 ), decrease (8,9 ), and remain the same over time (4, 5, 10 -15 ). Detailed knowledge of this physiological variable is important clinically because the frequency of RBC-ChE monitoring should be linked to the enzyme's physiological variation or lack thereof.…”

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confidence: 99%

Intraindividual Stability of Human Erythrocyte Cholinesterase Activity

et al. 2007

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Background: Erythrocyte cholinesterase (RBC-ChE) activities serve as useful and sensitive biomarkers to monitor exposure to cholinesterase-inhibiting substances, such as chemical warfare nerve agents and pesticides. Although the interindividual variation of RBC-ChE is well characterized, the magnitude of intraindividual variation for RBC-ChE remains controversial. An accurate measure of intraindividual variation is critical for establishing the appropriate frequency of RBC-ChE testing. Methods: We retrospectively tracked the intraindividual variation of RBC-ChE activities among 46 male nerve agent workers from a single US Army depot that participated in a medical surveillance program requiring periodic RBC-ChE monitoring. All RBC-ChE analysis was performed by the same medical laboratory technician by the delta pH method. Results: A mean of 38 and a median of 37 RBC-ChE measurements were available for each worker. The mean duration of employment for these workers was 20 years (median, 21 years). The mean CV for RBC-ChE in this set of 46 workers was 3.9%. Linear regression analysis of the data for each worker resulted in a mean slope of 0.0010 delta pH units/h per year. Conclusions: RBC-ChE activities increased in each person by a mean of 0.01 delta pH units/h every 10 years, which is a negligible rate. These findings highlight the

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Intraindividual Stability of Human Erythrocyte Cholinesterase Activity

et al. 2007

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“…Moreover, atmospheric analysis does not take into consideration absorption by other routes such as the skin, a real hazard among those who mix and apply pesticides. Cholinesterase assays have to some extent ensured that prescribed safety precautions during manufacture and application have been implemented [23]. Clear correlations between succinylcholine apnoea and butyrylcholinesterase assays are established and have been found to be very useful in the diagnosis of prolonged response to drugs used during anaesthesia.…”

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Cholinesterase estimations revisited: the clinical relevance

Karalliedde

2002

EJA

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“…BuChE is also used to monitor persons exposed to organophosphorus (OP) inhibitors (Gage, 1967;Hayes, 1983). BuChE is generally more sensitive to OP inhibitors compared to red blood cell AChE (Carter and Maddux, 1974;Grob, 1950;Grob and Harvey, 1949;Grob et al, 1950;Rider et al, 1969).…”

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Inhibition of Human Plasma and Serum Butyrylcholinesterase (EC 3.1.1.8) by α-Chaconine and α-Solanine

et al. 1996

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The purpose of these experiments was to determine the reversibility of a-chaconine and a-solanine inhibition of human plasma butyrylcholinesterase (BuChE). For the substrate a-naphthylacetate, optimal assay conditions were 0.50 M sodium phosphate buffer and a substrate concentration of 3-5 X 10~4 M. Dibucaine (1 X 10~5 M) indicated the usual phenotype for all subjects; achaconine and a-solanine at 2.88 X 10~6 M inhibited BuChE about 70 and 50%, respectively. One-and 24-hr incubations at 1 X 10~! M with a-chaconine, a-solanine, paraoxon, eserine, and ethanol yielded reversible inhibition with dilution except for paraoxon. Twenty-four-hour dialyses of incubations showed no inhibition except for paraoxon. PAGE enzyme activity gels of 1-and 24-hr incubations also showed no inhibition except for paraoxon. aChaconine and a-solanine are reversible inhibitors of human butyrylcholinesterase. At estimated tissue levels, a-chaconine, a-solanine, and solanidine inhibited BuChE 10-86%. In assays which combined a-chaconine, a-solanine, and solanidine, inhibition of BuChE was less than additive. No inhibition of albumin a-naphthylacetate esterase (an arylesterase) was noted with any inhibitor. The importance of these data to adverse toxicological effects of potato alkaloids is diSCUSSed. C 1996 SodMy of Toxicology.Potatoes, consumed by humans for at least 2000 years (Spoerke, 1994;Ugent, 1970), contain the steroidal alkaloids, a-chaconine, a-solanine, and solanidine. The toxicology of these known butyryl-and acetylcholinesterase inhibitors (Harris and Whittaker, 1962;Orgell, 1963) has been reviewed

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The significance of blood cholinesterase activity measurements

Cited by 27 publications

References 13 publications

Intraindividual Stability of Human Erythrocyte Cholinesterase Activity

Intraindividual Stability of Human Erythrocyte Cholinesterase Activity

Cholinesterase estimations revisited: the clinical relevance

Inhibition of Human Plasma and Serum Butyrylcholinesterase (EC 3.1.1.8) by α-Chaconine and α-Solanine

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