Organic peroxides, hydrogen peroxide, epoxides, and neoplasia.
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Carcinogens↗
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[Enzymic topography of the heart. 1. Activity of a 1.11.1.6. type peroxide: hydrogen peroxide oxidoreductase].
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Animals↗
Reduction of aflatoxin M1 in milk using hydrogen peroxide and hydrogen peroxide plus heat treatment.
Use of hydrogen peroxide (H2O2) under various conditions of temperature and time to inactivate aflatoxin M1 in artificially contaminated raw milk was examined. The degree of inactivation was measured by Enzym Linked Immunosorbent Assay (ELISA). It appeared that there is no change in the content of aflatoxin M1 in milk contained H2O2 and examined after 24 hours without heat treatment and in contaminated milk without add of H2O2 and heat treated treatment at (63 degrees C for 30 min, 75 degrees C for 15 sec) but slight inactivation (4.3%) was obtained in milk boiled for 5 min without H2O2. Maximum inactivation (27.8%, 28.8% and 45.1%) were obtained using 1% H2O2 followed by heat treatment at 36 degrees C for 30 min, 75 degrees C for 15 sec and boiling for 5 min respectively.
Aflatoxin M1↗
Effect of hydrogen peroxide on the initiation of microsomal lipid peroxidation.
Hydrogen peroxide reacts with reduced transition metals to generate the highly reactive hydroxyl radical (X OH), most often proposed as the predominant species for initiating microsomal lipid peroxidation. To assess the potential involvement of X OH, generated from hydrogen peroxide, in microsomal lipid peroxidation, we have altered the concentration of microsomal hydrogen peroxide and measured the resulting rates of malondialdehyde production. Hydrogen peroxide concentration in microsomes was changed by adding exogenous catalase, by washing to reduce both endogenous catalase activity and hydrogen peroxide-dependent glutathione oxidase activity, and by inhibiting endogenous catalase activity with azide in either the presence or absence of exogenous hydrogen peroxide. In only one instance was the rate of lipid peroxidation affected; exogenous hydrogen peroxide added to microsomes, previously incubated with azide, inhibited lipid peroxidation, the opposite effect from that predicted if X OH, generated from hydrogen peroxide, is actually the major initiating species. Neither these results, nor the inability of known X OH traps to inhibit microsomal lipid peroxidation, support the role of free hydrogen peroxide in the initiation of microsomal lipid peroxidation.
Animals↗
Impairment of brain mitochondrial function by hydrogen peroxide.
Hydrogen peroxide, at concentrations comparable to those observed under some pathological conditions, produced a concentration-dependent inhibition of state 3 (ADP-stimulated) and uncoupled mitochondrial respiratory activity. The ADP:O ratio was also substantially reduced. In contrast, the organic peroxide, t-butylhydroperoxide at the same concentrations produced no significant changes in respiratory activity. Intramitochondrial glutathione was oxidised to a similar extent in the presence of hydrogen peroxide or t-butylhydroperoxide. Thus, changes in this endogenous antioxidant apparently did not underlie the different responses to these peroxides. The effects of hydrogen peroxide were not altered by deferoxamine indicating that the extramitochondrial generation of hydroxyl radicals was not likely to be involved. However, modifications arising from the generation of hydroxyl radicals within the mitochondria remain a likely contributor to the observed deleterious effects on respiratory function. The inhibitory effects of hydrogen peroxide were greatest when pyruvate plus malate were present as respiratory substrates. Lesser inhibition was seen with glutamate plus malate and no significant inhibitory effects were detected in the presence of succinate. The findings suggest that mitochondrial components involved in pyruvate oxidation were particularly sensitive to the hydrogen peroxide treatment. However, no significant change was seen in activity of either the pyruvate dehydrogenase complex or NADH-ubiquinone oxidoreductase (complex I) when measured directly following treatment of the mitochondria with hydrogen peroxide.
Adenosine Diphosphate↗
Chemiluminescence intensities and spectra of luminol oxidation by sodium hypochlorite in the presence of hydrogen peroxide.
Hydrogen peroxide amplifies the chemiluminescence in the oxidation of luminol by sodium hypochlorite. A linear relationship between concentration of hydrogen peroxide and light intensity was found in the concentration range 5 x 10(-8)-7.5 x 10(-6) mol/l. At 7.5 x 10(-6) mol/l H2O2 the chemiluminescence is amplified 550-fold. The chemiluminescence spectra of these reactions have a wavelength maximum at 431 nm independent of the concentration of hydrogen peroxide. The results indicate that hydrogen peroxide is a necessary component in the chemiluminescent oxidation of the luminol by sodium hypochlorite.
Hydrogen Peroxide↗
[Gas embolism secondary to intraoperative use of hydrogen peroxide].
Hydrogen peroxide solution (H2O2) is used to irrigate and clean wounds. When applied to tissue hydrogen peroxide decomposes rapidly as a result of the action of catalases, releasing oxygen in the process. High pressure irrigation of the washing of closed cavities can cause serious complications. We report a case of gas embolism arising from the use of hydrogen peroxide during surgery for hydatidosis of the liver. A 64-year-old woman underwent surgery for removal of a hydatid cyst of the liver. When pressurized injection of 10 ml of 3% hydrogen peroxide was applied to the cystic cavity, cardiac arrhythmias were observed, a long with decreased PetCO2, hypotension and a "water mill" heart murmur. Gas embolism was suspected and treatment was instated immediately. Clinical course was good and without complications. We wish to warn against the potential dangers of using peroxide during surgery and of the importance of capnography for early diagnosis of gas embolism.
Embolism, Air↗
Occupational skin injury by hydrogen peroxide.
Hydrogen peroxide is widely used in products such as rocket fuel, bleaching preparations and topical disinfectants. Contact of hydrogen peroxide with the skin can cause severe skin damage. In this report, we describe a case of skin injury induced by hydrogen peroxide. The patient was a 34-year-old man working in a dry cleaning shop. While he was pouring 35% hydrogen peroxide, some of it accidentally splashed over his left shoulder and back, and then an erythema, purpura and vacuolar eruption, similar to bubble wrap, appeared on his left shoulder and down the left side of his back. Histologically, numerous vacuolar structures were observed in the epidermis, dermis and subcutaneous tissue. Coupled with the clinical features, these vacuolar structures were considered as 'oxygen bubbles'. Subcutaneous emphysema was detected by chest X-ray examination. All skin eruptions rapidly healed without scarring by using a steroid ointment. As far as we know, this is the first time such clinical and histological features have been described
Accidents, Occupational↗
Effect of carbamide peroxide and hydrogen peroxide on the surface morphology and zinc oxide levels of IRM fillings.
The effect of 10% carbamide peroxide or 10% hydrogen peroxide on the surface morphology and zinc oxide levels of IRM fillings was tested. Ninety IRM samples were treated with either 10% carbamide peroxide, 10% hydrogen peroxide or phosphate buffer which served as control. Treatment consisted of placing the samples in a dry incubator at 37 degrees C for 1, 3 or 7 days. At each time point, the samples were removed from the test solutions, dried and prepared for surface scanning electron microscopy and energy dispersive spectrometric analysis. After 3 days, 10% carbamide peroxide significantly reduced the zinc oxide levels as compared to the 10% hydrogen peroxide group (<0.01) and the controls (p<0.01). 10% hydrogen peroxide reduced the zinc oxide levels similarly to the control. No significant changes in the zinc oxide levels were found between 3 and 7 days in any of the groups tested. Microscopy examination of the carbamide peroxide group revealed granular surface with well defined crystalline areas. In the hydrogen peroxide group, numerous cracks with multiple sun burst-like areas were found. At the macroscopic level, the samples of this group appeared cracked and more swollen, as compared to controls and samples treated with carbamide peroxide. In conclusion, both 10% carbamide peroxide and 10% hydrogen peroxide altered the surface morphology and the zinc oxide levels of IRM fillings, but their modes of action differed.
Carbamide Peroxide↗
[Oxygen embolism after intraoperative use of hydrogen peroxide].
Hydrogen peroxide is widely used for irrigation of surgical wounds. However, its administration has been associated with gas embolism. We report a case of gas embolism after wound irrigation with hydrogen peroxide in a 11-year-old boy undergoing extraction of the extra-traumatic splint under general anesthesia. When 3% hydrogen peroxide 12 ml was applied to wound of the left femur after extraction of the splint, the patient showed clinical signs of pulmonary embolism. Symptomatic treatment was initiated immediately. When the patient awoke from anesthesia, he showed tonic convulsion. But he recovered without any complications. The administration of hydrogen peroxide into a closed tissue is contraindicated during surgery.
Anesthesia, General↗
Activation of complement in normal serum by hydrogen peroxide and hydrogen peroxide-related oxygen radicals produced by activated neutrophils.
Neutrophils activated by soluble particulate stimuli generate superoxide anion and subsequently form hydrogen peroxide and other oxygen radicals. The effect of hydrogen peroxide on the complement system in normal serum was investigated. Treatment of normal serum with hydrogen peroxide resulted in a diminution of the haemolytic activity of the total and alternative complement pathways and the haemolytic titres of C3 and C5 but not of C2, in normal serum. These decreases in complement activity depended on the concentration of hydrogen peroxide added to the serum. Immunoelectrophoretic analysis of hydrogen peroxide-treated serum showed that C3 and C5 proteins were activated. Complement degradation products C3a and C5a were produced in normal serum treated with hydrogen peroxide, and 20 mM EDTA abolished C3a and C5a production in hydrogen peroxide-treated serum but 20 mM Mg-EGTA did not. Catalase completely abolished and dimethylsulphoxide and D-mannitol, hydroxyl radical scavengers, partially inhibited the hydrogen peroxide-mediated complement activation. Hypochlorite, incubated with normal serum, significantly inhibited serum haemolytic activity, and sodium thiosulphate, a reducing agent, abolished the effect of hypochlorite. Normal serum incubated with activated neutrophils showed neutrophil chemotactic activity and decreased serum haemolytic activity, and the addition of catalase or methionine (5 mM) completely abolished the effects of activated neutrophils. These results suggest that hydrogen peroxide activates complement via an alternative pathway of complement activation and that hydroxyl radicals and other hydrogen peroxide-related species such as hypochlorite are most likely involved in hydrogen peroxide-mediated complement activation. Complement activation by oxygen radicals produced by activated neutrophils may be one of the mechanisms by which complement is activated in human immune complex diseases.
Complement Activation↗
Specific modification of two tryptophans within the nuclear-encoded subunits of bovine cytochrome c oxidase by hydrogen peroxide.
Hydrogen peroxide does more than react with the binuclear center of oxidized bovine cytochrome c oxidase and generate the well-characterized "peroxy" and "ferryl" forms. Hydrogen peroxide also inactivates detergent-solubilized cytochrome c oxidase in a time- and concentration-dependent manner. There is a 70-80% decrease of electron-transport activity, peroxidation of bound cardiolipin, modification of two nuclear-encoded subunits (IV and VIIc), and dissociation of approximately 60% of subunits VIa and VIIa. Modification of subunit VIIc and dissociation of subunit VIIa are coupled events that probably are responsible for the inactivation of cytochrome c oxidase. When cytochrome c oxidase is exposed to 500 microM hydrogen peroxide for 30 min at pH 7.4 and room temperature, subunits IV (modified up to 20%) and VIIc (modified up to 70%) each have an increased mass of 16 Da as detected by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and electrospray ionization mass spectrometry. In each case, the increased mass is caused by oxidation of a tryptophan (Trp19 within subunit VIIc and Trp48 within subunit IV), almost certainly due to formation of hydroxytryptophan. We conclude that hydrogen peroxide-induced oxidation of tryptophan and cardiolipin proceeds via the binuclear center since both modifications are prevented if the binuclear center is first blocked with cyanide. Bound cardiolipin and oxidized tryptophans are localized relatively far from the binuclear center (30-60 A); therefore, oxidation probably occurs by migration of a free radical generated at the binuclear center to these distal reaction sites.
Animals↗
Oral ulcerations with use of hydrogen peroxide.
Hydrogen peroxide has been advocated for many years as an oral rinse useful in control of various oral conditions. Several authorities, however, have suggested that this material may be harmful to oral tissues, especially if the tissues have been previously injured. This article presents two case reports demonstrating harmful oral effects from hydrogen peroxide rinses. The findings suggest that oral hygiene techniques emphasizing the use of 3% hydrogen peroxide in periodontal therapy may require reevaluation.
Adult↗
Changes in surface levels of mercury, silver, tin, and copper of dental amalgam treated with carbamide peroxide and hydrogen peroxide in vitro.
OBJECTIVES: The effect of 10% carbamide peroxide or 10% hydrogen peroxide on the surface levels of mercury, silver, tin, and copper of amalgam fillings was tested in vitro with scanning electron microscopy and energy dispersive spectrometric microanalysis. STUDY DESIGN: Samples of amalgam were treated for 14 and 28 days with either 10% carbamide peroxide or 10% hydrogen peroxide solutions and compared with phosphate buffer controls. RESULTS: A significant increase in mercury levels occurred after treatment with carbamide peroxide for 14 days (p < 0.01) and 28 days (p < 0.001) and after treatment with hydrogen peroxide for 28 days (p < 0.001). A significant increase in silver levels occurred after treatment with carbamide peroxide for 14 days (p < 0.05) and 28 days (p < 0.01) and subsequent to treatment with hydrogen peroxide for 14 days (p < 0.05) and 28 days (p < 0.001). A significant reduction in tin levels occurred after treatment with hydrogen peroxide for 14 days (p < 0.01) and 28 days (p < 0.001), and after treatment with carbamide peroxide for 28 days (p < 0.01). A significant reduction in copper levels was found after treatment with carbamide peroxide for 14 days (p < 0.05). CONCLUSIONS: It appears that prolonged treatment with bleaching agents may cause microstructural changes in amalgam surfaces, possibly increasing exposure of patients to toxic byproducts.
Carbamide Peroxide↗
Cytotoxicity and dentin permeability of carbamide peroxide and hydrogen peroxide vital bleaching materials, in vitro.
There has been recent concern about the inadvertent exposure of dentin with patent tubules as well as gingiva to bleaching systems containing 10-15% carbamide peroxide or 2-10% hydrogen peroxide for more than a few minutes. The aims of the present study were: (1) to determine the cytotoxicity of dilutions of hydrogen peroxide in cell culture; (2) to measure hydrogen peroxide diffusion from bleaching agents through dentin in vitro; and (3) to determine the risk of hydrogen peroxide-induced cytotoxicity from exposure of dentin to these vital bleaching agents. The 50% inhibitory dose (ID50) of hydrogen peroxide to succinyl dehydrogenase activity in cultured cells was found to be 0.58 mmol/L after 1 h. All bleaching materials demonstrated diffusion of hydrogen peroxide through dentin in an "in vitro pulp chamber" device. The one- and six-hour diffusates of all bleaching agents through 0.5-mm dentin exceeded the ID50 in monolayer cultures. Inhibition of succinyl dehydrogenase activity corresponded to the amount of hydrogen peroxide that can rapidly diffuse through dentin in vitro and reach concentrations which are toxic to cultured cells in less than 1 h.
3T3 Cells↗
Ionic and radical oxidations of DNA by hydrogen peroxide.
Hydrogen peroxide mediated oxidation of 2'-deoxyadenosine and isolated DNA was investigated. Reaction of hydrogen peroxide with 2'-deoxyadenosine under non radical conditions led to the formation of a predominant decomposition product. This was identified as 2'-deoxyadenosine N-1-oxide on the basis of detailed 1H and 13C NMR analysis and further confirmed by photolysis experiments. Quantitative determination of both radical and ionic DNA type damage was based on the use of a 32P-postlabeling method (5-hydroxymethyluracil and adenine N-1-oxide) and of an HPLC-EC assay (8-hydroxyguanine). Adenine N-1-oxide was shown to be the predominant ionic DNA base damage under non radical conditions. The presence of Fe(II)-DTPA complex in the reaction medium led to a reduction in the amount of adenine N-1-oxide by a factor of 4 whereas radical DNA type damages including 8-hydroxyguanine and 5-hydroxymethyluracil was increased by a factor of 2-3.
Animals↗
The induction/loss of the oxidant-resistant phenotype of Chinese hamster ovary (CHO) cell variants does not correlate with sensitivity to DNA single strand breakage by hydrogen peroxide.
Hydrogen peroxide resistant variants of Chinese hamster ovary (CHO) cells characterized by different levels of resistance to growth inhibition induced by the oxidant displayed a decreased susceptibility to the induction of DNA single strand breakage by hydrogen peroxide. Resistance to DNA damage, however, was maximal in cells resistant to killing by low concentrations of H2O, and did not increase further in cells characterized by a much higher resistance to the toxic action of the oxidant. Different sensitivities to the induction of DNA single strand breakage observed in wild type and resistant sublines were related to a decreased susceptibility/differential depletion of H2O2, rather than being dependent on different velocities in DNA repair processes. Growth of resistant cells in the absence of H2O2 resulted in a rapid loss of resistance to induction of DNA strand scission by H2O2. Cells retained resistance to the growth-inhibitory effect of the oxidant under conditions where resistance to the production of DNA single strand breaks was lost. Experiments aimed at elucidating the molecular basis for resistance to DNA damage induction by H2O2 have demonstrated that this effect is dependent upon the catalase activity of the specific sublines as well as on their different total protein content.
Animals↗
Effects of vitamin E on the platelet aggregation induced by combined adenosine diphosphate and hydrogen peroxide.
Hydrogen peroxide can either induce or inhibit or enhance the platelet aggregation in vitro depending upon the experimental conditions. Vitamin E and vitamin E-nicotinate are found to be effective to inhibit, to some extent, the platelet aggregation induced by combined adenosine diphosphate (ADP) and hydrogen peroxide (H2O2), added simultaneously, to the platelet rich plasma (PRP). Vitamin E and vitamin E-nicotinate seemed, however, to be unable to prevent the reduction of platelet response to ADP, which was brought about by the pretreatment of PRP with H2O2 of a lower concentration.
Adenosine Diphosphate↗