Increased plasma cholinesterase activity and succinylcholine resistance: a genetic variant.

Neitlich, Harvey W.

doi:10.1172/jci105353

Cited by 104 publications

(27 citation statements)

References 22 publications

(16 reference statements)

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“…Furthermore, a 22-fold elevation in the suxamethonium hydrolysing capacity of the blood of cats reduced the effectiveness of suxamethonium only 16-fold. These findings are contrary to observations in man (Kalow & Gunn, 1957;Neitlich, 1966) and strongly indicate that in rats and cats hydrolysis of suxamethonium in blood plays very little or no part in determining the concentration of the ester reaching the motor end plate and its subsequent metabolic degradation. The reason for the difference between man and the laboratory animals used is at least two-fold.…”

Section: Discussioncontrasting

confidence: 77%

The relationship between the level of cholinesterase in plasma and the action of suxamethonium in animals

Hobbiger

Peck

1970

British J Pharmacology

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Summary1. The neuromuscular blocking action of suxamethonium, given by intravenous injection, and the effect upon it of iso-OMPA (tetraisopropyl pyrophosphoramide) in doses which produced marked selective inhibition of cholinesterase in blood were studied in anaesthetized rats and cats, and in mice. 2. In cats experiments were also carried out in which suxamethonium was given by intravenous infusion until an effect which remained constant with time was achieved. From the degree of neuromuscular block (under equilibrium conditions) obtained with different infusion rates the infusion rate for 50% reduction in twitch tension of the indirectly stimulated soleus and gastrocnemius muscles (IR50) was calculated. The effect on it of raising the suxamethonium hydrolysing capacity of blood and of selectively reducing the level of cholinesterase in blood by various doses of iso-OMPA was then investigated. 3. At relevant stages of each experiment cholinesterase activity in blood was determined with butyrylcholine or benzoylcholine and where appropriate with suxamethonium as substrate. 4. The results obtained show that in rats and cats the effectiveness of suxamethonium is unrelated to the level of cholinesterase activity in blood and that raising the suxamethonium hydrolysing capacity in the blood up to 22-fold (in cats) only reduces the IR50 by a factor of 1-6. 5. The enhancement of the effectiveness of suxamethonium in the three species (2-to 3-fold in rats, 2-to 4-fold in mice and 7-to 8-fold in cats under the conditions used for comparison) which follows the administration of iso-OMPA is attributable to inhibition of cholinesterase in the tissues. 6. It is concluded that the results obtained clearly indicate that the species studied do not give information as regards suxamethonium and its metabolism which is applicable to man.

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Section: Discussioncontrasting

confidence: 77%

The relationship between the level of cholinesterase in plasma and the action of suxamethonium in animals

Hobbiger

Peck

1970

British J Pharmacology

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“…(1983), Kalow and Genest (1957), Kalow and Gunn (1959), Kalow and Staron (1957), Krause eta!. (1988), Neitlich ( 1966), Rubinstein eta!. ( 1970), and Yoshida and Motu!…”

Section: The Cholinesterasesunclassified

Blood Cholinesterases as Human Biomarkers of Organophosphorus Pesticide Exposure

Nigg

Knaak

2000

Reviews of Environmental Contamination and Toxicology

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“…E,s exists in several forms (Rubinstein et al, 1970) and results in 95 to 100% diminution of E u molecules; E,J results in about 66% reduction. One family has been described in which several members have greatly increased amounts of apparently normal serum cholinesterase (Neitlich, 1966;Yoshida and Motulsky, 1969). The gene responsible has been named E Cynthiana but it is not yet known if it is active at cholinesterase locus 1 or locus 2.…”

mentioning

confidence: 99%

E1k, another quantitative variant at cholinesterase locus 1.

Rubinstein¹,

Dietz²,

Lubrano³

1978

Journal of Medical Genetics

112

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Interaction with E,a led to the discovery of the E,s (Liddell et al., 1962) and Eli variants. E,s exists in several forms (Rubinstein et al., 1970) and results in 95 to 100% diminution of E u molecules; E,J results in about 66% reduction. One family has been described in which several members have greatly increased amounts of apparently normal serum cholinesterase (Neitlich, 1966;Yoshida and Motulsky, 1969). The gene responsible has been named E Cynthiana but it is not yet known if it is active at cholinesterase locus 1 or locus 2.We present here two families with a quantitative variant at cholinesterase locus 1 which results in about 33% reduction of E,u molecules; both of these families were recognised by means of interaction with the E, a gene. MethodsThe enzymatic and immunological methods used were the same as given in earlier publications Rubinstein et al., 1976;Dietz et al., 1973). (Table II

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Increased plasma cholinesterase activity and succinylcholine resistance: a genetic variant.

Cited by 104 publications

References 22 publications

The relationship between the level of cholinesterase in plasma and the action of suxamethonium in animals

The relationship between the level of cholinesterase in plasma and the action of suxamethonium in animals

Blood Cholinesterases as Human Biomarkers of Organophosphorus Pesticide Exposure

E1k, another quantitative variant at cholinesterase locus 1.

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