Association between life-threatening cocaine toxicity and plasma cholinesterase activity

Hoffman, Robert S.; Henry, Gillian; Howland, Mary Ann; Weisman, Richard; Weil, Lawrence; Goldfrank, Lewis R.

doi:10.1016/s0196-0644(05)80883-2

Cited by 72 publications

(28 citation statements)

References 17 publications

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“…Compared with cocaine and other metabolites, like norcocaine and benzylecgonine, these detoxified products have little biologic activity (Misra et al, 1975;Madden and Powers, 1990). A report that deficient plasma BChE activity increased the risk of toxicity after cocaine exposure (Hoffman et al, 1992) led to tests of BChE for prophylaxis.…”

Section: Discussion Previous Development Of Cocaine Hydrolases and Bimentioning

confidence: 99%

A Cocaine Hydrolase Engineered from Human Butyrylcholinesterase Selectively Blocks Cocaine Toxicity and Reinstatement of Drug Seeking in Rats

Brimijoin

Gao

Anker

et al. 2008

Neuropsychopharmacol

125

167

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Successive rational mutations of human butyrylcholinesterase (BChE) followed by fusion to human serum albumin have yielded an efficient hydrolase that offers realistic options for therapy of cocaine overdose and abuse. This albumin-BChE prevented seizures in rats given a normally lethal cocaine injection (100 mg/kg, i.p.), lowered brain cocaine levels even when administered after the drug, and provided rescue after convulsions commenced. Moreover, it selectively blocked cocaine-induced reinstatement of drug seeking in rats that had previously self-administered cocaine. The enzyme treatment was well tolerated and may be worth exploring for clinical application in humans.

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Section: Discussion Previous Development Of Cocaine Hydrolases and Bimentioning

confidence: 99%

A Cocaine Hydrolase Engineered from Human Butyrylcholinesterase Selectively Blocks Cocaine Toxicity and Reinstatement of Drug Seeking in Rats

Brimijoin

Gao

Anker

et al. 2008

Neuropsychopharmacol

125

167

View full text Add to dashboard Cite

show abstract

“…One study showed that plasma from individuals homozygous for the usual enzyme (UU) had ϳ40% cocaine remaining in plasma after 2-h incubation, compared with 70 and 94% in those heterozygous or homozygous for the atypical enzyme, respectively (Jatlow et al, 1979). Illicit cocaine users with severe toxicity were found to have 15 to 25% lower mean BChE activity compared with nonusers or users without complications (Devenyi, 1989;Hoffman et al, 1992;Om et al, 1993). Addicts have deliberately inhibited BChE with organophosphate pesticides in an attempt to prolong the cocaine "high" (Herschman and Aaron, 1991).…”

Section: Cocainementioning

confidence: 99%

Pharmacogenetics, Drug-Metabolizing Enzymes, and Clinical Practice

2006

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“…Several studies have shown that administration of plasma cholinesterase is protective in animal models of acute cocaine toxicity. In a multivariate model, plasma cholinesterase activity was correlated with severe cocaine toxicity in ED patients [50]. There are several phenotypes of human butylcholinesterase, and these may vary in their affinity for cocaine [51].…”

Section: Cocaine-protein Bindingmentioning

confidence: 99%

Mechanisms of Acute Cocaine Toxicity

Heard¹,

Palmer²,

Zahniser³

2008

TOPHARMJ

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Abstract:Patients with acute cocaine poisoning present with life-threatening symptoms involving several organ systems. While the effects of cocaine are myriad, they are the result of a limited number of cocaine-protein interactions, including monoamine transporter, neurotransmitter receptor and voltage-gated ion channels. These primary interactions trigger a cascade of events that ultimately produce the clinical effects. The purpose of this article is to review the primary interactions of cocaine and the effects that these interactions trigger. We also describe the progression of symptoms observed in cocaine poisoning as they relate to serum cocaine concentrations.

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Association between life-threatening cocaine toxicity and plasma cholinesterase activity

Cited by 72 publications

References 17 publications

A Cocaine Hydrolase Engineered from Human Butyrylcholinesterase Selectively Blocks Cocaine Toxicity and Reinstatement of Drug Seeking in Rats

A Cocaine Hydrolase Engineered from Human Butyrylcholinesterase Selectively Blocks Cocaine Toxicity and Reinstatement of Drug Seeking in Rats

Pharmacogenetics, Drug-Metabolizing Enzymes, and Clinical Practice

Mechanisms of Acute Cocaine Toxicity

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