Acetylcholine-hydrolyzing activities in soluble brain fraction: Characterization with reversible and irreversible inhibitors

作者：Estevez Jorge^*; Selva Veronica; Benabent Monica; Mangas Iris; Sogorb Miguel Angel; Vilanova Eugenio

来源：Chemico-Biological Interactions, 2016, 259: 374-381.

DOI：10.1016/j.cbi.2016.08.004

• Organophosphorus
• Cholinesterase
• Phenyl valerate esterase
• PMSF
• Mipafox
• Paraoxon
• Iso-OMPA
• Ethopropazine
• BW284C51

Some effects of organophosphorus compounds (OPs) esters cannot be explained through actions on currently recognized targets acetylcholinesterase or neuropathy target esterase (NTE). In soluble chicken brain fraction, three components (E alpha, E beta and E gamma) of pheny lvalerate esterase activity (PVase) were kinetically discriminated and their relationship with acetylcholine-hydrolyzing activity (cholinesterase activity) were studied in previous works. In this work, four enzymatic components (CS1, CS2, CS3 and CS4) of cholinesterase activity have been discriminated in soluble fraction, according to their sensitivity to irreversible inhibitors mipafox, paraoxon, PMSF and iso-OMPA and to reversible inhibitors ethopropazine and BW284C51. Cholinesterase component CS1 can be related to the Ea component of PVase activity and identified as butyrylcholinesterase (BuChE). No association and similarities can be stablished among the other PVase component (E beta and E gamma) with the other cholinesterase components (CS2, CS3, CS4). The kinetic analysis has allowed us to stablish a method for discriminating the enzymatic component based on a simple test with two inhibitors. It can be used as biomarker in toxicological studies and for monitoring these cholinesterase components during isolation and molecular identification processes, which will allow OP toxicity to be understood by a multi-target approach.

• 出版日期2016-11-25