Species differences in paraoxonase mediated hydrolysis of several organophosphorus insecticide metabolites

Journal of Toxicology
R L CarrJ E Chambers

Abstract

Paraoxonase (PON1) is a calcium dependent enzyme that is capable of hydrolyzing organophosphate anticholinesterases. PON1 activity is present in most mammals and previous research established that PON1 activity differs depending on the species. These studies mainly used the organophosphate substrate paraoxon, the active metabolite of the insecticide parathion. Using serum PON1 from different mammalian species, we compared the hydrolysis of paraoxon with the hydrolysis of the active metabolites (oxons) of two additional organophosphorus insecticides, methyl parathion and chlorpyrifos. Paraoxon hydrolysis was greater than that of methyl paraoxon, but the level of activity between species displayed a similar pattern. Regardless of the species tested, the hydrolysis of chlorpyrifos-oxon was significantly greater than that of paraoxon or methyl paraoxon. These data indicate that chlorpyrifos-oxon is a better substrate for PON1 regardless of the species. The pattern of species differences in PON1 activity varied with the change in substrate to chlorpyrifos-oxon from paraoxon or methyl paraoxon. For example, the sex difference observed here and reported elsewhere in the literature for rat PON1 hydrolysis of paraoxon was not present wh...Continue Reading

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Citations

Apr 21, 2016·Polish Journal of Veterinary Sciences·M Kulka
Oct 25, 2016·Toxicology Letters·Jeffrey L Langston, Todd M Myers
Dec 11, 2019·Biomolecules·Kumari PriyankaKirandip Gill
May 17, 2021·Drug Metabolism and Pharmacokinetics·Shotaro UeharaHiroshi Yamazaki
Dec 19, 2020·Current Drug Metabolism·Steven X HuKenneth L Feenstra

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