Role of reactive oxygen species in organophosphate insecticide phosalone toxicity in erythrocytes in vitro

Altuntaş, İrfan; Delibaş, Namık; Doğuç, Duygu Kumbul; Özmen, Sadık; Gültekin, Fatih

doi:10.1016/s0887-2333(02)00133-9

Cited by 69 publications

(26 citation statements)

References 15 publications

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“…In our previous in vitro and in vivo studies, MDA formation increased with the administration of MD, fenthion, phosalone and diazinon (Altuntas and Delibas, 2002;Altuntas et al, 2002a, b;Altuntas et al, 2003) in a similar manner to the present study. The increase in MDA formation may be due to MD itself inducing LPO or possible due to an increase in ROS induced by MD.…”

Section: Discussionsupporting

confidence: 90%

The effects of subchronic methidathion toxicity on rat liver: Role of antioxidant vitamins C and E

et al. 2006

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Methidathion (MD) phosphorodithioic acid S-[(5-methoxy-2-oxo-1,3,4-thiadiazol-3(2H)-yl)methyl] O,O-dimethyl ester is the organophosphate insecticide (OPI) most commonly used worldwide in the pest control of crops. Subchronic MD exposure was evaluated for its effects on lipid peroxidation, the serum activities of cholinesterase (ChE), and enzymes concerning liver damage, and the protective effects of combination of vitamins E and C in albino rats. Additionally, the histopathological changes in liver tissue were examined. Experimental groups were as follows: control group; a group treated with 5 mg/kg body weight MD (MD group); and a group treated with 5 mg/kg body wight MD plus vitamin E plus vitamin C (MD+AO group). The MD and MD+AO groups were treated orally with MD on five days a week for 4 weeks. The serum activities of cholinesterase (ChE), alanine transferase (ALT), aspartate amiotransferase (AST), lactate dehydrogenase (LDH), gamma-glutamyltransferase (GGT), alkaline phosphatase (ALP), and the concentration of malondialdehyde (MDA) and liver histopathology were studied. In serum samples, MD significantly increased MDA concentration and ALP, AST, GGT, LDH activities but decreased the ALT and ChE activities. In the MD+AO group, MDA level and ALP, AST, LDH activities were significantly decreased and ChE activity was increased compared to the MD group. Histopathological changes found in liver tissue of rats treated with MD included were infiltration with mononuclear cells in all portal areas, sinusoidal dilatation, and focal microvesicular steatosis and hydropic degenerations in parenchymal tissue. The severity of these lesions was reduced by administration of vitamins. From these results, it can be concluded that subchronic MD causes liver damage, and lipid peroxidation may be a molecular mechanism involved in MD-induced toxicity. Furthermore, the combination of vitamins E and C can reduce the toxic effects of MD on liver tissue of rats.

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Section: Discussionsupporting

confidence: 90%

The effects of subchronic methidathion toxicity on rat liver: Role of antioxidant vitamins C and E

et al. 2006

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“…Thus, dogma indicates that the target of OP pesticides is AChE, but many authors postulate that these compounds also disturb cellular redox processes, and change the activities of antioxidant enzymes (Abdollahi et al, 2004;Possamai et al, 2007). OP metabolism produces reactive oxygen species (ROS) that are highly reactive molecules, which have one or more unpaired electrons (Altuntas et al, 2003). ROS cause lipid peroxidation resulting in the formation of highly reactive stable and unstable hydroperoxides of saturated and unsaturated lipids with eventual damage to DNA.…”

Section: Introductionmentioning

confidence: 99%

Impacts of oxidative stress on acetylcholinesterase transcription, and activity in embryos of zebrafish (Danio rerio) following Chlorpyrifos exposure

Rodrı́guez-Fuentes

Rubio-Escalante

Noreña-Barroso

et al. 2015

Comparative Biochemistry and Physiology Part C: Toxicology &

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“…BOA is widely used as a synthetic intermediate of related derivatives and is an important group of allelochemicals that respond to tissue damage or pathogen attack in gramineous plants, such as corn, rye, and wheat (10)(11)(12)(13)(14). BOA is a defensive compound that inhibits the growth and development of microorganisms and plants and also deters insect feeding (15,16).…”

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confidence: 99%

Metabolic Pathway Involved in 6-Chloro-2-Benzoxazolinone Degradation by Pigmentiphaga sp. Strain DL-8 and Identification of the Novel Metal-Dependent Hydrolase CbaA

Dong

Wang

Huang

et al. 2016

Appl Environ Microbiol

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ABSTRACT6-Chloro-2-benzoxazolinone (CDHB) is a precursor of herbicide, insecticide, and fungicide synthesis and has a broad spectrum of biological activity. Pigmentiphaga sp. strain DL-8 can transform CDHB into 2-amino-5-chlorophenol (2A5CP), which it then utilizes as a carbon source for growth. The CDHB hydrolase (CbaA) was purified from strain DL-8, which can also hydrolyze 2-benzoxazolinone (BOA), 5-chloro-2-BOA, and benzamide. The specific activity of purified CbaA was 5,900 U · mg protein ؊1for CDHB, with K m and k cat values of 0.29 mM and 8,500 s ؊1 , respectively. The optimal pH for purified CbaA was 9.0, the highest activity was observed at 55°C, and the inactive metal-free enzyme could be reactivated by Mg 2؉ , Ni 2؉ , Ca 2؉ , or Zn 2؉ . Based on the results obtained for the CbaA peptide mass fingerprinting and draft genome sequence of strain DL-8, cbaA (encoding 339 amino acids) was cloned and expressed in Escherichia coli BL21(DE3). CbaA shared 18 to 21% identity with some metal-dependent hydrolases of the PF01499 family and contained the signature metal-binding motif Q 127 XXXQ 131 XD 133 XXXH 137 . The conserved amino acid residues His288 and Glu301 served as the proton donor and acceptor. E. coli BL21(DE3-pET-cbaA) resting cells could transform 0.2 mM CDHB into 2A5CP. The mutant strain DL-8⌬cbaA lost the ability to degrade CDHB but retained the ability to degrade 2A5CP, consistent with strain DL-8. These results indicated that cbaA was the key gene responsible for CDHB degradation by strain DL-8. IMPORTANCE2-Benzoxazolinone (BOA) derivatives are widely used as synthetic intermediates and are also an important group of allelochemicals acting in response to tissue damage or pathogen attack in gramineous plants. However, the degradation mechanism of BOA derivatives by microorganisms is not clear. In the present study, we reported the identification of CbaA and metabolic pathway responsible for the degradation of CDHB in Pigmentiphaga sp. DL-8. This will provide microorganism and gene resources for the bioremediation of the environmental pollution caused by BOA derivatives. 6-Chloro-2-benzoxazolinone (CDHB) is the precursor of fenoxaprop-p-ethyl (FE) and metamifop synthesis (1). FE is a postemergence aryloxyphenoxy propionate (AOPP) herbicide that is used to control annual and perennial weeds in crops, such as soybean, turf, and wheat (2, 3). Many studies have demonstrated that FE can be hydrolyzed to fenoxaprop acid (FA) and further transformed into CDHB and 2-(4-hydroxyphenoxy)-propionic acid (HPP) by soil microorganisms (4-6). Recently, the hydrolysis of FE to FA by several esterases from different microorganisms has been reported (7-9). However, the underlying genes and the metabolic pathway responsible for the degradation of CDHB in microorganisms are unknown.CDHB is a type of 2-benzoxazolinone (BOA) derivative. BOA is widely used as a synthetic intermediate of related derivatives and is an important group of allelochemicals that respond to tissue damage or pathogen attack in gramineous plants, s...

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Role of reactive oxygen species in organophosphate insecticide phosalone toxicity in erythrocytes in vitro

Cited by 69 publications

References 15 publications

The effects of subchronic methidathion toxicity on rat liver: Role of antioxidant vitamins C and E

The effects of subchronic methidathion toxicity on rat liver: Role of antioxidant vitamins C and E

Impacts of oxidative stress on acetylcholinesterase transcription, and activity in embryos of zebrafish (Danio rerio) following Chlorpyrifos exposure

Metabolic Pathway Involved in 6-Chloro-2-Benzoxazolinone Degradation by Pigmentiphaga sp. Strain DL-8 and Identification of the Novel Metal-Dependent Hydrolase CbaA

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