Field results using cholinesterase reactivation techniques to diagnose acute anticholinesterase poisoning in birds and fish

1993 ◽  
Vol 25 (3) ◽  
pp. 315-321 ◽  
Author(s):  
William Stansley
Keyword(s):  
Cholinesterase Reactivation

Cholinesterase reactivation in organophosphorus poisoned patients depends on the plasma concentrations of the oxime pralidoxime methylsulphate and of the organophosphate

1993 ◽  
Vol 67 (2) ◽  
pp. 79-84 ◽  
Author(s):  
J. L. Willems ◽  
H. C. De Bisschop ◽  
A. G. Verstraete ◽  
C. Declerck ◽  
Y. Christiaens ◽  
...  
Keyword(s):  
Plasma Concentrations ◽  
Cholinesterase Reactivation ◽  
Pralidoxime Methylsulphate

Cholinesterase Reactivation in Vivo with a Novel Bis-Oxime Optimized by Computer-Aided Design

2003 ◽  
Vol 307 (1) ◽  
pp. 190-196 ◽  
Author(s):  
P. I. Hammond ◽  
C. Kern ◽  
F. Hong ◽  
T. M. Kollmeyer ◽  
Y.-P. Pang ◽  
...  
Keyword(s):  
Computer Aided Design ◽  
Computer Aided ◽  
Aided Design ◽  
Cholinesterase Reactivation

Severe fenthion intoxications due to ingestion and inhalation with survival outcome

2002 ◽  
Vol 21 (1) ◽  
pp. 49-54 ◽  
Author(s):  
A M Tsatsakis ◽  
G K Bertsias ◽  
V Liakou ◽  
I N Mammas ◽  
I Stiakakis ◽  
...  
Keyword(s):  
Intensive Care Unit ◽  
Intensive Care ◽  
Psychiatric Patient ◽  
Attempted Suicide ◽  
Survival Outcome ◽  
Blood Levels ◽  
Chemical Agent ◽  
Toxicological Data ◽  
Cholinesterase Reactivation

Two cases of severe fenthion intoxication are presented. The first is a case of a psychiatric patient who attempted suicide with ingestion of the compound, and the second case was of a child exposed to the chemical agent by air spraying. Both patients were treated in the intensive care unit with atropine and pralidoxime and finally survived. Fenthion blood levels on admission were 2.7 and 0.95 μg/mL, respectively. Different concentrations of pralidoxime were added to the first patient's poisoned serum in order to assess in vitro the effect of pralidoxime on cholinesterase reactivation. The clinical and toxicological data of the poisonings are discussed, as well as the potential therapeutic use of pralidoxime in organophosphate intoxication.

CARBOFURAN POISONING IN HERONS: DIAGNOSIS USING CHOLINESTERASE REACTIVATION TECHNIQUES

1995 ◽  
Vol 31 (2) ◽  
pp. 186-192 ◽  
Author(s):  
Katherine A. Hunt ◽  
Michael J. Hooper ◽  
Edward E. Littrell
Keyword(s):  
Cholinesterase Reactivation

scholarly journals Cholinesterase Reactivation: In Vitro Studies

1975 ◽  
Vol 3 (1) ◽  
pp. 60-61 ◽  
Author(s):  
A. Ganendran ◽  
S. Balabaskaran
Keyword(s):  
In Vitro Studies ◽  
Cholinesterase Inhibition ◽  
Clinical Impression ◽  
Organophosphorus Insecticides ◽  
Cholinesterase Reactivation

In vitro studies confirm the clinical impression that P–2–AM does not reverse the cholinesterase inhibition caused by organophosphorus insecticides.

scholarly journals Molecular Modeling Studies on the Multistep Reactivation Process of Organophosphate-Inhibited Acetylcholinesterase and Butyrylcholinesterase

Biomolecules ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 169
Author(s):  
Jakub Jończyk ◽  
Jędrzej Kukułowicz ◽  
Kamil Łątka ◽  
Barbara Malawska ◽  
Young-Sik Jung ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Organophosphorus Compounds ◽  
Covalent Bond ◽  
General Mechanism ◽  
Binding Modes ◽  
Enzyme Active Site ◽  
Reactivation Process ◽  
Serious Injury ◽  
Molecular Aspects ◽  
Cholinesterase Reactivation

Poisoning with organophosphorus compounds used as pesticides or misused as chemical weapons remains a serious threat to human health and life. Their toxic effects result from irreversible blockade of the enzymes acetylcholinesterase and butyrylcholinesterase, which causes overstimulation of the cholinergic system and often leads to serious injury or death. Treatment of organophosphorus poisoning involves, among other strategies, the administration of oxime compounds. Oximes reactivate cholinesterases by breaking the covalent bond between the serine residue from the enzyme active site and the phosphorus atom of the organophosphorus compound. Although the general mechanism of reactivation has been known for years, the exact molecular aspects determining the efficiency and selectivity of individual oximes are still not clear. This hinders the development of new active compounds. In our research, using relatively simple and widely available molecular docking methods, we investigated the reactivation of acetyl- and butyrylcholinesterase blocked by sarin and tabun. For the selected oximes, their binding modes at each step of the reactivation process were identified. Amino acids essential for effective reactivation and those responsible for the selectivity of individual oximes against inhibited acetyl- and butyrylcholinesterase were identified. This research broadens the knowledge about cholinesterase reactivation and demonstrates the usefulness of molecular docking in the study of this process. The presented observations and methods can be used in the future to support the search for new effective reactivators.

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