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Miroslav Pohanka,Oto Pavlis,Branislav Ruttkay-Nedecky,Jiri Sochor,Jakub Sobotka,Jiri Pikula,Vojtech Adam,Rene Kizek 한국미생물학회 2012 The journal of microbiology Vol.50 No.3
Francisella tularensis is the causative agent of tularemia. It is an intracellular pathogen with the ability to survive within phagosomes and induce pyroptotic cell death. In this study, we attempted to prove whether oxidative imbalance plays a significant role in tularemia pathogenesis. In our experimental model, we subcutaneously infected female BALB/c mice (dose 105 CFU of F. tularensis LVS). Liver, spleen, and blood were collected from mice at regular intervals from days 1–15 after infection. The bacterial burden was assessed by a cultivation test. The burden was unchanging from the 2nd to 6th day after infection. The bacterial burden corresponded to the plasmatic level of IFN-γ, IL-6, and liver malondialdehyde. After the phase of acute bacteraemia and the innate immunity reaction, the levels of reduced glutathione and total low molecular weight antioxidants decreased significantly and the activity of caspase-3 increased in the liver. The level of reduced glutathione decreased to 25% of the original level, and the total level of low molecular weight antioxidants was less than 50% of the initial amount. The demonstrated effects of tularemia-induced pathology had a more extensive impact on the liver than on the spleen.
Pohanka, Miroslav,Karasova, Jana Zdarova,Musilek, Kamil,Kuca, Kamil,Jung, Young-Sik,Kassa, Jiri Informa Healthcare 2011 Journal of enzyme inhibition and medicinal chemist Vol.26 No.1
<P>These experiments were performed on a rat model. The rats were divided into eight groups and consequently exposed to either a saline solution (control), atropine or a combination of atropine and tabun. The reactivation efficacy of the oximes was estimated on the rats exposed to tabun, atropine and a reactivator of AChE. The oximes HI-6, obidoxime, trimedoxime, K203 and KR-22836 were used as representative compounds of commonly available and new AChE reactivators. Besides the positive effect of the administered reactivators on blood AChE activity, the sizable modulation of low molecular weight antioxidant (LMWA) levels was also determined. The LMWA levels in the the animals treated with the oxime reactivators were decreased in comparison with the animals treated by atropine alone. It was found that the levels of LMWA returned to the level found in the control animals when either trimedoxime, K203 or KR-22836 were administered. The principle of oxime reactivator function and a novel insight into AChE activity regulation and oxidative stress is discussed.</P>
Holas, Ondrej,Musilek, Kamil,Pohanka, Miroslav,Kuca, Kamil,Opletalova, Veronika,Jung, Young-Sik Korean Chemical Society 2010 Bulletin of the Korean Chemical Society Vol.31 No.6
Acetylcholinesterase reactivators are crucial antidotes for the treatment of organophosphate intoxication. Standard in vitro test was chosen using a rat brain homogenate as the source of AChE. Screening of reactivation potency was performed with two concentration of reactivator (1000 ${\mu}M$ and 10 ${\mu}M$). Results were compared to established reactivators pralidoxime, methoxime, HI-6, trimedoxime and obidoxime. More than 30 novel reactivators performed equal or better reactivation ability of POX-inhibited AChE compared to currently used reactivators. The structure-activity relationship for reactivators of paraoxon-inhibited AChE was developed.
Ondrej Holas,Kamil Musilek,Miroslav Pohanka,Kamil Kuca,Veronika Opletalova,Young-Sik Jung 대한화학회 2010 Bulletin of the Korean Chemical Society Vol.31 No.6
Acetylcholinesterase reactivators are crucial antidotes for the treatment of organophosphate intoxication. Standard in vitro test was chosen using a rat brain homogenate as the source of AChE. Screening of reactivation potency was performed with two concentration of reactivator (1000 μM and 10 μM). Results were compared to established reactivators pralidoxime, methoxime, HI-6, trimedoxime and obidoxime. More than 30 novel reactivators performed equal or better reactivation ability of POX-inhibited AChE compared to currently used reactivators. The structure-activity relationship for reactivators of paraoxon-inhibited AChE was developed.
Kuca, Kamil,Cabal, Jiri,Jung, Yung Sik,Musilek, Kamil,Soukup, Ondrej,Jun, Daniel,Pohanka, Miroslav,Musilova, Lucie,Karasová,, Jana,Novotný,, Ladislav,Hrabinova, Martina Blackwell Publishing Ltd 2009 Basic & clinical pharmacology & toxicology Vol.105 No.3
<P>Abstract: </P><P>Newly developed acetylcholinesterase reactivators K117 [1,5-bis(4-hydroxyiminomethylpyridinium)-3-oxapentane dichloride] and K127 [(1-(4-hydroxyiminomethylpyridinium)-5-(4-carbamoylpyridinium)-3-oxapentane dibromide)] were tested for their potency to reactivate tabun-inhibited human brain cholinesterases. Pralidoxime and trimedoxime were chosen as standard reference reactivators. Human tissue was used, as that was closer on the real treatment of human beings. As a result, oxime K127 was found as the best tested reactivator according to the constant <I>k</I><SUB>r</SUB>, characterizing the overall reactivation process. On the contrary, the maximal reactivation ability expressed as percentage of reactivation was the best for trimedoxime. This differences were caused as a result of using the enzyme from different species. Due to this, experiments on human tissue should be conducted after <I>in vitro</I> and <I>in vivo</I> tests on animals to eliminate such important failures of promising oximes.</P>