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At least 217 records · Page 12Linked to original sources
PubMed1992

Vascular cells under peroxide induced oxidative stress: a balance study on in vitro peroxide handling by vascular endothelial and smooth muscle cells.

Enzymes such as glutathione peroxidase and catalase play an important role in the cellular defence against (per)oxidative stress. Balance- and inhibitor-studies were undertaken with in vitro cultured human vascular endothelial cells (EC) and smooth muscle cells (SMC) to assay the relative importance of these enzymes in the handling of cumene hydroperoxide (Chp) and hydrogen peroxide (H2O2). Low concentrations of Chp (up to 80 microM) could be removed to near completion within the first hour of incubation by stimulation of the hexose monophosphate shunt (HMS) of both cell types. The HMS activity reached a plateau upon incubation with higher concentrations of Chp (> 80 microM). The non-converted Chp in the higher concentrations could be detected quantitatively in the incubation solution. After inhibition of the glutathione reductase by 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU), incubation with Chp (40 microM) did not result in a stimulation of the HMS activity. Moreover the added Chp could be recovered from the medium. So Chp is exclusively handled by the GSH-redox cycle. When low concentrations of H2O2 (up to 80 microM) were added to EC or SMC approximately 50% of the peroxide loss could not be accounted for. Inhibitor studies with aminotriazole proved that catalase was responsible for the handling of this unaccounted H2O2. In both ECs and SMCs at lower concentrations of H2O2 the GSH-redox cycle was as effective as catalase and at higher H2O2 concentrations the catalase pathway plays the major role.

Benzene Derivatives↗
PubMed1979

The mechanism of NADPH-dependent lipid peroxidation. The propagation of lipid peroxidation.

NADPH-dependent lipid peroxidation occurs in two distinct sequential radical steps. The first step, initiation, is the ADP-perferryl ion-catalyzed formation of low levels of lipid hydroperoxides. The second step, propagation, is the iron-catalyzed breakdown of lipid hydroperoxides formed during initiation generating reactive intermediates and products characteristic of lipid peroxidation. Propagation results in the rapid formation of thiobarbituric acid-reactive material and lipid hydroperoxides. Propagation can be catalyzed by ethylenediamine tetraacetate-chelated ferrous ion, diethylenetriamine pentaacetic acid-chelated ferrous ion, or by ferric cytochrome P-450. However, cytochrome P-450 is destroyed during propagation.

Animals↗
PubMed1979

[Lipid peroxides and atherosclerosis. The content of lipid peroxidation products in the blood in ischemic heart disease].

It was established that the content of primary (acylhydroperoxide) and secondary (intermollecular "seams" in aminophospholipids) products of lipid peroxide oxidation in blood of patients with ischemic heart disease is increased against the background of hyperlipidemia and hypercholesterolemia. It is suggested that intensification of lipid peroxide oxidation may play a role in the pathogenesis of atherosclerosis.

Adult↗
PubMed1980

[Lipid peroxides and atherosclerosis. Hypothesis: the role of cholesterol and free-radical lipid peroxidation in altering cell membrane properties in hypercholesterolemia and atherosclerosis].

When experimental animals are kept on an atherogenic diet the NADP.H-dependent phospholipid deoxygenase in the membranes of the hepatic endoplasmic reticulum is activated and the degree of membrane oxidation is increased. "Peroxide" modification of microsomal membranes is attended by changes in their conformation and as a consequence, changes in the activity of membrane-bound enzymes. Proceeding from the fact that the synthesis of the components and the assembly of the supramolecular lipoprotein structure as well as cholesterol catabolism are accomplished by the enzyme systems localized in the hepatic microsomes, the role of peroxidation of the microsomal lipids in the pathogenesis of atherosclerosis is discussed.

Animals↗
PubMed2003

Lanthanum(III)-catalyzed disproportionation of hydrogen peroxide: a heterogeneous generator of singlet molecular oxygen-1O2 (1Deltag)-in near-neutral aqueous and organic media for peroxidation of electron-rich substrates.

The decomposition of hydrogen peroxide into singlet molecular oxygen-(1)O(2) ((1)Delta(g))-in the presence of lanthanum(iii) salts was studied by monitoring its characteristic IR luminescence at 1270 nm. The process was found to be heterogeneously catalyzed by La(III), provided that the heterogeneous catalyst is generated in situ. The yield of (1)O(2) generation was assessed as 45+/-5 % both in water and in methanol. The pH-dependence on the rate of (1)O(2) generation corresponds to a bell-shaped curve from pH 4.5 to 13 with a maximum around pH 8. The study of the influence of H(2)O(2) showed that the formation of (1)O(2) begins as soon as one equivalent of H(2)O(2) is introduced. It then increases drastically up to two equivalents and more smoothly above. Unlike all other metal salt catalyst systems known to date for H(2)O(2) disproportionation, this chemical source of (1)O(2) is able to generate (1)O(2) not only in basic media, but also under neutral and slightly acidic conditions. In addition, this La-based catalyst system has a very low tendency to induce unwanted oxygenating side reactions, such as epoxidation of alkenes. These two characteristics of the heterogeneous lanthanum catalyst system allow non-photochemical (i.e., "dark") singlet oxygenation of substrate classes that cannot be peroxidized successfully with conventional molybdate catalysts, such as allylic alcohols and alkenyl amines.

Journal Article↗
PubMed2006

Distillation kinetics of solid mixtures of hydrogen peroxide and water and the isolation of pure hydrogen peroxide in ultrahigh vacuum.

We present results of the growth of thin films of crystalline H2O2 and H2O2*2H2O (dihydrate) in ultrahigh vacuum by distilling an aqueous solution of hydrogen peroxide. We traced the process using infrared reflectance spectroscopy, mass loss on a quartz crystal microbalance, and in a few cases ultraviolet-visible reflectance. We find that the different crystalline phases-water, dihydrate, and hydrogen peroxide-have very different sublimation rates, making distillation efficient to isolate the less volatile component, crystalline H2O2.

Journal Article↗
PubMedDate not supplied

Age-dependent production of mitochondrial hydrogen peroxide, lipid peroxides and fluorescent pigments in the rat heart.

Mitochondria were prepared from hearts of 3-, 14-, 18-, and 24-month-old male Wistar rats. Respiratory control ratio (RCR) values did not change with age in the glutamate or succinate-induced respiration except at 24 months in which RCR values significantly increased with both the substrates. Using still glutamate or succinate as substrates the production of H2O2 was measured in the presence of antimycin. A 70% and 25% increase in H2O2 formation was observed at 14 and 18 months of age, respectively, in comparison to the youngest group. Only in the presence of succinate was a 25% elevation in H2O2 found at 24 months of age. These observations parallel with the decrease of the ratio between tissue levels of reduced and oxidized glutathione that was observed at 14 and 18 months of age. The concentration of myocardial malondialdehyde, a secondary product of lipid peroxidation, remained the same at all ages measured, most probably because it is readily metabolized in vivo. On the contrary the myocardial level of lipofuscin, which is not degraded by the cell, progressively increased beginning from 18 months of age.

Aging↗
PubMed1992

Cell death and lipid peroxidation in isolated hepatocytes incubated in the presence of hydrogen peroxide and iron salts.

The incubation of isolated hepatocytes in the presence of glucose plus glucose oxidase, a H2O2-generating system, resulted in extensive loss of cell viability, as expressed by the release of lactate dehydrogenase (LDH). Disturbance of metabolic functions such as glycogen and protein synthesis was also caused by H2O2, but in no case was malondialdehyde (MDA)-like products detected. The lytic effect of H2O2 was significantly enhanced by incubating hepatocytes in the presence of iron salts. Under these conditions, MDA-like products were detected, but lipid peroxidation and cell injury did not correlate. Iron chelators modulated the cytotoxicity of H2O2 in different (and opposite) ways: when iron was complexed with ADP, increased cell lysis was observed compared to uncomplexed iron plus H2O2. Iron-DTPA, on the contrary, decreased such a lytic effect. The preincubation of hepatocytes with desferrioxamine mesylate (Desferal; a strong iron chelator) abolished the cytolytic effects produced by the association of iron salts and H2O2, as well as the membrane oxidative injury due to H2O2 alone, thus suggesting the existence of an intracellular source of iron. This kind of mechanism (metal chelation rather than radical scavenging) is supported by the absence of any protective effect by some free radical scavengers against the oxidative injury induced by the association iron H2O2. Nevertheless, the glycogenolytic effects observed in the presence of H2O2 were not modified by Desferal. In our opinion, the cytotoxicity of the association H2O2 plus iron salts involves at least two different and independent mechanisms.

Animals↗
PubMed1993

Effect of hydrogen peroxide on sugar transport in Schizosaccharomyces pombe. Absence of membrane lipid peroxidation.

Stationary unaerated cells of S. pombe containing endogenous substrates but not energized by any exogenous ones take up 2-deoxy-D-glucose, 6-deoxy-D-glucose, D-xylose and D-arabinose actively over diffusion equilibrium. The active uptake is inhibited by 20-100 mmol/L H2O2 which causes an increase in KT but has no effect on Jmax. This "competitive inhibition" indicates that H2O2 affects directly the sugar binding sites of the transporters. The ATP-binding site of the plasma membrane H(+)-ATPase is also affected by 100 mmol/L H2O2; the KT decreases 7-fold, Jmax about 2.5-fold. These effects are not likely to be mediated by membrane lipid peroxidation which appears to be lacking in S. pombe, and this lack may be one of the reasons for the high resistance of this yeast to H2O2. Because of this S. pombe represents a suitable system for studying direct effects of oxidants on membrane proteins.

Antimycin A↗
PubMed1998

Linoleic acid peroxidation--the dominant lipid peroxidation process in low density lipoprotein--and its relationship to chronic diseases.

Modern separation and identification methods enable detailed insight in lipid peroxidation (LPO) processes. The following deductions can be made: (1) Cell injury activates enzymes: lipoxygenases generate lipid hydroperoxides (LOOHs), proteases liberate Fe ions--these two processes are prerequisites to produce radicals. (2) Radicals attack any activated CH2-group of polyunsaturated fatty acids (PUFAs) with about a similar probability. Since linoleic acid (LA) is the most abundant PUFA in mammals, its LPO products dominate. (3) LOOHs are easily reduced in biological surroundings to corresponding hydroxy acids (LOHs). LOHs derived from LA, hydroxyoctadecadienoic acids (HODEs), surmount other markers of LPO. HODEs are of high physiological relevance. (4) In some diseases characterized by inflammation or cell injury HODEs are present in low density lipoproteins (LDL) at 10-100 higher concentration, compared to LDL from healthy individuals.

Aging↗
PubMed1987

Lipid peroxidation and lipid peroxide detected by chemiluminescence.

This article emphasizes the advantages of using a luminescence spectrometer based on photon counting techniques for the detection of lipid peroxidation. An overview is presented of how chemiluminescence can be stimulated in the luminol-cytochrome c heme peptide system as an assay for lipid hydroperoxides. This method is used for finding antioxidant drugs. The specificity and advantages of the chemiluminescent method for detecting lipid hydroperoxides is reviewed.

Animals↗
PubMed2002

Spectrofluorometric determination of vanadium based on the formation of a ternary complex between vanadium, peroxides, and 2-alpha-pyridylthioquinaldinamide. Application to the determination of hydrogen peroxide and peroxy acids.

A selective and sensitive method for the determination of the total amount of vanadium in nutritional and biological substrates is proposed. The method is based on the reaction of vanadium with 2-alpha-pyridylthioquinaldinamide (PTQA) in the presence of H2O2. The product of this reaction emits constant fluorescence, in a sulfuric acid environment, at 490 nm, with the exciting radiation set at 340 nm. Various parameters such as acidity, flow rate, solvents, and temperature were studied. The presence of a surface-active agent was also considered in order to increase sensitivity. At the optimal conditions, a calibration curve was constructed, revealing a linear range of 2-100 microg L(-1) and a detection limit as low as 0.5 microg L(-1) while the RSD ranged in the area of 0.1-1.8%, depending on vanadium concentration. The method was successfully applied to the analysis of a wide variety of food samples, which are known to contribute to the dietary required amount of vanadium and to relevant biological matrixes. Reversing the conditions of the above reaction, the effect of the peroxy group on the vanadium-PTQA system was examined. The formation of a vanadyl complex was revealed which was suitable for the determination of hydrogen peroxide and peroxy acids. Linear calibration curves in the range of 0.2-50 microM for H2O2 and 0.1-2 microM for a respective peroxy acid were obtained, yielding detection limits of 0.05 and 0.03 microM, respectively.

Calibration↗
PubMed2003

Binuclear manganese compounds of potential biological significance. Part 2. Mechanistic study of hydrogen peroxide disproportionation by dimanganese complexes: the two oxygen atoms of the peroxide end up in a dioxo intermediate.

The dimanganese(II,II) complexes 1a [Mn(2)(L)(OAc)(2)(CH(3)OH)](ClO(4)) and 1b [Mn(2)(L)(OBz)(2)(H(2)O)](ClO(4)), where HL is the unsymmetrical phenol ligand 2-(bis-(2-pyridylmethyl)aminomethyl)-6-((2-pyridylmethyl)(benzyl)aminomethyl)-4-methylphenol, react with hydrogen peroxide in acetonitrile solution. The disproportionation reaction was monitored by electrospray ionization mass spectrometry (ESI-MS) and EPR and UV-visible spectroscopies. Extensive EPR studies have shown that a species (2) exhibiting a 16-line spectrum at g approximately 2 persists during catalysis. ESI-MS experiments conducted similarly during catalysis associate 2a with a peak at 729 (791 for 2b) corresponding to the formula [Mn(III)Mn(IV)(L)(O)(2)(OAc)](+) ([Mn(III)Mn(IV)(L)(O)(2)(OBz)](+) for 2b). At the end of the reaction, it is partly replaced by a species (3) possessing a broad unfeatured signal at g approximately 2. ESI-MS associates 3a with a peak at 713 (775 for 3b) corresponding to the formula [Mn(II)Mn(III)(L)(O)(OAc)](+) ([Mn(II)Mn(III)(L)(O)(OBz)](+) for 3b). In the presence of H(2)(18)O, these two peaks move to 733 and to 715 indicating the presence of two and one oxo ligands, respectively. When H(2)(18)O(2) is used, 2a and 3a are labeled showing that the oxo ligands come from H(2)O(2). Interestingly, when an equimolar mixture of H(2)O(2) and H(2)(18)O(2) is used, only unlabeled and doubly labeled 2a/b are formed, showing that its two oxo ligands come from the same H(2)O(2) molecule. All these experiments lead to attribute the formula [Mn(III)Mn(IV)(L)(O)(2)(OAc)](+) to 2a and to 3a the formula [Mn(II)Mn(III)(L)(O)(OAc)](+). Freeze-quench/EPR experiments revealed that 2a appears at 500 ms and that another species with a 6-line spectrum is formed transiently at ca. 100 ms. 2a was prepared by reaction of 1a with tert-butyl hydroperoxide as shown by EPR and UV-visible spectroscopies and ESI-MS experiments. Its structure was studied by X-ray absorption experiments which revealed the presence of two or three O atoms at 1.87 A and three or two N/O atoms at 2.14 A. In addition one N atom was found at a longer distance (2.3 A) and one Mn at 2.63 A. 2a can be one-electron oxidized at E(1/2) = 0.91 V(NHE) (DeltaE(1/2) = 0.08 V) leading to its Mn(IV)Mn(IV) analogue. The formation of 2a from 1a was monitored by UV-visible and X-ray absorption spectroscopies. Both concur to show that an intermediate Mn(II)Mn(III) species, resembling 4a [Mn(2)(L)(OAc)(2)(H(2)O)](ClO(4))(2), the one-electron-oxidized form of 1a, is formed initially and transforms into 2a. The structures of the active intermediates 2 and 3 are discussed in light of their spectroscopic properties, and potential mechanisms are considered and discussed in the context of the biological reaction.

Crystallography, X-Ray↗
PubMed1988

Efficacy and tolerance of a miconazole-benzoyl peroxide cream combination versus a benzoyl peroxide gel in the topical treatment of acne vulgaris.

62-65% reduction in the number of lesions was obtained in the treatment of 52 patients with acne vulgaris in this randomized single-blind study comparing a 5% benzoyl peroxide/2% miconazole cream (BPO-MCZ) with a 5% benzoyl peroxide gel (BPO). While BPO gel was equally effective in male and female patients (66 and 73% reduction of lesions), the BPO-MCZ cream was significantly more effective in the latter (50 vs. 74% mean reduction of lesions). Tolerance was significantly better with the BPO/MCZ cream preparation, particularly in females.

Acne Vulgaris↗
PubMed1990

Detection of myoglobin-derived radicals on reaction of metmyoglobin with hydrogen peroxide and other peroxidic compounds.

The reaction of metmyoglobin with equimolar concentrations of hydrogen peroxide has been studied using both electron spin resonance (e.s.r.) and optical spectroscopy. Using the former technique a strong anisotropic e.s.r. signal is observed, in the presence of the spin trap DMPO, which decays relatively rapidly. This previously unobserved signal, which is also observed on reaction of metmyoglobin with a number of other powerful oxidants (peracetic acid, 3-chloroperoxybenzoic acid, monoperoxyphthalic acid, iodosyl benzene, tBuOOH and cumene hydroperoxide) is assigned to a slowly-tumbling, metmyoglobin-derived, spin adduct. The parameters of this signal (aN 1.45, aH 0.83 mT) are consistent with the trapped radical having a heteroatom centre: this is believed to be oxygen. The concentration of this species is not affected by compounds such as 2-deoxyribose, mannitol and phenylalanine which are all efficient hydroxyl radical scavengers, demonstrating that the formation of this radical is not due to reaction of "free" HO. generated by breakdown of H2O2 by released iron ions. The concentration of this species is however decreased by desferal, ascorbate. Trolox C, salicylate and, to a lesser extent, linoleic acid; with the first three of these compounds further substrate-derived radicals are also observed. Examination of similar reaction systems (though in the absence of DMPO) by optical spectroscopy shows that the myoglobin (IV) species is formed and that this species behaves in a somewhat different manner with these added compounds. These results suggest that the radical trapped in the e.s.r. experiments is a myoglobin-derived species, probably a tyrosine peroxyl radical, arising from oxidative damage to the globin moiety. The diminution of both the e.s.r. signal of the spin adduct and the optical absorption of the myoglobin (IV) species in the presence of linoleic acid suggests that these myoglobin-derived species can initiate oxidative damage but that this process can be ameliorated by the presence of a number of water-soluble compounds such as ascorbate, Trolox C, desferal and salicylate.

Electron Spin Resonance Spectroscopy↗
PubMed1985

Comparative antioxidant enzyme study in freshwater fishes. I. Distribution of superoxide dismutase, peroxide-decomposing enzymes and lipid peroxidation in herbivorous fishes.

The activities of Cu,Zn-superoxide dismutase, Mn-superoxide dismutase, catalase and glutathione peroxidase were comparatively studied in organ homogenates from two herbivorous fishes, viz., the grass carp and the silver carp. 2. The protein contents and lipid peroxidation of organ homogenates were also compared. The comparative measurements primarily provide control values for subsequent toxicological examinations. 3. The highest total superoxide dismutase activities were found in the kidney, spleen and liver in the grass carp, and in the kidney and liver in the silver carp. 4. The antioxidant enzyme activities and other parameters of the organ homogenates appear to be independent of the feeding mode, but are rather characteristic of the fish variety.

Animals↗
PubMedDate not supplied

[Effect of hypochlorite and hydrogen peroxide on the ability of hemoglobin to stimulate lipid peroxidation of low density lipoproteins].

The ability of hemoglobin, modified by H2O2 or HOCl/OCl-, to induce lipid peroxidation (LPO) in low density lipoproteins (LDL) was studied, as well as the effects of haptoglobin. It was found that Hb modification by H2O2 or HOCl/OCl- increased generation of TBA-reactive substances in low density lipoproteins. Modified Hb was as double or more reactive compared to intact Hb. Free radical scavengers (ethanol and mannitol) gave no effect on LPO in LDL. On the other hand, ferric iron chelator desferrioxamine decreased LPO 5-6 times. Ferrous iron chelator- o-phenanthroline was effective only in the case of LPO, induced by H2O2 modified Hb. Haptoglobin (plasma protein forming complexes with Hb) decreased LPO induced by both intact or HOCl/OCl modified Hb. The results of the paper show that modification of Hb by H2O2 or HOCl/OCl- increase the ability of Hb to induce LPO in LDL, probably due to metHb, ferrylHb or free iron production.

Free Radical Scavengers↗