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In vitro oxime protection of human red blood cell acetylcholinesterase inhibited by diisopropyl-fluorophosphate
Journal of applied toxicology, 2008-05, Vol.28 (4), p.422-429
Lorke, D. E.
Hasan, M. Y.
Arafat, K.
Kuča, K.
Musilek, K.
Schmitt, A.
Petroianu, G. A.
2008
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Lorke, D. E.
Hasan, M. Y.
Arafat, K.
Kuča, K.
Musilek, K.
Schmitt, A.
Petroianu, G. A.
Titel
In vitro oxime protection of human red blood cell acetylcholinesterase inhibited by diisopropyl-fluorophosphate
Ist Teil von
Journal of applied toxicology, 2008-05, Vol.28 (4), p.422-429
Ort / Verlag
Chichester, UK: John Wiley & Sons, Ltd
Erscheinungsjahr
2008
Quelle
MEDLINE
Beschreibungen/Notizen
Oximes are enzyme reactivators used in treating poisoning with organophosphorus cholinesterase (AChE) inhibitors. The oxime dose which can be safely administered is limited by the intrinsic toxicity of the substances such as their own AChE‐inhibiting tendency. Clinical experience with the available oximes is disappointing. To meet this need, new AChE reactivators of potential clinical utility have been developed. The purpose of the study was to estimate in vitro both the intrinsic toxicity and the extent of possible protection conferred by established (pralidoxime, obidoxime, HI‐6, methoxime, trimedoxime) and experimental (K‐type) oximes, using diisopropyl‐fluoro‐phosphate (DFP) as an AChE inhibitor. The IC50 of DFP against human red blood cell AChE was determined (∼120 nm). Measurements were then repeated in the presence of increasing oxime concentrations, leading to an apparent increase in DFP IC50. Calculated IC50 values were plotted against oxime concentrations to obtain an IC50 shift curve. The slope of this shift curve (tanα) was used to quantify the magnitude of the protective effect (nm IC50 increase per µm oxime). We show that, in the case of a linear relationship between oxime concentration and IC50, the binding constant K, determined using the Schild equation, equals IC50/DFP/tanα. Based on the values of tanα and of the binding constant K, some of the new K‐oxime reactivators are far superior to pralidoxime (tanα = 0.8), obidoxime (1.5), HI‐6 (0.8), trimedoxime (2.9) and methoxime (5.9), with K‐107 (17), K‐108 (20), and K‐113 (16) being the outstanding compounds. Copyright © 2008 John Wiley & Sons, Ltd.
Sprache
Englisch
Identifikatoren
ISSN: 0260-437X
eISSN: 1099-1263
DOI: 10.1002/jat.1344
Titel-ID: cdi_proquest_miscellaneous_33083386
Format
–
Schlagworte
Acetylcholinesterase - metabolism
,
Antidotes - metabolism
,
Antidotes - pharmacology
,
Antidotes - toxicity
,
Biological and medical sciences
,
cholinesterase
,
Cholinesterase Inhibitors - toxicity
,
Cholinesterase Reactivators - metabolism
,
Cholinesterase Reactivators - pharmacology
,
Cholinesterase Reactivators - toxicity
,
DFP
,
Dose-Response Relationship, Drug
,
Erythrocytes - drug effects
,
Erythrocytes - enzymology
,
Female
,
Humans
,
Isoflurophate - toxicity
,
K-oximes
,
Male
,
Medical sciences
,
Models, Biological
,
organophosphate
,
oxime
,
Oximes - metabolism
,
Oximes - pharmacology
,
Oximes - toxicity
,
Protein Binding
,
Schild equation
,
Toxicology
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