Abstract
This review comprises studies on the mechanisms of toxicity and detoxication of organophosphorus (OP) compounds done in Croatia in different research areas. One area is the synthesis of antidotes against OP poisoning and their in vivo testing in experimental animals. In vitro studies included in this review focus on the mechanisms of reversible inhibition of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), protection of cholinesterases from inhibition by OPs, and reactivation of phosphylated cholinesterases. The third area comprises distribution profiles of BChE and paraoxonase (PON) phenotypes in selected population groups and the detection of OPs and metabolites in humans. Finally, methods are described for the detection of OP compounds in human blood and other media by means of cholinesterase inhibition.
Highlights
Elsa REINER1, Zoran RADI]2, and Vera SIMEON-RUDOLF1 Institute for Medical Research and Occupational Health, Zagreb, Croatia1, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, La Jolla, CA, USA2
In vitro studies included in this review focus on the mechanisms of reversible inhibition of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), protection of cholinesterases from inhibition by OPs, and reactivation of phosphylated cholinesterases
This paper summarizes studies on the toxicity and detoxication of organophosphorus compounds that have been conducted in Croatia
Summary
This review comprises studies on the mechanisms of toxicity and detoxication of organophosphorus (OP) compounds done in Croatia in different research areas. The third area comprises distribution profiles of BChE and paraoxonase (PON) phenotypes in selected population groups and the detection of OPs and metabolites in humans. Cholinesterases (AChE and BChE) and phosphoric triester hydrolases (PON and DFPase) are involved in the toxicity and/or detoxication of organophosphates. AChE (acetylcholinesterase; EC 3.1.1.7) and BChE (butyrylcholinesterase; EC 3.1.1.8) are inhibited by OPs, while PON (paraoxonase; EC 3.1.8.1) and DFPase (EC 3.1.8.2) hydrolyse organophosphates. Present studies are mainly focused on enzyme structure, role of individual residues in the enzyme interaction with OPs, search for effective antidotes and decontaminating agents for OPs, and on developing methods to identify OPs and their metabolites in humans and the environment. The paper was presented as an introductory lecture to the symposium on OP compounds held in Croatia as part of the EUROTOX 2006 Congress [1]
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