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National Institute of Environmental Health Sciences

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Your Environment. Your Health.

Publication Detail

Title: Proteomic analysis of adducted butyrylcholinesterase for biomonitoring organophosphorus exposures.

Authors: Marsillach, Judit; Hsieh, Edward J; Richter, Rebecca J; MacCoss, Michael J; Furlong, Clement E

Published In Chem Biol Interact, (2013 Mar 25)

Abstract: Organophosphorus (OP) compounds include a broad group of toxic chemicals such as insecticides, chemical warfare agents and antiwear agents. The liver cytochromes P450 bioactivate many OPs to potent inhibitors of serine hydrolases. Cholinesterases were the first OP targets discovered and are the most studied. They are used to monitor human exposures to OP compounds. However, the assay that is currently used has limitations. The mechanism of action of OP compounds is the inhibition of serine hydrolases by covalently modifying their active-site serine. After structural rearrangement, the complex OP inhibitor-enzyme is irreversible and will remain in circulation until the modified enzyme is degraded. Mass spectrometry is a sensitive technology for analyzing protein modifications, such as OP-adducted enzymes. These analyses also provide some information about the nature of the OP adduct. Our aim is to develop high-throughput protocols for monitoring OP exposures using mass spectrometry.

PubMed ID: 23123252 Exiting the NIEHS site

MeSH Terms: No MeSH terms associated with this publication

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