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PubMed1992

Cytophotometric assay of cytochrome oxidase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase activities in human peroxidized spermatozoa.

Human spermatozoa contain appreciable amounts of intracellular glutathione, which has a protective function against peroxidative degradation of spermatozoal polyunsaturated fatty acids by the NADPH-dependent glutathione peroxidase/reductase enzymatic system. The glutathione system provides a basic defense against peroxidative damage, without which the superoxide dismutase system would dominate. Since oxidative damage is said to include enzyme leakage and changes in metabolism, cytochrome oxidase and lactate dehydrogenase activities were used as indicators of the energy metabolism in unwashed and washed human spermatozoa during lipid peroxidation. Lipid peroxidation was induced by aerobic incubation of sperms in the presence of sodium ascorbate and ferrous sulphate. In addition, since NADPH concentrations influence the concentration of reduced glutathione, we studied glucose-6-phosphate dehydrogenase activity as an indicator of pentose phosphate shunt activity, the main source of NADPH. Microdensitometric measurements of the three enzymes were made by a Vickers M85a scanning microdensitometer. We found that the lipid peroxidation process greatly affects the 3 enzymatic activities examined and that seminal plasma protects against the extensive deleterious effects of lipid peroxidation.

Ascorbic Acid↗
PubMed1997

Effect of cryopreservation and sperm concentration on lipid peroxidation in human semen.

OBJECTIVES: To assess (1) the effect of increased lipid peroxidation on sperm membrane damage that occurs during the freeze-thaw process of cryopreservation; (2) the effect of sperm concentration on lipid peroxidation in normal fertile men; and (3) the relation between sperm motility, morphology, and lipid peroxidation. METHODS: Lipid peroxidation was measured as levels of malonaldehyde by the thiobarbituric acid method. Malonaldehyde levels in fresh and frozen-thawed semen specimens from normal donors (n = 20) were compared at a sperm concentration of 20 x 10(6)/mL. Sperm concentrations of 5, 10, 20, and 40 x 10(6)/mL were used to assess the effect of sperm concentration on malonaldehyde levels in frozen specimens. A computer-assisted semen analyzer was used to analyze sperm concentrations and motility. Comparison of the effect of TEST-yolk buffer, glycerol, and Ham's F-10 buffer on lipid peroxidation was studied in fresh semen from normal fertile men (n = 5). RESULTS: Malonaldehyde levels did not differ between fresh and cryopreserved semen specimens (P = 0.99). There was no difference in malonaldehyde levels from TEST-yolk buffer, glycerol, and Ham's F-10 buffer. As sperm concentrations increased, so did malonaldehyde levels, from 1.21 +/- 0.05 nM/hr at 5 x 10(6)/mL to 3.50 +/- 0.46 nM/hr at 40 x 10(6)/mL (P = 0.000007). Sperm motility, morphology, and malonaldehyde levels in freeze-thaw specimens were not correlated before or after removal of the cryoprotective medium. CONCLUSIONS: Malonaldehyde levels do not differ between fresh and frozen semen in normal men. Cryopreservation-induced membrane damage is not related to lipid peroxidation but may be associated with stress induced during freezing and thawing. Malonaldehyde levels increase as sperm concentrations increase. There is no correlation between sperm motility, morphology, and malonaldehyde levels.

Cryopreservation↗
PubMed1992

Leaching of hydrogen peroxide from bleached bovine enamel.

Accurately weighed bovine enamel slabs were individually immersed in 2 ml of 35% hydrogen peroxide for 1, 3, 5, 30, or 60 min. A control group was obtained by individual immersion of bovine enamel slabs in 2 ml of saline for 60 min. All samples were washed, dried, acid-etched with 37% phosphoric acid for 60 s, then washed and dried again. Two milliliters of double-distilled water were used for individual sample leaching. Leaching was done for 1, 5, 10, 20 min, or 7 days for the experimental groups and for 7 days for the control group. The samples of one of the experimental groups were leached for a second time for 1 min. A total of 112 samples was used in this study. Hydrogen peroxide was spectrophotometrically identified and quantified in all leaching solutions based on the oxidation reaction of leuco-crystal violet buffer solution by hydrogen peroxide, a reaction catalyzed by horseradish peroxidase. The results revealed a significant difference in the quantity of leached peroxide between bleached samples (irrespective of the duration of leaching) and control, saline-treated ones. No difference was observed in the quantity of leached peroxide between releached samples and control, saline-treated ones. However, these were small, random, and numerically insignificant. Statistically significant differences were also noted among some of the experimental groups. They were thought to hold no clinical significance. The results suggested that upon immersion, the complete leaching of peroxide from bleached enamel occurs rapidly.

Animals↗
PubMed2001

Induction of aerobic peroxidation of liposomal membranes by bis(cyclopentadienyl)-vanadium(IV) (acetylacetonate) complexes.

The ability of bis(cyclopentadienyl)-vanadium(IV) (acetylacetonate) (1) to initiate oxygen-dependent lipid peroxidation in zwitterionic liposomal membranes was examined in detail. A comparison of the rates of the lipid peroxidation reaction demonstrated that the electron-donating capacity of the substituted acetylacetonate ligand significantly influences the rate of reaction. An increase in the rate of lipid peroxidation correlated to a decrease in the V(IV)/V(V) redox potential. Notably, lipid peroxidation initiated with 1 proceeded without the formation of radicals as shown by EPR spin trap techniques. In contrast, lipid peroxidation initiated with non-chelated bis(cyclopentadienyl)-vanadium(IV) dichloride (6) was associated with the production of radicals under similar experimental conditions. There also was a significant pH effect on the extent of peroxidation initiated with 6 versus the reaction initiated with 1. The mode of action of 1 likely involves the activation of molecular oxygen by the vanadium(IV) center followed by allylic hydrogen atom abstraction from the lipid.

Aerobiosis↗
PubMed2001

Utilization of peroxide and its relevance in oxygen insertion reactions catalyzed by chloroperoxidase.

Chloroperoxidase (CPO) catalyzed oxygen insertions are highly enantioselective and hence of immense biotechnological potential. A peroxide activation step is required to give rise to the compound I species that catalyzes this chiral reaction. A side reaction, a catalase type peroxide dismutation, is another feature of CPO's versatility. This work systematically investigates the utilization of different peroxides for the two reactions, i.e. the catalase type reaction and the oxygen insertion reaction. For the oxygen insertion reaction, indene and phenylethyl sulfide were chosen as substrate models for epoxidation and sulfoxidation respectively. The results clearly show that CPO is stable towards hydrogen peroxide and has a total number of turnovers near one million prior to deactivation. The epoxidation reactions terminate before completion because the enzyme functioning in its catalatic mode quickly removes all of the hydrogen peroxide from the reaction mixture. Sulfoxidation reactions are much faster than epoxidation reactions and thus are better able to compete with the catalase reaction for hydrogen peroxide utilization. A preliminary study towards optimizing the reaction system components for a laboratory scale synthetic epoxidation is reported.

Alcohols↗
PubMed2001

Necrotic cell death by hydrogen peroxide in immortal DF-1 chicken embryo fibroblast cells expressing deregulated MnSOD and catalase.

The reactive oxygen species are known as endogenous toxic oxidant damaging factors in a variety of cell types, and in response, the antioxidant genes have been implicated in cell proliferation, senescence, immortalization, and tumorigenesis. The expression of manganese superoxide dismutase mRNA was shown to increase in most of the immortal chicken embryo fibroblast (CEF) cells tested, while expression of catalase mRNA appeared to be dramatically decreased in all immortal CEF cells compared to their primary counterparts. The expression of copper-zinc superoxide dismutase mRNA was shown to increase slightly in some immortal CEF cells. The glutathione peroxidase expressed relatively similar levels in both primary and immortal CEF cells. As primary and immortal DF-1 CEF cells were treated with 10-100 microM of hydrogen peroxide (concentrations known to be sublethal in human diploid fibroblasts), immortal DF-1 CEF cells were shown to be more sensitive to hydrogen peroxide, and total cell numbers were dramatically reduced when compared with primary cell counterparts. This increased sensitivity to hydrogen peroxide in immortal DF-1 cells occurred without evident changes in either antioxidant gene expression, mitochondrial membrane potential, cell cycle distribution or chromatin condensation. However, the total number of dead cells without chromatin condensation was dramatically elevated in immortal DF-1 CEFs treated with hydrogen peroxide, indicating that the inhibition of immortal DF-1 cell growth by low concentrations of hydrogen peroxide is due to increased necrotic cell death, but not apoptosis. Taken together, our observation suggests that the balanced antioxidant function might be important for cell proliferation in response to toxic oxidative damage by hydrogen peroxide.

Animals↗
PubMed2001

Lipid peroxidation-mediated oxidative stress and dopamine neuronal apoptosis in the substantia nigra during development.

The cellular pathways underlying naturally occurring neuronal apoptosis in the rat substantia nigra (SN) during the perinatal period remain largely unknown. Determining the mediators of this process in development may shed light on causes of premature neuronal death in adult neurodegenerative disorders, including the loss of dopamine neurons in Parkinson's disease. In the present study, we investigated whether lipid peroxidation-mediated oxidative stress mediates developmental death of nigral neurons by (1) establishing the profile of lipid peroxidation and other oxidative stress markers throughout the postnatal period both in the SN and striatum, and (2) examining whether the inhibitor of lipid peroxidation, alpha-tocopherol, protects these neurons from death. In addition to monitoring, the level of lipid peroxidation throughout development, we also measured the activities of three antioxidant enzymes, namely superoxide dismutase (SOD), catalase and glutathione peroxidase (GPx). We have shown that lipid peroxidation and SOD activity progressively increased from postnatal day (PND) 3 to PND 42 in both SN and striatum. During this period, GPx activity remained stable, while catalase activity transiently increased at PND 8 only in the SN. Furthermore, alpha-tocopherol treatment from embryonic day 18 to PND 2 did not reduce the number of apoptotic neurons at PND 3. These results do not support the hypothesis that lipid peroxidation-mediated oxidative stress is the major mediator of nigral dopamine neuronal apoptosis during the perinatal period.

Animals↗
PubMedDate not supplied

Redox cycling and lipid peroxidation: the central role of iron chelates.

Toxicities associated with redox cycling, including lipid peroxidation, are often attributed to the hydroxyl radical through a superoxide-driven, iron-catalyzed Haber-Weiss reaction. However, other cellular reducing agents more prevalent than superoxide, i.e., glutathione, ascorbate, cysteine and certain enzymes, can also reduce chelated iron and thereby initiate lipid peroxidation which is not inhibited by superoxide dismutase. The autoxidation of ferrous chelates yields partially reduced oxygen intermediates similar to those produced during the iron-catalyzed Haber-Weiss reaction. The mechanism of their formation, and the nature of the strong oxidant responsible for the initiation of lipid peroxidation are poorly understood, but are apparently influenced by the chelation of the iron. These conclusions stem from experiments which demonstrated variable amounts of inhibition of lipid peroxidation, dependent on the autoxidation of various ferrous chelates, by added superoxide dismutase or catalase. In addition, certain ferrous chelates are unable to initiate peroxidation of lipids in a liposomal configuration, yet capable of initiating peroxidation of lipids which were dispersed with a detergent. The results of these studies point out the need to isolate and identify the predominant physiological iron chelates for assessment of their ability to participate in redox related toxicities within the cell.

Adenosine Diphosphate↗
PubMed2002

Increased dopamine peroxidation in postmortem Parkinsonian brain.

We have previously reported the presence, in human midbrain, of an enzymatic activity which catalyzes the formation of dopaminochrome from dopamine (DA) and hydrogen peroxide. Here, we report, for the first time, an increased DA peroxidizing activity in the midbrain and basal ganglia of autoptic Parkinsonian brains. The crude activity was determined spectrophotometrically in extracts of paraffin-embedded slices obtained from autopsied brain. No addition of substrate was necessary since endogenous substrates such as DA and hydrogen peroxide were present in the samples. In Parkinson's patients' midbrain, this activity was substantially increased compared to normal midbrain. Moreover, the DA peroxidizing activity, which was absent in basal ganglia of normal people, was detectable in all our Parkinson's patients. These observations suggest that a peroxidizing pathway of DA may be present in human brain. The increased peroxidizing activity in Parkinson's patients generates the toxic compound dopaminochrome which may play a role in the pathogenesis of this disease.

Aged↗
PubMed1999

Role of glutathione, lipid peroxidation and antioxidants on acute bile-duct obstruction in the rat.

The aim of this work was to evaluate the role of lipid peroxidation and glutathione on liver damage induced by 7-day biliary obstruction in the rat. Male Wistar rats were bile-duct-ligated and divided in groups of 10 animals. Groups received vitamin E (400 IU/rat, p.o., daily) or trolox (50 mg/kg, p.o., daily) or both. Lipid peroxidation increased significantly in the livers of bile-duct-ligated rats. Vitamin E and trolox prevented lipid peroxidation. GSH was oxidized in the BDL group and the GSH/GSSG ratio decreased as a consequence. However, total glutathione content increased in liver and blood indicating a possible induction in de novo synthesis of GSH. Antioxidants preserved the normal GSH/GSSG ratio. Despite the observation that antioxidants verted lipid peroxidation and oxidation of GSH, liver injury (as assessed by serum enzyme activities, bilirubin concentration, liver glycogen content and histology) was not affected by the treatments. These results suggest that drugs that inhibit lipid peroxidation and oxidation of glutathione have no effect on conventional biochemical markers of liver injury and on liver histology of bile-duct-ligated rats for 7 days. It seems more likely that the detergent action of bile salts is responsible for solubilization of plasma membranes and cell death, which in turn may lead to oxidative stress, GSH oxidation and lipid peroxidation.

Animals↗
PubMed1994

Visceral lipid peroxidation occurs at reperfusion after supraceliac aortic cross-clamping.

PURPOSE: Recently, we have reported that lipid peroxidation specific to oxygen free radical-mediated injury increased immediately after reperfusion of human liver allografts. However, in the human liver transplantation setting it was impossible to disassociate the contributions to lipid peroxidation caused by the warm and cold ischemic phases from those caused by reperfusion. Therefore we now have studied lipid peroxidation at reperfusion after supraceliac aortic cross-clamping in patients with normal livers. METHODS: Ethane, a noninvasive biomaker of lipid peroxidation, was measured in exhaled breath of patients before and during cross-clamping of the thoracic aorta and at sequential time intervals after visceral reperfusion. RESULTS: Approximately a two-fold transient increase in the ethane level was observed at around 15 minutes after reperfusion in those patients whose aortas were cross-clamped for more than 18 minutes. CONCLUSIONS: These results indicate that free radical-mediated lipid peroxidation occurs at reperfusion of warm ischemic viscera in the clinical setting of aortic repair. This observation supports the hypothesis that substantial lipid peroxidation occurs when tissues are subjected to cold or warm ischemia followed by reperfusion.

Aged↗
PubMed2004

Cytotoxicity evaluation after coexposure to perchloroethylene and selected peroxidant drugs in rat hepatocytes.

There is evidence of hepatotoxic effects caused by Perchloroethylene (PCE), presumably due to reactive metabolic intermediates; lipid peroxidation is under study as a potential mechanism of toxicity. We aimed to verify if PCE levels comparable to those reached in the blood of exposed subjects can cause cell damage and lipid peroxidation. The association of PCE with lipid peroxidation inducing drugs (cyclosporine A, valproic acid and amiodarone) was also tested on rat isolated hepatocytes. AST and LDH release, MTT test and lipid peroxidation assay showed that PCE determines dose-dependent effects on rat isolated hepatocytes. The toxic potential resulting from our data would be valproic acid < cyclosporine A < amiodarone. While valproic acid and cyclosporine caused a mild toxicity, the effects of amiodarone were more severe; in particular, the association of PCE with amiodarone showed a clear additive effect. The role of lipid peroxidation in the liver toxicity exerted by the tested compounds was confirmed by our data, and resulted relevant after treatment of cells with amiodarone and PCE. Extrapolating these results to human, we can suggest that a subject professionally exposed to PCE, who chronically assumes a lipid peroxidation inducing drug like amiodarone, may be potentially exposed to a higher risk of liver toxicity.

Amino Acid Oxidoreductases↗
PubMed2000

Urinary aldehydes as indicators of lipid peroxidation in vivo.

The excretion of malondialdehyde (MDA), lipophilic aldehydes and related carbonyl compounds in rat and human urine was investigated. MDA was found to be excreted mainly in the form of two adducts with lysine, indicating that its predominant reaction in vivo is with the lysine residues of proteins. Adducts with the phospholipid bases serine and ethanolamine and the nucleic acid bases guanine and deoxyguanosine also were found. Except for the adduct with deoxyguanosine (dG-MDA), the excretion of these compounds increased with peroxidative stress imposed in the form of vitamin E deficiency or the administration of iron or carbon tetrachloride. Marked differences in the concentration of dG-MDA in different tissues were correlated with their content of fatty acids having three or more double bonds, the putative source of MDA. Fourteen nonpolar and eleven polar lipophilic aldehydes and other carbonyl compounds were identified as their 2,4-diphenylhydrazine derivatives in rat urine. The excretion of five nonpolar and nine polar compounds was increased under conditions of peroxidative stress. The profile of lipophilic aldehydes obtained for human urine resembled that for rat urine. Except for a reported 4-hydroxynon-2-enal conjugate with mercapturic acid, the conjugated forms of the lipophilic aldehydes excreted in urine remain unidentified. Aldehyde excretion is influenced by numerous factors that affect the formation of lipid peroxides in vivo such as energy status, physical activity and environmental temperature, as well as by wide variations in the intake of peroxides in the diet. Consequently, urinalysis for aldehydic products of lipid peroxidation is an unreliable indicator of the general state of peroxidative stress in vivo.

Aldehydes↗
PubMed2001

Catecholamines inhibit lipid peroxidation in young, aged, and Alzheimer's disease brain.

Some catecholamines and indolamines inhibit lipid peroxidation. Recent studies indicate that catecholaminergic inhibition of lipid peroxidation may be receptor mediated in vivo and in cell cultures. Because oxidative stress is one of the hypothesized pathogenic mechanisms for neurodegenerative diseases, including Alzheimer's disease (AD), we hypothesized that catecholaminergic and indolaminergic inhibition of lipid peroxidation would be altered in AD as compared to age-matched non-AD. To test this hypothesis we studied the effect of a variety of neurotransmitters and their antagonists on ascorbate-stimulated lipid peroxidation in membrane fragment preparations derived from postmortem human brain. In this in vitro system, the inhibition of lipid peroxidation by dopamine and serotonin did not appear to be receptor mediated. Further, our findings indicate that there is no apparent effect of age or AD on the inhibition of lipid peroxidation by catecholaminergic and indolaminergic agents.

8-Hydroxy-2-(di-n-propylamino)tetralin↗
PubMed2003

Dihydrolipoic acid inhibits 15-lipoxygenase-dependent lipid peroxidation.

The potential antioxidant effects of the hydrophobic therapeutic agent lipoic acid (LA) and of its reduced form dihydrolipoic acid (DHLA) on the peroxidation of either linoleic acid or human non-HDL fraction catalyzed by soybean 15-lipoxygenase (SLO) and rabbit reticulocyte 15-lipoxygenase (RR15-LOX) were investigated. DHLA, but not LA, did inhibit SLO-dependent lipid peroxidation, showing an IC(50) of 15 microM with linoleic acid and 5 microM with the non-HDL fraction. In specific experiments performed with linoleic acid, inhibition of SLO activity by DHLA was irreversible and of a complete, noncompetitive type. In comparison with DHLA, the well-known lipoxygenase inhibitor nordihydroguaiaretic acid and the nonspecific iron reductant sodium dithionite inhibited SLO-dependent linoleic acid peroxidation with an IC(50) of 4 and 100 microM, respectively, while the hydrophilic thiol N-acetylcysteine, albeit possessing iron-reducing and radical-scavenging properties, was ineffective. Remarkably, DHLA, but not LA, was also able to inhibit the peroxidation of linoleic acid and of the non-HDL fraction catalyzed by RR15-LOX with an IC(50) of, respectively, 10 and 5 microM. Finally, DHLA, but once again not LA, could readily reduce simple ferric ions and scavenge efficiently the stable free radical 1,1-diphenyl-2-pycrylhydrazyl in ethanol; DHLA was considerably less effective against 2,2'-azobis(2-amidinopropane) dihydrochloride-mediated, peroxyl radical-induced non-HDL peroxidation, showing an IC(50) of 850 microM. Thus, DHLA, at therapeutically relevant concentrations, can counteract 15-lipoxygenase-dependent lipid peroxidation; this antioxidant effect may stem primarily from reduction of the active ferric 15-lipoxygenase form to the inactive ferrous state after DHLA-enzyme hydrophobic interaction and, possibly, from scavenging of fatty acid peroxyl radicals formed during lipoperoxidative processes. Inhibition of 15-lipoxygenase oxidative activity by DHLA could occur in the clinical setting, eventually resulting in specific antioxidant and antiatherogenic effects.

Acetylcysteine↗
PubMed1987

Detection of phospholipid peroxides in biological samples.

Peroxidation of membrane lipids has been hypothesized to play a key role in various types of tissue degeneration and pathology. Lipid peroxides are formed when oxygen reacts with an unsaturated fatty acid chain. Virtually all of the unsaturated fatty acids in biological systems are bound by ester linkages in phospholipids or triglycerides. Phospholipid and triglyceride peroxides are primary products of lipid peroxidation and have rarely been measured. Most of the commonly used methods for detection of lipid peroxidation are based on detection of malondialdehyde or other chemical species that are derived from oxidized fatty acids. This review presents an overview of recently developed methods aimed at identifying and measuring oxidized phospholipids and triglycerides which are direct evidence of the occurrence of lipid peroxidation in vivo.

Animals↗
PubMed1998

Role of xanthine oxidase in hydrogen peroxide production.

Increased production of oxygen free radicals may play a role in many diseases such as hypertension. As evidence indicates that xanthine oxidase may be involved in creating these reactive oxygen species, experiments were performed to additionally characterize hydrogen peroxide (H2O2) production in xanthine oxidase catalyzed reactions. In vitro measurements of hydrogen peroxide production from the xanthine/xanthine oxidase reaction were performed in buffered saline using an electrochemical technique, and the effect of allopurinol on inhibition of xanthine oxidase was determined. Experiments were also performed in blood plasma to characterize endogenous hydrogen peroxide producing capability and xanthine oxidase activity. In the presence of sodium azide, an inhibitor of catalase, peroxide production was measured in plasma after adding xanthine or xanthine oxidase and the results were similar to those obtained in buffered saline. When only sodium azide was added to plasma, hydrogen peroxide was produced at a level of 36.1 +/- 7.6 microM (n = 5). From these measurements, endogenous xanthine oxidase activity was estimated to be 6.5 +/- 0.3 mU/ml (n = 5). These results suggests that sufficient substrate exists in plasma to produce micromolar levels of hydrogen peroxide and xanthine oxidase may catalyze these reactions.

Allopurinol↗
PubMed1999

Metalloporphyrins are potent inhibitors of lipid peroxidation.

The objectives of these studies were to determine whether metalloporphyrins could inhibit lipid peroxidation, characterize factors that influence their potency and compare their potency to prototypical antioxidants. Lipid peroxidation was initiated with iron and ascorbate in rat brain homogenates and the formation of thiobarbituric acid reactive species was used as an index of lipid peroxidation. Metalloporphyrins were found to be a novel and potent class of lipid peroxidation inhibitors. Inhibition of lipid peroxidation by metalloporphyrins was dependent on the transition metal ligated to the porphyrin, indicating that metal centered redox chemistry was important to the mechanism of their antioxidant activities. Manganese porphyrins with the highest superoxide dismutase (SOD) activities, MnOBTM-4-PyP and MnTM-2-PyP (charges are omitted throughout text for clarity), were the most potent inhibitors of lipid peroxidation with calculated IC50s of 1.3 and 1.0 microM, respectively. These manganese porphyrins were 2 orders of magnitude more potent than either trolox (IC50 = 204 microM) or rutin (IC50 = 112 microM). The potencies of the manganese porphyrins were related not only to their redox potentials and SOD activities, but also to other factors that may contribute to their ability to act as electron acceptors. The broad array of antioxidant activities possessed by metalloporphyrins make them attractive therapeutic agents in disease states that involve the overproduction of reactive oxygen species.

Animals↗