About: Effect of acetylcholinesterase oxime-type reactivators K-48 and HI-6 on human liver microsomal cytochromes P450 in vitro.

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About: Effect of acetylcholinesterase oxime-type reactivators K-48 and HI-6 on human liver microsomal cytochromes P450 in vitro. Goto Sponge NotDistinct Permalink

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Substances K-48 and HI-6, oxime-type acetylcholinesterase (AChE) reactivators, were tested for their potential to inhibit the activities of human liver microsomal cytochromes P450 (CYP). The compounds were shown to bind to microsomal cytochromes P450 with spectral binding constants of 0.25 ? 0.05 μM (K-48) and 0.54 ? 0.15 μM (HI-6). To find which cytochrome P450 from the human liver microsomal fraction interacts with these compounds, an inhibition of enzyme activities specific for nine individual CYP enzymes (CYP1A2, CYP2A6, CYP2B6, CYP2C8, CYP2C9, CYP2C19, CYP2D6, CYP2E1, and CYP3A4) was studied. The results have shown no prominent inhibition of individual CYP activities with both compounds except the CYP2E1 activity and the HI-6 reactivator. However, the inhibition of this activity was less than 50% which makes the possible drug interactions highly unlikely. Hence, the interaction of K-48 and HI-6 oxime-type AChE reactivators with human liver microsomal CYP enzymes does not seem to be clin Substances K-48 and HI-6, oxime-type acetylcholinesterase (AChE) reactivators, were tested for their potential to inhibit the activities of human liver microsomal cytochromes P450 (CYP). The compounds were shown to bind to microsomal cytochromes P450 with spectral binding constants of 0.25 ? 0.05 μM (K-48) and 0.54 ? 0.15 μM (HI-6). To find which cytochrome P450 from the human liver microsomal fraction interacts with these compounds, an inhibition of enzyme activities specific for nine individual CYP enzymes (CYP1A2, CYP2A6, CYP2B6, CYP2C8, CYP2C9, CYP2C19, CYP2D6, CYP2E1, and CYP3A4) was studied. The results have shown no prominent inhibition of individual CYP activities with both compounds except the CYP2E1 activity and the HI-6 reactivator. However, the inhibition of this activity was less than 50% which makes the possible drug interactions highly unlikely. Hence, the interaction of K-48 and HI-6 oxime-type AChE reactivators with human liver microsomal CYP enzymes does not seem to be clin (en)
Title	Effect of acetylcholinesterase oxime-type reactivators K-48 and HI-6 on human liver microsomal cytochromes P450 in vitro. Effect of acetylcholinesterase oxime-type reactivators K-48 and HI-6 on human liver microsomal cytochromes P450 in vitro. (en)
skos:prefLabel	Effect of acetylcholinesterase oxime-type reactivators K-48 and HI-6 on human liver microsomal cytochromes P450 in vitro. Effect of acetylcholinesterase oxime-type reactivators K-48 and HI-6 on human liver microsomal cytochromes P450 in vitro. (en)
skos:notation	RIV/61989592:15110/09:00009612!RIV10-MSM-15110___
http://linked.open...avai/riv/aktivita	Z
http://linked.open...avai/riv/aktivity	Z(MSM6198959216)
http://linked.open...iv/cisloPeriodika	3
http://linked.open...vai/riv/dodaniDat	2010
http://linked.open...aciTvurceVysledku	Jančová, Petra ANZENBACHER, Pavel Šiller, Michal Anzenbacherová, Eva
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Palackého v Olomouci / Lékařská fakulta
http://linked.open...dnocenehoVysledku	311982
http://linked.open...ai/riv/idVysledku	RIV/61989592:15110/09:00009612
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Acetylcholinesterase; Cytochrome P450; CYP; AChE reactivation; Oximes; Human microsomes (en)
http://linked.open.../riv/klicoveSlovo	Acetylcholinesterase Cytochrome P450 Oximes CYP AChE reactivation Human microsomes
http://linked.open...odStatuVydavatele	IE - Irsko
http://linked.open...ontrolniKodProRIV	[B568877ABEE6]
http://linked.open...i/riv/nazevZdroje	Chemico-Biological Interactions
http://linked.open...in/vavai/riv/obor	FR
http://linked.open...ichTvurcuVysledku	4 (xsd:int)
http://linked.open...cetTvurcuVysledku	8 (xsd:int)
http://linked.open...UplatneniVysledku	2009
http://linked.open...v/svazekPeriodika	180
http://linked.open...iv/tvurceVysledku	Anzenbacher, Pavel Anzenbacherová, Eva Jančová, Petra Šiller, Michal Jun, D. Veinlichová, A. Fusek, J. Kuca, K.
http://linked.open...n/vavai/riv/zamer	Modulation of signalling and regulatory pathways in normal and cancer cells
issn	0009-2797
number of pages	5 (xsd:int)
http://localhost/t...ganizacniJednotka	15110

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