Estimation of Peroxidative Damage

Esterbauer, H.

doi:10.1007/978-3-642-85011-0_5

Cited by 88 publications

(104 citation statements)

References 42 publications

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“…4-HNE is produced by the peroxidation of lipids and binds to nucleophilic groups on proteins. Covalent binding of 4-HNE to proteins is a biomarker of lipid peroxidation (Esterbauer, 1996;Waeg et al, 1996). As shown in 4-HNE covalent binding to protein did not significantly increase with time in the liver homogenates of either WT or KO mice.…”

Section: Discussionmentioning

confidence: 84%

“…Oxidative stress also leads to lipid peroxidation, a major mechanism of cellular damage with some chemicals. 4-HNE is a lipid peroxidationderived aldehyde that covalently binds to protein and has been used as a biomarker of lipid peroxidation (Esterbauer, 1996). To determine the role of lipid peroxidation Western blot analysis for 4-HNE covalent binding was performed by using anti-4-HNE.…”

Section: Effect Of a Toxic Dose Of Apap On The Activity And Nitrationmentioning

confidence: 99%

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Acetaminophen-Induced Hepatotoxicity and Protein Nitration in Neuronal Nitric-Oxide Synthase Knockout Mice

Agarwal¹,

Hennings²,

Rafferty³

et al. 2011

J Pharmacol Exp Ther

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In overdose acetaminophen (APAP) is hepatotoxic. Toxicity occurs by metabolism to N-acetyl-p-benzoquinone imine, which depletes GSH and covalently binds to proteins followed by protein nitration. Nitration can occur via the strong oxidant and nitrating agent peroxynitrite, formed from superoxide and nitric oxide (NO). In hepatocyte suspensions we reported that an inhibitor of neuronal nitric-oxide synthase (nNOS; NOS1), which has been reported to be in mitochondria, inhibited toxicity and protein nitration. We recently showed that manganese superoxide dismutase (MnSOD; SOD2) was nitrated and inactivated in APAP-treated mice. To understand the role of nNOS in APAP toxicity and MnSOD nitration, nNOS knockout (KO) and wild-type (WT) mice were administered APAP (300 mg/kg). In WT mice serum alanine aminotransferase (ALT) significantly increased at 6 and 8 h, and serum aspartate aminotransferase (AST) significantly increased at 4, 6 and 8 h; however, in KO mice neither ALT nor AST significantly increased until 8 h. There were no significant differences in hepatic GSH depletion, APAP protein binding, hydroxynonenal covalent binding, or histopathological assessment of toxicity. The activity of hepatic MnSOD was significantly lower at 1 to 2 h in WT mice and subsequently increased at 8 h. MnSOD activity was not altered at 0 to 6 h in KO mice but was significantly decreased at 8 h. There were significant increases in MnSOD nitration at 1 to 8 h in WT mice and 6 to 8 h in KO mice. Significantly more nitration occurred at 1 to 6 h in WT than in KO mice. MnSOD was the only observed nitrated protein after APAP treatment. These data indicate a role for nNOS with inactivation of MnSOD and ALT release during APAP toxicity.

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Section: Discussionmentioning

confidence: 84%

Section: Effect Of a Toxic Dose Of Apap On The Activity And Nitrationmentioning

confidence: 99%

Acetaminophen-Induced Hepatotoxicity and Protein Nitration in Neuronal Nitric-Oxide Synthase Knockout Mice

Agarwal¹,

Hennings²,

Rafferty³

et al. 2011

J Pharmacol Exp Ther

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“…Reduction in cellular protein and RNA contents in medaka embryogenesis by ethanol (an index of oxidative stress) thus prompted us to extend our investigation to determine the status of oxidative stress and alcohol metabolizing enzyme mRNA levels in medaka embryos. Quantification of oxidative stress is very difficult due to short half-lives of free radicals and many products initially produced from polyunsaturated fatty acids (Esterbauer, 1996). For this reason, the detection of oxidative stress is mainly based on the quantification of malondialdehyde (MDA) which is formed as a result of peroxidation of polyunsaturated fatty acids (Rio et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

Disruption of circulation by ethanol promotes fetal alcohol spectrum disorder (FASD) in medaka (Oryzias latipes) embryogenesis

Khan

Dasmahapatra

2008

Comparative Biochemistry and Physiology Part C: Toxicology &

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Japanese medaka (Oryzias latipes) embryos exposed to ethanol have developed craniofacial, cardiovascular and skeletal defects which can be compared with the phenotypic features of fetal alcohol spectrum disorder (FASD) observed in human. The present experiment was designed to show that the disruption in circulation by ethanol during embryogenesis is a potential cause of FASD. Fertilized eggs were exposed to ethanol (0, 100 and/or 400 mM) for 24 or 48 h at various developmental stages (Iwamatsu stages 4-30) and were analyzed at 6 day post fertilization (dpf). It was observed that controls and the embryos exposed to 100 mM ethanol were in circulating state; however, a significant number of embryos of stages 4-24 exposed to 400 mM ethanol had disrupted circulation. Compared to controls, protein and RNA contents were significantly reduced in noncirculating embryos. Lipid peroxidation (LPO) analysis was made at 3, 6, 24, 48, 96 and 144 hour post fertilization (hpf). LPO was increased with the advancement of morphogenesis; however, ethanol or the circulation status had no effect. We further analyzed alcohol dehydrogenase (Adh 5 and adh8) and aldehyde dehydrogenase (Aldh9A and Aldh1A2) enzyme mRNAs in the embryos exposed to 400 mM ethanol for 24h. A developmental stage specific reduction in these enzyme mRNAs by ethanol was observed. We conclude that ethanol-induced disruption in circulation during embryogenesis is a potential cause of the development of FASD features in medaka.

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“…The end-products of lipid peroxidation (HNE and MDA) cause protein damage by addition reactions with lysine amino groups, cysteine sulfhydryl groups, and histidine imidazole groups (Esterbauer et al, 1991;Esterbauer, 1996). Modifications of protein by aldehyde products of lipid peroxidation contribute to neurodegenerative disorders, activation of kinases (Uchida et al, 1999;Uchida, 2003) and inhibition of the nuclear transcription factor (Camandola et al, 2000).…”

Section: Toxic Effects Of Secondary Products Of Lipid Peroxidationmentioning

confidence: 99%

Lipid Peroxidation: Chemical Mechanism, Biological Implications and Analytical Determination

Repetto¹,

Semprine²,

Boveris³

2012

Lipid Peroxidation

267

228

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Estimation of Peroxidative Damage

Cited by 88 publications

References 42 publications

Acetaminophen-Induced Hepatotoxicity and Protein Nitration in Neuronal Nitric-Oxide Synthase Knockout Mice

Acetaminophen-Induced Hepatotoxicity and Protein Nitration in Neuronal Nitric-Oxide Synthase Knockout Mice

Disruption of circulation by ethanol promotes fetal alcohol spectrum disorder (FASD) in medaka (Oryzias latipes) embryogenesis

Lipid Peroxidation: Chemical Mechanism, Biological Implications and Analytical Determination

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