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PubMed2002

Metformin improves lipid metabolism and attenuates lipid peroxidation in high fructose-fed rats.

AIM: Insulin resistance, hyperinsulinaemia and disturbances in glucose metabolism can be produced in normal rats by feeding them a fructose-enriched diet. Metformin, an antidiabetic drug, enhances insulin sensitivity in type 2 diabetic patients. Previous studies have shown that metformin improves insulin sensitivity in fructose-fed rats. The aim of this study was to determine the effect of metformin treatment on overall lipid metabolism and lipid peroxidation in rats that were fed a fructose-enriched diet, which leads to insulin resistance. The relationship between hyperinsulinaemia and hyperglycaemia with lipid peroxide levels was also investigated. MATERIALS AND METHODS: The animals were divided into two batches. One batch received a standard diet and the other was fed a fructose-enriched diet (72 g/100 g feed). After 2 weeks, each batch of rats was subdivided into two groups. One group received metformin (50 mg/kg per day in water) and the other received the standard diet and served as control. RESULTS: High fructose feeding resulted in hyperinsulinaemia, hyperglycaemia and alterations in lipids and lipid metabolism, and plasma and tissue lipid peroxides were significantly elevated. Administration of metformin (50 mg/kg/day) was associated with significant normalization of plasma insulin level and lipid alterations. These rats also showed significantly higher lipoprotein lipase (LPL) and lecithin cholesterol acyl transferase (LCAT) activities in plasma than untreated, fructose-fed rats. Lipid peroxides content was also decreased in plasma and tissues. Significant positive correlations were observed between the levels of plasma insulin and plasma glucose with plasma lipid peroxides. CONCLUSIONS: We conclude that enhanced lipid peroxidation occurs in addition to disturbances in lipid metabolism in fructose-fed rats. Plasma insulin level probably contributes to this increased peroxidation. Improved insulin action in metformin-treated rats could be responsible for the amelioration of these abnormalities induced by fructose feeding.

Animals↗
PubMed1996

Ascorbate-stimulated lipid peroxidation in human brain is dependent on iron but not on hydroxyl radical.

Lipid peroxidation has been postulated as a cause of neuronal damage in both aging and neurodegenerative disease. In studies of neurodegenerative disease, iron, iron plus ascorbate, or ascorbate alone has been used to stimulate lipid peroxidation. The mechanism by which ascorbate stimulates lipid peroxidation in human brain is unclear. The studies reported here were performed to determine whether ascorbate-stimulated lipid peroxidation in human brain membrane fragments was dependent on iron, superoxide radical, hydrogen peroxide, or hydroxyl radical. Our findings indicate that although ascorbate-stimulated lipid peroxidation in brain is iron dependent, it apparently does not require hydrogen peroxide or hydroxyl radical, but rather is dependent on superoxide radical formation.

Adult↗
PubMed1997

Amyloid beta-peptides increase annular and bulk fluidity and induce lipid peroxidation in brain synaptic plasma membranes.

Amyloid beta-peptides (A beta) may alter the neuronal membrane lipid environment by changing fluidity and inducing free radical lipid peroxidation. The effects of A beta(1-40) and A beta(25-35) on the fluidity of lipids adjacent to proteins (annular fluidity), bulk lipid fluidity, and lipid peroxidation were determined in rat synaptic plasma membranes (SPM). A fluorescent method based on radiationless energy transfer from tryptophan of SPM proteins to pyrene and pyrene monomer-eximer formation was used to determine SPM annular fluidity and bulk fluidity, respectively. Lipid peroxidation was determined by the thiobarbituric acid assay. Annular fluidity and bulk fluidity of SPM were increased significantly (p < or = 0.02) by A beta(1-40). Similar effects on fluidity were observed for A beta(25-35) (P < or = 0.002). Increased fluidity was associated with lipid peroxidation. Both A beta peptides significantly increased (p < or = 0.006) the amount of malondialdehyde in SPM. The addition of a water-soluble analogue of vitamin E (Trolox) inhibited effects of A beta on lipid peroxidation and fluidity in SPM. The fluidizing action of A beta peptides on SPM may be due to the induction of lipid peroxidation by those peptides. A beta-induced changes in neuronal function, such as ion flux and enzyme activity, that have been reported previously may result from the combined effects of lipid peroxidation and increased membrane fluidity.

Amyloid beta-Peptides↗
PubMed2001

Peroxidative stress selectively down-regulates the neuronal stress response activated under conditions of endoplasmic reticulum dysfunction.

Oxidative stress has been implicated in mechanisms leading to neuronal cell injury in various pathological states of the brain. Here, we investigated the effect of peroxide exposure on the expression of genes coding for cytoplasmic and endoplasmic reticulum (ER) stress proteins. Primary neuronal cell cultures were exposed to H(2)O(2) for 6 h and mRNA levels of hsp70, grp78, grp94, gadd153 were evaluated by quantitative PCR. In addition, peroxide-induced changes in protein synthesis and cell viability were investigated. Peroxide treatment of cells triggered an almost 12-fold increase in hsp70 mRNA levels, but a significant decrease in grp78, grp94 and gadd153 mRNA levels. To establish whether peroxide exposure blocks the ER-resident stress response, cells were also exposed to thapsigargin (Tg, a specific inhibitor of ER Ca(2+)-ATPase) which has been shown to elicit the ER stress response. Tg exposure induced 7.2-fold, 3.6-fold and 8.8-fold increase in grp78, grp94 and gadd153 mRNA levels, respectively. However, after peroxide pre-exposure, the Tg-induced effect on grp78, grp94 and gadd153 mRNA levels was completely blocked. The results indicate that oxidative damage causes a selective down-regulation of the neuronal stress response activated under conditions of ER dysfunction. This down-regulation was only observed in cultures exposed to peroxide levels which induced severe suppression of protein synthesis and cell injury, implying a causative link between peroxide-induced down-regulation of ER stress response system and development of neuronal cell injury. These observations could have implications for our understanding of the mechanisms underlying neuronal cell injury in pathological states of the brain associated with oxidative damage, including Alzheimer's disease where the neuronal stress response activated under conditions of ER dysfunction has been shown to be down-regulated. Down-regulation of ER stress response may increase the sensitivity of neurones to an otherwise nonlethal form of stress.

Animals↗
PubMed2002

Oligodendroglial cells in culture effectively dispose of exogenous hydrogen peroxide: comparison with cultured neurones, astroglial and microglial cells.

To investigate the antioxidative capacities of oligodendrocytes, rat brain cultures enriched for oligodendroglial cells were prepared and characterized. These cultures contained predominantly oligodendroglial cells as determined by immunocytochemical staining for the markers galactocerebroside and myelin basic protein. If oligodendroglial cultures were exposed to exogenous hydrogen peroxide (100 micro m), the peroxide disappeared from the incubation medium following first order kinetics with a half-time of approximately 18 min. Normalization of the disposal rate to the protein content of the cultures by calculation of the specific hydrogen peroxide detoxification rate constant revealed that the cells in oligodendroglial cultures have a 60% to 120% higher specific capacity to dispose of hydrogen peroxide than cultures enriched for astroglial cells, microglial cells or neurones. Oligodendroglial cultures contained specific activities of 133.5 +/- 30.4 nmol x min(-1) x mg protein(-1) and 27.5 +/- 5.4 nmol x min(-1) x mg protein(-1) of glutathione peroxidase and glutathione reductase, respectively. The specific rate constant of catalase in these cultures was 1.61 +/- 0.54 min(-1) x mg protein(-1). Comparison with data obtained by identical methods for cultures of astroglial cells, microglial cells and neurones revealed that all three of the enzymes which are involved in hydrogen peroxide disposal were present in oligodendroglial cultures in the highest specific activities. These results demonstrate that oligodendroglial cells in culture have a prominent machinery for the disposal of hydrogen peroxide, which is likely to support the protection of these cells in brain against peroxides when produced by these or by surrounding brain cells.

Animals↗
PubMed1998

Benzoyl peroxide increases UVA-induced plasma membrane damage and lipid oxidation in murine leukemia L1210 cells.

Ultraviolet A radiation induces oxidative stress and cell damage. The purpose of this investigation was to examine whether ultraviolet A-induced cell injury was amplified by the presence of a non-ultraviolet A absorbing molecule capable of generating free radicals. Benzoyl peroxide was used as a lipid soluble potential radical-generating agent. Plasma membrane permeability assessed by trypan blue uptake was used to measure cell damage in murine leukemia L1210 cells. Cells were irradiated with a pulsed Nd/YAG laser at 355 nm using 0-160 J per cm2. The ratio of the fluence-response slope in the presence of 40 microM benzoyl peroxide to that of irradiated controls was 4.3 +/- 2.6. Benzoyl peroxide alone or benzoyl peroxide added after irradiation did not cause increased trypan blue uptake. The ratio of the fluence-response slopes in the presence of 40 microM benzoyl peroxide to that of irradiated controls was 4.7 +/- 1.4 when cells were irradiated (0-43 J per cm2) with a xenon lamp, filtered to remove wavelengths <320 nm. The increased trypan blue uptake in 355 nm-irradiated cells in the presence of benzoyl peroxide was inhibited in a concentration-dependent manner by butylated hydroxytoluene, vitamin E, and trolox, a water-soluble vitamin E derivative. Lipid oxidation, assessed as thiobarbituric acid reactive substances, was significantly increased in samples irradiated with ultraviolet A in the presence of benzoyl peroxide at fluences >34 J per cm2. The increased trypan blue uptake and thiobarbituric acid reactive substances were inhibited by butylated hydroxytoluene. These results suggest that agents not absorbing ultraviolet A radiation may enhance ultraviolet A-initiated oxidative stress in cells.

Absorption↗
PubMed2001

[Dependence of lipid peroxidation on pigmentation of the porcine iris].

PURPOSE: Melanin has been shown to act as antioxidant in lipid peroxidation studies. We have now investigated lipid peroxidation in dependence on stromal pigmentation in isolated porcine irises. METHODS: The same number of lightly pigmented and heavily pigmented porcine irises (visual selection) were homogenized in buffer (50 mmol/l Na2HPO4, 50 mmol/l NaH2PO4 and 4 mmol/l sodium azide; 1:20 w/v). 500 microliters homogenate were incubated at 37 degrees C for 5, 10, 20 and 40 min in absence and presence of Fe2+ as inducer of lipid peroxidation. Lipid peroxidation was assayed by the thiobarbituric acid (TBA) test. Results are expressed as nmol of TBA reactive material produced (TBAR) per mg protein. Fe2+ concentration of the supernatant was determined spectrophotometrically with phenanthroline. RESULTS: 70 mumol/l, 180 mumol/l and 360 mumol/l Fe2+ induced lipid peroxidation. A plateau region was reached after 20 min. Lipid peroxidation differed in dependence on stromal pigmentation in porcine irises by a factor of 2.8. 180 mumol/l Fe2+ induced 1.373 +/- 0.138 nmol TBAR/mg protein in lightly pigmented irises compared to 0.491 +/- 0.125 nmol TBAR/mg protein in heavily pigmented irises after 10 min incubation (p < 0.0001, n = 4). On the other hand, the content of Fe2+ in the supernatant was the same within error. CONCLUSIONS: There was a stronger induction of lipid peroxidation in lightly pigmented porcine irises compared to heavily pigmented porcine irises. This effect may be related to the difference in stromal melanin content and its antioxidant activity.

Animals↗
PubMed1996

3-Hydroxyanthranilic acid is an efficient, cell-derived co-antioxidant for alpha-tocopherol, inhibiting human low density lipoprotein and plasma lipid peroxidation.

alpha-Tocopherol (alpha-TOH) can promote lipid peroxidation in human low density lipoprotein (LDL) unless co-antioxidants are present that eliminate the chain-carrying alpha-tocopheroxyl radical (alpha-TO.) (Bowry, V. W., Mohr, D., Cleary, J., and Stocker, R. (1995) J. Biol. Chem. 270, 5756-5763). Interferon-gamma inhibits human monocyte/macrophage-facilitated LDL lipid peroxidation via induction of cellular tryptophan degradation and production and release of 3-hydroxyanthranilic acid (3HAA) (Christen, S., Thomas, S. R., Garner, B., and Stocker, R. (1994) J. Clin. Invest. 93, 2149-2158). We now report on the mechanism of antioxidant action of 3HAA. 3HAA directly reduced alpha-TO. in UV-exposed micellar dispersions of alpha-TOH or in LDL incubated with soybean 15-lipoxygenase (SLO), as assessed by electron paramagnetic resonance spectroscopy. 3HAA did not inhibit SLO enzyme activity. Anthranilic acid, which lacks the phenoxyl group, was incapable of reducing alpha-TO.. 3HAA dose-dependently inhibited the peroxidation of surface phospholipids and core cholesteryl esters in LDL exposed to SLO, peroxyl radicals (ROO.), or Cu2+; oxidants that convert alpha-TOH to alpha-TO.. In all cases, sparing of LDL's alpha-TOH, but not ubiquinol-10 (CoQ10H2), was observed until the majority of 3HAA was consumed. Addition of 3HAA or ascorbate prevented further consumption of alpha-TOH and accumulation of lipid hydroperoxides when added to aqueous or lipophilic ROO.-oxidizing LDL after complete and partial consumption of CoQ10H2 and alpha-TOH, respectively. In contrast, addition of urate, an efficient ROO. scavenger incapable of scavenging alpha-TO., did not efficiently inhibit ongoing lipid peroxidation. Oxidation of 3HAA-supplemented human plasma by aqueous ROO. resulted in the successive consumption of ascorbate, CoQ10H2, 3HAA, bilirubin, alpha-TOH, and urate. Lipid peroxidation was prevented as long as ascorbate, CoQ10H2, and 3HAA were present, but subsequently proceeded as a free-radical chain reaction concomitant with alpha-TOH, bilirubin, and urate consumption. Addition of 3HAA to aqueous ROO.-oxidizing plasma, after complete consumption of ascorbate and CoQ10H2, strongly inhibited ongoing lipid peroxidation and consumption of alpha-TOH, bilirubin, and urate immediately and as efficiently as did ascorbate. These findings demonstrate that 3HAA is a highly efficient co-antioxidant for plasma lipid peroxidation by virtue of its ability to interact with alpha-TO. in lipoproteins. Since interferon-gamma is the principal inducer of tryptophan degradation and release of 3HAA by monocytes/macrophages, this may represent a localized extracellular antioxidant defense against LDL oxidation in inflammation.

3-Hydroxyanthranilic Acid↗
PubMed2001

Intracellular acidification triggered by mitochondrial-derived hydrogen peroxide is an effector mechanism for drug-induced apoptosis in tumor cells.

We recently showed that two photoproducts of merocyanine 540, C2 and C5, triggered cytochrome C release; however, C5 was inefficient in inducing caspase activity and apoptosis in leukemia cells, unlike C2. Here we show that HL60 cells acidified upon exposure to C2 but not C5. The intracellular drop in pH and caspase activation were dependent upon hydrogen peroxide production, and were inhibited by scavengers of hydrogen peroxide. On the contrary, caspase inhibitors did not block hydrogen peroxide production. In turn, increased intracellular hydrogen peroxide concentration was downstream of superoxide anion produced within 2 h of exposure to C2. Inhibitor of NADPH oxidase diphenyleneiodonium neither inhibited superoxide production nor caspase activation triggered by C2. However, exposure of purified mitochondria to C2 resulted in significantly increased superoxide production. Furthermore, cytochrome C release from isolated mitochondria induced by C2 was completely inhibited in the presence of scavengers of hydrogen peroxide. Contrarily, scavenging hydrogen peroxide had no effect on the cyclosporin A-sensitive mitochondrial permeability transition induced by C5. Our data suggest a scenario where drug-induced hydrogen peroxide production induces intracellular acidification and release of cytochrome C, independent of the inner membrane pore, thereby creating an intracellular environment permissive for caspase activation.

Apoptosis↗
PubMed2003

Superoxide activates uncoupling proteins by generating carbon-centered radicals and initiating lipid peroxidation: studies using a mitochondria-targeted spin trap derived from alpha-phenyl-N-tert-butylnitrone.

Although the physiological role of uncoupling proteins (UCPs) 2 and 3 is uncertain, their activation by superoxide and by lipid peroxidation products suggest that UCPs are central to the mitochondrial response to reactive oxygen species. We examined whether superoxide and lipid peroxidation products such as 4-hydroxy-2-trans-nonenal act independently to activate UCPs, or if they share a common pathway, perhaps by superoxide exposure leading to the formation of lipid peroxidation products. This possibility can be tested by blocking the putative reactive oxygen species cascade with selective antioxidants and then reactivating UCPs with distal cascade components. We synthesized a mitochondria-targeted derivative of the spin trap alpha-phenyl-N-tert-butylnitrone, which reacts rapidly with carbon-centered radicals but is unreactive with superoxide and lipid peroxidation products. [4-[4-[[(1,1-Dimethylethyl)-oxidoimino]methyl]phenoxy]butyl]triphenylphosphonium bromide (MitoPBN) prevented the activation of UCPs by superoxide but did not block activation by hydroxynonenal. This was not due to MitoPBN reacting with superoxide or the hydroxyl radical or by acting as a chain-breaking antioxidant. MitoPBN did react with carbon-centered radicals and also prevented lipid peroxidation by the carbon-centered radical generator 2,2'-azobis(2-methyl propionamidine) dihydrochloride (AAPH). Furthermore, AAPH activated UCPs, and this was blocked by MitoPBN. These data suggest that superoxide and lipid peroxidation products share a common pathway for the activation of UCPs. Superoxide releases iron from iron-sulfur center proteins, which then generates carbon-centered radicals that initiate lipid peroxidation, yielding breakdown products that activate UCPs.

Animals↗
PubMed2003

Hydrogen peroxide induces topoisomerase I-mediated DNA damage and cell death.

Reactive oxygen species modify DNA, generating various DNA lesions including modified bases such as 8-oxoguanine (8-oxoG). These base-modified DNA lesions have been shown to trap DNA topoisomerase I (TOP1) into covalent cleavage complexes. In this study, we have investigated the role of TOP1 in hydrogen peroxide toxicity. We showed that ectopic expression of TOP1 in Saccharomyces cerevisiae conferred sensitivity to hydrogen peroxide, and this sensitivity was dependent on RAD9 checkpoint function. Moreover, in the mammalian cell culture system, hydrogen peroxide-induced growth inhibition and apoptosis were shown to be partly TOP1-dependent as evidenced by a specific increase in resistance to hydrogen peroxide in TOP1-deficient P388/CPT45 murine leukemia cells as compared with their TOP1-proficient parental cell line P388. In addition, hydrogen peroxide was shown to induce TOP1-DNA cross-links. These results support a model in which hydrogen peroxide promotes the trapping of TOP1 on oxidative DNA lesions to form TOP1-DNA cleavage complexes that contribute to hydrogen peroxide toxicity.

Animals↗
PubMed1999

Stimulation of active sodium-potassium transport by hydrogen peroxide in cultured rabbit nonpigmented ciliary epithelium.

PURPOSE: Studies were conducted to examine the effect of hydrogen peroxide on active sodium-potassium transport in a cell line derived from nonpigmented ciliary epithelium of the rabbit eye. METHODS: Studies were carried out using a rabbit nonpigmented ciliary epithelium cell line. 86Rb uptake by intact cells was measured in the presence or absence of ouabain. The ouabain-sensitive potassium (86Rb) uptake rate was used as an index of the rate of active sodium-potassium transport. Cell sodium content was measured by atomic absorption spectrophotometry. Na,K-ATPase activity was determined by measuring ATP hydrolysis in the presence or absence of ouabain, using membrane material isolated by centrifugation of cell homogenates. RESULTS: Ouabain-sensitive potassium (86Rb) uptake rate measured in cells that had been preincubated with 200microM hydrogen peroxide for either 30 min or 60 min was increased to 196% and 181% of the control uptake rate, respectively. Lesser concentrations of hydrogen peroxide caused lesser degrees of stimulation. 200microM hydrogen peroxide caused an increase of cell sodium content. Such a change of cell sodium content is likely to be responsible, at least in part, for the observed stimulation of active sodium-potassium transport. However, the response may also be partly dependent on activation of a protein kinase since the serine/threonine protein kinase inhibitors staurosporine (1microM) and H-89 (20microM) were both found to prevent the stimulatory effect of 200microM hydrogen peroxide on ouabain-sensitive potassium (86Rb) uptake. Interestingly, neither H-89 nor staurosporine prevented the elevation of sodium content in cells that received 200microM hydrogen peroxide. CONCLUSIONS: Taken together, these findings suggest a low concentration of hydrogen peroxide causes increased sodium entry into the cell and also activates a protein kinase-dependent mechanism for sodium pump stimulation. The protein kinase-dependent mechanism does not appear to be triggered by an increased rate of sodium entry since staurosporine did not prevent the stimulation of ouabain-sensitive potassium (86Rb) uptake elicited by an increase in sodium permeability caused by amphotericin B.

Animals↗
PubMed1997

Changes in susceptibility of tissues to lipid peroxidation after ingestion of various levels of docosahexaenoic acid and vitamin E.

To examine the effects of dietary docosahexaenoic acid (DHA) on the potential changes in endogenous lipid peroxidation in the liver and kidney, diets containing a fixed amount of vitamin E (VE; RRR-alpha-tocopherol equivalent; 134 mg/kg diet) and a graded amount of DHA at the levels of 0, 1.0, 3.4 and 8.7% of total dietary energy were fed to rats for 14 d (Expt 1). In Expt 2, diets containing a fixed amount of DHA (8.7% of total dietary energy) and a graded amount of VE at the levels of 54, 134 and 402 mg/kg were fed to rats for 15 d. In Expt 1 it was found that endogenous lipid peroxide contents of the liver and kidney, as measured by thiobarbituric acid value and chemiluminescence intensity, were higher, and their alpha-tocopherol contents lower than those of the controls, with a gradual increase and decrease in values respectively as the dietary DHA level increased (Expt 1). However, the contents of water-soluble antioxidants, i.e. ascorbic acid and non-protein-SH (glutathione), increased with increases in the dietary DHA level, while the Se-dependent glutathione peroxidase (EC 1.11.1.9) activities did not change or tended to be lower. When the graded level of VE was given to rats in Expt 2, lipid peroxide contents in the liver and kidney did not change significantly in response to the increasing levels of dietary VE, although their alpha-tocopherol contents were higher than control values, increasing with increases in the dietary VE levels. The lipid peroxide scavengers other than alpha-tocopherol changed similarly to those in Expt 1. The results obtained in Expts 1 and 2 indicate that DHA enhances the susceptibility of the liver and kidney to lipid peroxidation concomitant with higher levels of DHA in these tissues, as shown by the fatty acid composition. In addition, VE is unable to protect membranes of the liver and kidney rich in DHA from lipid peroxidation, even after ingestion of the highest level of VE. However, the liver lipid peroxide content of the group given the highest level of DHA was not as high as expected, based on the peroxidizability index which was calculated from the fatty acid composition of the liver lipid.

Analysis of Variance↗
PubMed2001

Effects of dietary fat and endurance exercise on plasma cortisol, prostaglandin E2, interferon-gamma and lipid peroxides in runners.

OBJECTIVE: Exercise and the neuroendocrine and oxidative stress it elicits on immune function is modulated by dietary fat intake. The effects of increasing dietary fat on endurance exercise-induced alterations 80% of VO2max for 2 hours) in the plasma levels of cortisol and prostaglandin E2 (PGE2), interferon-gamma (IFN-gamma) and lipid peroxides were investigated. As higher levels of cortisol, PGE2 and lipid peroxides could be immunosuppressive, the effects of different levels of dietary fat on these measures in runners were determined. METHODS: Healthy trained runners (males and females) consumed serially 15% fat diet (of daily energy), 30% fat diet and 40% fat diets for four weeks each. In the last week of each diet period the subjects ran to exhaustion at 80% of their VO2max and blood was drawn pre- and post-run. Cortisol, IFN-gamma, PGE2 and lipid peroxides were determined using standard techniques. RESULTS: Pre-exercise levels of plasma cortisol were elevated, IFN-gamma was unchanged and PGE2 and lipid peroxides decreased on the 40%F diet compared to 30%F and 15%F. Post-exercise levels of plasma cortisol (p < 0.004), PGE2 (p < 0.0057) and lipid peroxide levels increased (p < 0.0001) after endurance exercise on all diets. The rates of increase of plasma cortisol levels during exercise were similar on all three diets. Although absolute cortisol levels were higher in the high fat group, the rate of increase of plasma cortisol level during exercise was similar on each diet. The dietary fat levels did not affect IFN-gamma, however, PGE2 and lipid peroxides decreased with increasing fat at baseline at 40%F level (p < 0.01; 30%F vs. 40% F: p < 0.002; 15%F vs. 40%F: p < 0.007). CONCLUSIONS: Data from the present study suggest that higher levels of fat in the diet, up to 40%, increase endurance running time without adverse effects on plasma cortisol, IFN-gamma, and lipid peroxide levels.

Adult↗
PubMed2004

Lipid peroxidation in the presence of albumin, inhibitory and prooxidative effects.

Oxidative modifications of LDL are involved in atherogenesis. Previously we have developed a simple assay to evaluate the susceptibility of lipids to copper-induced peroxidation in the relatively natural milieu of unfractionated serum in the presence of excess citrate. Based on our previous results we have proposed that the inducer of peroxidation in our optimized assay is a copper-citrate complex. Recent investigations indicate that under certain conditions a copper-albumin complex may induce peroxidation of ascorbate. Two different complexes may be formed in albumin-containing systems (e.g. serum) namely 1:1 and 2:1 copper-albumin complexes. The aim of the present work was to evaluate the possibility that at least one of these complexes may be responsible for the induction of peroxidation of lipids in lipidic systems containing copper and albumin, including our optimized assay. Towards this end, we have investigated the dependence of copper-induced peroxidation on the concentration of added albumin in lipidic systems in the absence and presence of citrate. In all the systems investigated in this study (PLPC liposomes, LDL, HDL and mixtures of HDL and LDL) we found that at low concentrations of free copper (e.g. in the presence of excess citrate) the 2:1 copper-albumin complex is redox-active and that this complex is the major contributor to the initiation of lipid peroxidation in these systems and in our optimized assay. The possible relevance of the induction of peroxidation in vivo by the latter complex has yet to be studied.

Citric Acid↗
PubMed2006

Alpha-tocopherol amplifies benzoyl peroxide free radical decomposition in a chemical system.

Benzoyl peroxide is commonly used in the treatment of acne, even though some adverse effects have been reported, probably mediated by the formation of peroxide-derived free radicals and the depletion of antioxidants. In the present work we have studied, in a chemical system, the effect of alpha-tocopherol on benzoyl peroxide radical decomposition to analyse the presence of an interaction between these two compounds, leading to an enhanced peroxide-cytotoxicity, as we have previously reported. Under our experimental conditions alpha-tocopherol strongly amplified the peroxide free radical decomposition occurring either in the presence or in the absence of UV irradiation, and lead to the formation of an unknown radical species in addition to benzoyloxy, phenyl and tocopheroxyl free radicals. The results of this study show that the enhancement of benzoyl peroxide toxicity in cells exposed simultaneously to this peroxide and alpha-tocopherol, is likely due to the generation of the detected radical species.

Benzoyl Peroxide↗
PubMed2003

Lead-exposed increase in movement behavior and brain lipid peroxidation in fish.

Lipid peroxides formation and motor activity were studied in fish under lead exposure for a period of 30 days. The in vitro studies of lead exposure were also performed in fish brain homogenates. Spontaneous motor activity of fish was affected by lead exposure (50 microg/L). The behaviors were increased in fish during the first three days with jerky movements and then as spontaneous movements between 16 and 30 days of lead exposure. Lipid peroxidation, which is measured as thiobarbituric acid reactive species, was increased by 52% on 15 days and 156% on 30 days of lead exposure (50 microg/L). The effects of lead exposure (50 microg) were also observed in in vitro fish brain homogenates (1 mL, 5% w/v) alone, in presence of pro-oxidant system (as iron 100 microg) or anti-oxidant system (as alpha-tocopherol, 100 microg). Steady state increments of lipid peroxidation were apparent up to the concentration of 40 microg of lead treatment in brain homogenates, which subsequently attained a plateau up to the treatment of 100 microg lead. Lead at the concentration of 50 microg promoted lipid peroxidation by 225%. Iron-induced lipid peroxidation was 135% as compared to control. Lead neurotoxicity was further aggravated by iron by 33%, while the combined impact was 476% higher when compared with the control (i.e., untreated brain homogenates). Alpha-tocopherol reduced the levels of lipid peroxidation by 31%. Moreover, treatment of alpha-tocopherol also suppressed the lead neurotoxicity by 53%. These findings suggest that lead intoxication increases spontaneous motor activity and lipid peroxides in brain of fish in chronic exposure. I, therefore, speculate that presence of iron may accentuate lead neurotoxicity, while on the other hand, treatment with biological anti-oxidant alpha-tocopherol may provide relief from lead neurotoxicity.

Animals↗
PubMed2004

Photo-assisted oxidation of chlorophenols in aqueous solutions using hydrogen peroxide and titanium dioxide.

In the present work, the efficiency of phenol and chlorophenol degradation under irradiation using hydrogen peroxide as oxidant and titanium dioxide powder as photo-catalyst was investigated. In the absence of titanium oxide, increased concentrations of hydrogen peroxide resulted in higher conversions. Generally, phenol was the most readily oxidized compound, whereas in excess of hydrogen peroxide, the more chlorine atoms were present in the ring, the less degradable the chlorophenol was, in terms of initial rate of oxidation. In the case of 4-chlorophenol, the catalytic photo-oxidation efficiency with hydrogen peroxide and titanium oxide was dependent on the catalyst concentration exhibiting a maximum at 0.025-0.05 g L(-1) titanium oxide. The combined use of titanium oxide and hydrogen peroxide resulted in higher degree of oxidation compared to results obtained when using hydrogen peroxide. Finally, the presence of Fe(III) proved to be beneficial for the photo-catalytic oxidation only in the presence of hydrogen peroxide.

Chlorophenols↗