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Ayodele J. Akinyemi, Ganiyu Oboh and Adedayo O. Ademiluyi

chinese Habanero) prevents Fe 2+ -induced lipid peroxidation in brain – in vitro . Food Chem 102 (1): 178–85. Ohkawa H, Ohishi N, Yagi K. (1979). Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem 95 : 351–358. Orhan I, Sener B, Choudhary MI, Khalid A. (2004). Acetylcholinesterase and butyrylcholinesterase inhibitory activity of some Turkish medicinal plants. J Ethnopharmacol 91 : 57–60. Romani R, Antognelli C, Baldracchini F, De Santis A, Isani G, Giovannini E. (2003). Increased acetylcholinesterase

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Natalia Wszelaki, Agnieszka Kuciun and Anna Kiss

References R.M. Lane, S.G. Potkin and A. Enz, Targeting acetylcholinesterase and butyrylcholinesterase in dementia, Int. J. Neuropsychopharmacol.   9 (2006) 101-124; DOI: 10.1017/S1461145705005833. R.J. Houghton and M.J. Howes, Natural products and derivatives affecting neurotransmission relevant to Alzheimer's and Parkinson's disease, Neurosignals   14 (2005) 2-22; DOI: 10.1159/000085382. G.L. Ellman, D. Courtney, V. Andres and R.M. Featherstone, A new and rapid colorimetric

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Miroslav Pohanka

-936. Buratti FM, D'Aniello A, Volpe MT, Menequz A, and Testai E. (2005). Malathion bioactivation in the human liver: the contribution of different cytochrome p450 isoforms. Drug Metab Dispos   33 : 295-302. Campanella L, Lelo D, Martini E, and Tomassetti M. (2007). Organophosphorus and carbamete pesticide analysis using an inhibition tyrosinase organic phase enzyme sensor; comparison by butyrylcholinesterase + choline oxidase opee and application to natural waters. Anal Chim Acta   587 : 22-32. Cometa MF, Lorenzini P

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Dominik Szwajgier

. Neurochem., 2005, 92, 749-758. 38. Simmering R., Pforte H, Jacobasch G., Blaut B., The growth of the flavonoid-degrading intestinal bacterium, Eubacterium ramulus, is stimulated by dietary flavonoids in vivo. FEMS Microbiol.Ecol., 2002, 40, 243-248. 39. Szwajgier D., Borowiec K., Phenolic acids from malt are efficient acetylcholinesterase and butyrylcholinesterase inhibitors. J. Inst.Brew., 2012, 118, 40-48. 40. Tong-Un T., Muchimapura S., Phachonpai W., Wattanathorn J., Nasal administration of quercetin liposomes modulate

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Anita Bosak, Maja Katalinić and Zrinka Kovarik

References Whittaker VP. How the cholinesterases got their modern names. Chem Biol Interact 2010;187:23-6. Darvesh S, Hopkins DA, Geula C. Neurobiology of butyrylcholinesterase. Nat Rev Neurosci 2003;4:131-8. Alles GA, Hawes RC. Cholinesterases in the blood of man. J Biol Chem 1940;133:375-90. Enzyme Nomenclature, Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the Nomenclature and

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Elsa Reiner, Zoran Radić and Vera Simeon-Rudolf

the peripheral anionic site on acetylcholinesterase: Inhibition by substrates and coumarin derivatives. Molec Pharmacol 199139:98-104. Simeon-Rudolf V, Reiner E, Škrinjarić-Špoljar M, Radić B, Lucić A, Primožić I, Tomić S. Quinuclidinium-imidazolium compounds: Synthesis, mode of interaction with acetylcholinesterase and effect upon Soman intoxicated mice. Arch Toxicol 199872:289-95. Simeon-Rudolf V, Kovarik Z, Radić Z, Reiner E. Reversible inhibition of acetylcholinesterase and butyrylcholinesterase by 4

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Slavica Vučinić, Milica Zlatković, Biljana Antonijević, Marijana Ćurčić and Bogdan Bošković

Despite improvements to intensive care management and specific pharmacological treatments (atropine, oxime, diazepam), the mortality associated with organophosphate (OP) poisoning has not substantially decreased. The objective of this examination was to describe the role of fresh frozen plasma (FFP) in acute OP poisoning. After a deliberate ingestion of malathion, a 55-year-old male suffering from miosis, somnolence, bradycardia, muscular fasciculations, rales on auscultation, respiratory insufficiency, as well as from an inhibition of red blood cell acetylcholinesterase (AChE) and plasma butyrylcholinesterase (BuChE), was admitted to hospital. Malathion was confirmed in a concentration of 18.01 mg L-1. Apart from supportive measures (including mechanical ventilation for four days), antidotal treatment with atropine, oxime - pralidoxime methylsulphate (ContrathionR), and diazepam was administered, along with FFP. The potentially beneficial effects of FFP therapy included a prompt increase of BuChE activity (from 926 IU L-1 to 3277 IU L-1; reference range from 7000 IU L-1 to 19000 IU L-1) and a reduction in the malathion concentration, followed by clinical recovery. Due to BuChE replacement, albumin content, and volume restitution, FFP treatment may be used as an alternative approach in patients with acute OP poisoning, especially when oximes are not available.

Open access

Horst Thiermann, Kai Kehe, Dirk Steinritz, John Mikler, Ira Hill, Thomas Zilker, Peter Eyer and Franz Worek

Red Blood Cell Acetylcholinesterase and Plasma Butyrylcholinesterase Status: Important Indicators for the Treatment of Patients Poisoned by Organophosphorus Compounds

Inhibition of acetylcholinesterase (AChE) is regarded as the primary toxic mechanism of organophosphorus compounds (OP). Therapeutic strategies are directed to antagonise overstimulation of muscarinic receptors with atropine and to reactivate inhibited AChE with oximes. Reactivation is crucial within the neuromuscular synapse, where atropine is ineffective, since peripheral neuromuscular block eventually leads to respiratory failure. Patients with OP intoxication have to be identified as early as possible.

During an international NBC-defence exercise anesthetised pigs were poisoned with sarin, followed by treatment with atropine and oxime. Blood samples were drawn and red blood cell (RBC)-AChE activity determined with a fielded test system on-site. Within a few minutes the poisoning was verified. After administration of HI-6, RBC-AChE activity increased rapidly. Blood samples were reanalysed in our laboratory in Munich. Almost identical course of the AChE activities was recorded by both systems.

The more comprehensive cholinesterase status was determined in Munich. Oxime administration can be stopped when AChE is aged completely, but has to be continued as long as poison is present in the body and reactivation is possible.

To aid the on-site physician in optimising diagnosis and treatment, a fielded test system should be available to allow rapid determination of the complete cholinesterase status.

Open access

Zrinka Kovarik, Ana Vrdoljak, Suzana Berend, Maja Katalinić, Kamil Kuča, Kamil Musilek and Božica Radić

Evaluation of Oxime K203 as Antidote in Tabun Poisoning

We studied bispyridinium oxime K203 [(E)-1-(4-carbamoylpyridinium)-4-(4-hydroxyiminomethylpyridinium)-but-2-ene dibromide] with tabun-inhibited human acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) in vitro, and its antidotal effect on tabun-poisoned mice and rats in vivo. We compared it with oximes K048 and TMB-4, which have proven the most efficient oxime antidotes in tabun poisoning by now. Tabun-inhibited AChE was completely reactivated by K203, with the overall reactivation rate constant of 1806 L mol-1 min-1. This means that K203 is a very potent reactivator of tabun-inhibited AChE. In addition, K203 reversibly inhibited AChE (K i = 0.090 mmol L-1) and BChE (K i = 0.91 mmol L-1), and exhibited its protective effect against phosphorylation of AChE by tabun in vitro. In vivo, a quarter of the LD50 K203 dose insured survival of all mice after the application of as many as 8 LD50 doses of tabun, which is the highest dosage obtained compared to K048 and TMB-4. Moreover, K203 showed high therapeutic potency in tabun-poisoned rats, preserving cholinesterase activity in rat plasma up to 60 min after poisoning. This therapeutic improvement obtained by K203 in tabun-poisoning places this oxime in the spotlight for further development.

Open access

Maja Katalinić, Nikolina Maček Hrvat, Jana Žďárová Karasová, Jan Misik and Zrinka Kovarik

, Cerasoli DM, Federko JM, Luo C, Saxena A, Doctor BP, Olson C. Protection against soman or VX poisoning by human butyrylcholinesterase in guinea pigs and cynomolgus monkeys. Chem Biol Interact 2005;157-158:205-10. PMID: 16289064 19. Rosenberg YJ, Laube B, Mao L, Jiang X, Hernandez-Abanto S, Lee KD, Adams R. Pulmonary delivery of an aerosolized recombinant human butyrylcholinesterase pretreatment protects against aerosolized paraoxon in macaques. Chem Biol Interact 2013;203:167-71. doi: 10.1016/j. cbi.2012.11.004 20. Kovarik Z, Katalinić M