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PubMed2002

Evaluation of antilipid peroxidative action of propolis ethanol extract.

The antilipid peroxidative action of the ethanol extract of Brazilian propolis at a concentration of 47% (w/v) was evaluated by examining the inhibitory effect of the extract on the formation of hydroperoxide- and endoperoxide-type lipid peroxides during heating of authentic polyunsaturated fatty acids and on Fe(3+)-ADP/ascorbic acid- and Fe(3+)-ADP/NADPH-dependent lipid peroxidation reactions in rat liver microsomes. Hydroperoxide-type lipid peroxides were measured by the haemoglobin-methylene blue method and endoperoxide-type lipid peroxides by the thiobarbituric acid (TBA), Fe(3+)-TBA and LPO-586 methods. Propolis ethanol extract inhibited dose-dependently the formation of hydroperoxide- and endoperoxide-type lipid peroxides during heating of linoleic acid, linolenic acid or arachidonic acid and the amount of the extract causing a half inhibition of these lipid peroxide formations ranged between 20 and 75 microg. Propolis ethanol extract inhibited dose-dependently both Fe(3+)-ADP/ascorbic acid- and Fe(3+)-ADP/NADPH-dependent lipid peroxidation reactions in rat liver microsomes when lipid peroxides produced in both reactions were measured by the TBA method. The amount of propolis extract causing a half inhibition of the Fe(3+)-ADP/ascorbic acid-dependent lipid peroxidation was about 5 microg, while that of the extract causing a half inhibition of the Fe(3+)-ADP/NADPH-dependent lipid peroxidation was about 0.15 microg. These results indicate that the propolis ethanol extract exerts an antilipid peroxidative action at very low doses.

Adenosine Diphosphate↗
PubMed1994

The role of glucose in cellular defences against cytotoxicity of hydrogen peroxide in Chinese hamster ovary cells.

The presence of glucose in the cellular environment influences the response of cells to hydrogen peroxide. This study examines the effect of glucose on clonogenic cell survival of Chinese hamster ovary cells exposed to micromolar concentrations of exogenous hydrogen peroxide. Exposure to hydrogen peroxide (20 mumol/10(7) cells) resulted in considerable cytotoxicity that was unaffected by the presence or absence of glucose. However, glucose protected the cells from killing induced by milder exposure (1 mumol/10(7) cells) to the oxidant causing a shift in the dose-response curve. This effect was considered in terms of glucose metabolism via the pentose phosphate cycle. A low nontoxic concentration of hydrogen peroxide (0.1 mumol/10(7) cells) markedly increased pentose phosphate cycle activity in normal cells. Clonogenic survival and activity of the cycle for cells depleted of total glutathione to about 8.6% of its initial value and/or with catalase activity reduced to about 10% of control levels were also determined. Neither of these modifications alone completely abolished the protective effect of glucose. Efficacy of glucose protection against cytotoxicity of hydrogen peroxide diminished in cells depleted of glutathione, and this was not accompanied by any detectable increase in pentose phosphate cycle activity above the control level. Cells depleted of catalase alone had a profile of survival and pentose phosphate cycle activity similar to that of control cells when exposed to hydrogen peroxide. Cells depleted of both glutathione and catalase were almost as sensitive to hydrogen peroxide as the cells incubated without glucose. They also did not express any detectable increase in pentose phosphate cycle activity. Survival of those cells, when exposed to hydrogen peroxide, was almost the same regardless if glucose was present or not. These results demonstrate an important role for the glutathione redox cycle, catalase, and the pentose phosphate cycle in protection against hydrogen peroxide in Chinese hamster ovary cells. They confirm the essential role of glucose and pentose phosphate cycle activity for the detoxification of hydrogen peroxide via the glutathione redox cycle. The data suggest that the ability of catalase to metabolise peroxide may also depend on metabolism of glucose via the pentose phosphate cycle. A clear understanding of the protective mechanisms in cells against hydrogen peroxide has many applications since this common reactive oxygen species is implicated in several pathophysiologies and in the action of certain chemotherapeutic drugs.

Amitrole↗
PubMed2003

Prospective comparison of hydrogen peroxide-enhanced three-dimensional endoanal ultrasonography and endoanal magnetic resonance imaging of perianal fistulas.

PURPOSE: This study was conducted to determine agreement between hydrogen peroxide-enhanced three-dimensional endoanal ultrasonography and endoanal magnetic resonance imaging in the preoperative assessment of perianal fistulas and to compare these results with the surgical findings. METHODS: Twenty-one patients (aged 26-71 years) with clinical symptoms of a cryptoglandular perianal fistula and a visible external opening underwent preoperative hydrogen peroxide-enhanced three-dimensional endoanal ultrasonography, endoanal magnetic resonance imaging, and surgical exploration. The results were assessed separately by experienced observers blinded as to each other's findings. Each fistula was described with notice of the following characteristics: classification of the primary fistula tract according to Parks (intersphincteric, transsphincteric, extrasphincteric, or suprasphincteric), horseshoe, or not classified; presence of secondary tracts (circular or linear); and location of an internal opening. RESULTS: The median time between hydrogen peroxide-enhanced three-dimensional endoanal ultrasonography and endoanal magnetic resonance imaging was 66 (interquartile range, 21-160) days; the median time between the last study (hydrogen peroxide-enhanced three-dimensional endoanal ultrasonography or endoanal magnetic resonance imaging) and surgery was 154 (interquartile range, 95-189) days. Agreement for the classification of the primary fistula tract was 81 percent for hydrogen peroxide-enhanced three-dimensional endoanal ultrasonography and surgery, 90 percent for endoanal magnetic resonance imaging and surgery, and 90 percent for hydrogen peroxide-enhanced three-dimensional endoanal ultrasonography and endoanal magnetic resonance imaging. For secondary tracts, agreement was 67 percent for hydrogen peroxide-enhanced three-dimensional endoanal ultrasonography and surgery, 57 percent for endoanal magnetic resonance imaging and surgery, and 71 percent for hydrogen peroxide-enhanced three-dimensional endoanal ultrasonography and endoanal magnetic resonance imaging in case of circular tracts and 76 percent, 81 percent, and 71 percent, respectively, in case of linear tracts. Agreement for the location of an internal opening was 86 percent for hydrogen peroxide-enhanced three-dimensional endoanal ultrasonography and surgery, 86 percent for endoanal magnetic resonance imaging and surgery, and 90 percent for hydrogen peroxide-enhanced three-dimensional endoanal ultrasonography and endoanal magnetic resonance imaging. CONCLUSIONS: For evaluation of perianal fistulas, hydrogen peroxide-enhanced three-dimensional endoanal ultrasonography and endoanal magnetic resonance imaging have good agreement, especially for classification of the primary fistula tract and the location of an internal opening. These results also show good agreement compared with surgical findings. Therefore, hydrogen peroxide-enhanced three-dimensional endoanal ultrasonography and endoanal magnetic resonance imaging can both be used as reliable methods for preoperative evaluation of perianal fistulas.

Adult↗
PubMed1993

Peroxide induces vasoconstriction in the human placenta by stimulating thromboxane.

OBJECTIVE: Placental lipid peroxides and thromboxane are abnormally increased in preeclampsia. Thromboxane is a potent vasoconstrictor of the placental vasculature. Peroxides stimulate cyclooxygenase (prostaglandin H synthase), and thereby could increase thromboxane, to cause vasoconstriction in the placenta. This study was performed to test the hypothesis that peroxides would produce vasoconstriction in the human placenta by stimulating thromboxane production. STUDY DESIGN: Isolated human placental cotyledons were perfused for 20-minute intervals with 100 mumol/L t-butyl hydroperoxide alone, and during and after perfusion with low-dose aspirin (5 x 10(-5) mol/L) (n = 6) or the thromboxane receptor blocker SQ 29,548 (n = 2). Krebs-Ringer-bicarbonate buffer gassed with 95% oxygen and 5% carbon dioxide was used for the perfusion buffer. Perfusion pressure was monitored continuously, and effluent flow rates were measured during each experimental treatment. Maternal and fetal effluent samples were analyzed for thromboxane B2 and 6-keto-prostaglandin F1 alpha. RESULTS: Compared with control Krebs-Ringer-bicarbonate buffer perfusion, peroxide perfusion significantly increased (p < 0.05) vascular resistance (14 +/- 2 vs 25 +/- 3 mm Hg.min/ml, mean +/- SE, respectively), thromboxane B2 secretion (fetal 0.20 +/- 0.04 vs 1.65 +/- 0.26 ng/min, maternal 4.8 +/- 1.5 vs 8.1 +/- 2.1 ng/min) and 6-keto-prostaglandin F1 alpha secretion (fetal 21 +/- 5 vs 60 +/- 1.8 pg/min, maternal nondetectable). Peroxide perfusion increased the thromboxane B2/6-keto-prostaglandin F1 alpha ratio threefold on the fetal side. Subsequent perfusion with aspirin significantly blocked the peroxide-induced vasoconstriction (13 +/- 1 mm Hg.min/ml during aspirin + peroxide) and the peroxide-induced increase in the secretion of thromboxane B2 (fetal 0.52 +/- 0.12 ng/min, maternal 2.0 +/- 0.3 ng/min) and 6-keto-prostaglandin F1 alpha (fetal 30 +/- 8 pg/min). After perfusion with aspirin the thromboxane B2/6-keto-prostaglandin F1 alpha ratio declined. When the thromboxane receptor blocker was used instead of aspirin, maternal and fetal secretion rates of thromboxane were still significantly increased by peroxide perfusion, but there was no change in perfusion pressure or vascular resistance. CONCLUSIONS: (1) Peroxide induces placental vasoconstriction coincident with increased secretion of thromboxane; (2) low-dose aspirin blocks both increased thromboxane secretion and vasoconstriction, whereas a thromboxane receptor antagonist allows increased thromboxane secretion but prevents peroxide induced vasoconstriction; (3) therefore, peroxide induces vasoconstriction by stimulating thromboxane synthesis.

6-Ketoprostaglandin F1 alpha↗
PubMed1988

Lipid peroxidation and phospholipase A2 activity in liposomes composed of unsaturated phospholipids: a structural basis for enzyme activation.

The effect of lipid peroxidation on membrane structure and phospholipase A2 activity was studied using liposomes composed of bovine liver phosphatidylcholine (PC) and phosphatidylethanolamine (PE). The phospholipids were mixed at set ratios and sonicated to yield small unilamellar vesicles. The liposome preparations were subjected to lipid peroxidation as induced by cumene hydroperoxide and hematin. Under these conditions, a sharp increase in lipid peroxidation was noted over a 30 min incubation period and was accompanied by loss of polyunsaturated fatty acids (PUFA). Liposomes enriched in PE were most extensively peroxidized with a preferred oxidation of this phospholipid. The extent of PC oxidation was also greater in liposomes containing the largest proportions of PE. Analysis of liposome anisotropy, via steady-state fluorescence polarization of diphenylhexatriene indicated that progressive increases in either PE content or the level of lipid peroxidation increased the apparent microviscosity of the vesicles. Moreover, lipid peroxidation increased anisotropy more effectively than variations in the ratios of PE vs. PC. Thus, peroxidation of 5-10% of the phospholipids produced the same anisotropy increase as a 20% increase in the ratio of PE vs. PC. Analysis of vesicle turbidity suggested that fusion was also more readily achieved through lipid peroxidation. When liposomes were incubated with 0.4 U/ml of snake venom phospholipase A2, a direct correlation was found between the degree of lipid peroxidation and the extent of phospholipid hydrolysis. The more unsaturated phospholipid, PE, was most extensively hydrolyzed following peroxidation. Increasing the proportion of PE also resulted in more extensive phospholipid hydrolysis. These findings indicate that lipid peroxidation produces a general increase in membrane viscosity which is associated with vesicle instability and enhanced phospholipase A2 attack. A structural basis for membrane phospholipase A2 activation as a consequence of lipid peroxidation is discussed in light of these findings.

Animals↗
PubMed1985

Enhancement of reactive oxygen-dependent mitochondrial membrane lipid peroxidation by the anticancer drug adriamycin.

Mitochondrial degeneration is a consistently prominent morphological alteration associated with adriamycin toxicity which may be the consequence of adriamycin-enhanced peroxidative damage to unsaturated mitochondrial membrane lipids. Using isolated rat liver mitochondria as an in vitro model system to study the effects of the anticancer drug adriamycin on lipid peroxidation, we found that NADH-dependent mitochondrial peroxidation--measured by the 2-thiobarbituric acid method--was stimulated by adriamycin as much as 4-fold. Marker enzyme analysis indicated that the mitochondria were substantially free of contaminating microsomes (less than 5%). Lipid peroxidation in mitochondria incubated in KCl-Tris-HCl buffer (pH 7.4) under an oxygen atmosphere was optimal at 1-2 mg of mitochondrial protein/ml and with NADH at 2.5 mM. Malonaldehyde production was linear with time to beyond 60 min, and the maximum enhancement of peroxidation was observed with adriamycin at 50-100 microM. Interestingly, in contrast to its stimulatory effect on NADH-supported mitochondrial peroxidation, adriamycin markedly diminished ascorbate-promoted lipid peroxidation in mitochondria. Superoxide dismutase, catalase, 1,3-dimethylurea, reduced glutathione, alpha-tocopherol and EDTA added to incubation mixtures inhibited endogenous and adriamycin-augmented NADH-dependent peroxidation of mitochondrial lipids, indicating that multiple species of reactive oxygen (superoxide anion radical, hydrogen peroxide and hydroxyl radical) and possibly trace amounts of endogenous ferric iron participated in the peroxidation reactions. In submitochondrial particles freed of endogenous defenses against oxyradicals, lipid peroxidation was increased 7-fold by adriamycin. These observations suggest that some of the effects of adriamycin on mitochondrial morphology and biochemical function may be mediated by adriamycin-enhanced reactive oxygen-dependent mitochondrial lipid peroxidation.

Animals↗
PubMed1995

Evidence for the activation of the signal-responsive phospholipase A2 by exogenous hydrogen peroxide.

The intracellular events that lead to arachidonic acid release from bovine endothelial cells in culture treated with hydrogen peroxide were characterized. The hydrogen peroxide-stimulated release of arachidonic acid was time- and dose-dependent, with maximal release achieved at 15 minutes after the addition of 100 microM hydrogen peroxide. Hydrogen peroxide-stimulated release of arachidonic acid was blocked with the phospholipase A2 inhibitor quinacrine. Treatment of the cells with hydrogen peroxide did not result in liberation of oleic acid, indicating that hydrogen peroxide exercised its effect on an arachidonate-specific phospholipase. Pretreatment of the cells with antioxidants, transition metal chelators, and hydroxyl radical scavengers did not affect the hydrogen peroxide-stimulated arachidonic acid release, indicating that the response to hydrogen peroxide is not oxygen radical-mediated. The response to hydrogen peroxide does not appear to be calcium-dependent, due to the following two observations: (a) No increase in intracellular calcium was seen upon exposure of the FURA2-loaded cells to hydrogen peroxide at concentrations sufficient to release arachidonic acid, and (b) no change in the release response was detected in cells loaded with the intracellular calcium chelator BAPTA. Significant inhibition of arachidonic acid release was seen when the cells were pretreated with inhibitors of protein kinase C, but not with inhibitors of tyrosine kinase. The results of these studies indicate that hydrogen peroxide-stimulated arachidonic acid release is mediated by a specific signal-responsive phospholipase A2, and that this process is not mediated via the actions of either lipid peroxidation or calcium but, rather, that a stimulation of intracellular kinase activity is necessary for this response.

Animals↗
PubMed2002

Inhibition of glyceraldehyde-3-phosphate dehydrogenase by peptide and protein peroxides generated by singlet oxygen attack.

Reaction of certain peptides and proteins with singlet oxygen (generated by visible light in the presence of rose bengal dye) yields long-lived peptide and protein peroxides. Incubation of these peroxides with glyceraldehyde-3-phosphate dehydrogenase, in the absence of added metal ions, results in loss of enzymatic activity. Comparative studies with a range of peroxides have shown that this inhibition is concentration, peroxide, and time dependent, with H2O2 less efficient than some peptide peroxides. Enzyme inhibition correlates with loss of both the peroxide and enzyme thiol residues, with a stoichiometry of two thiols lost per peroxide consumed. Blocking the thiol residues prevents reaction with the peroxide. This stoichiometry, the lack of metal-ion dependence, and the absence of electron paramagnetic resonance (EPR)-detectable species, is consistent with a molecular (nonradical) reaction between the active-site thiol of the enzyme and the peroxide. A number of low-molecular-mass compounds including thiols and ascorbate, but not Trolox C, can prevent inhibition by removing the initial peroxide, or species derived from it. In contrast, glutathione reductase and lactate dehydrogenase are poorly inhibited by these peroxides in the absence of added Fe2+-EDTA. The presence of this metal-ion complex enhanced the inhibition observed with these enzymes consistent with the occurrence of radical-mediated reactions. Overall, these studies demonstrate that singlet oxygen-mediated damage to an initial target protein can result in selective subsequent damage to other proteins, as evidenced by loss of enzymatic activity, via the formation and subsequent reactions of protein peroxides. These reactions may be important in the development of cellular dysfunction as a result of photo-oxidation.

Animals↗
PubMed1995

The inhibitory effect of 3-amino-1,2,4-triazole on relaxation induced by hydroxylamine and sodium azide but not hydrogen peroxide or glyceryl trinitrate in rat aorta.

1. In this study we investigated the role of catalase in relaxation induced by hydroxylamine, sodium azide, glyceryl trinitrate and hydrogen peroxide in isolated rings of rat aorta. 2. Hydrogen peroxide (1 microM-1 mM)-induced concentration-dependent relaxation of phenylephrine (PE)-induced tone in endothelium-containing rings. In endothelium-denuded rings, however, higher concentrations (30 microM-1 mM) of hydrogen peroxide were required to produce relaxation. The endothelium-dependent component of hydrogen peroxide-induced relaxation was abolished following pretreatment with N(O)-nitro-L-arginine methyl ester (L-NAME, 30 microM). L-NAME (30 microM) had no effect, however, on hydrogen peroxide-induced relaxation in endothelium-denuded rings. 3. Pretreatment of endothelium-denuded rings with catalase (1000 u ml-1) blocked relaxation induced by hydrogen peroxide (10 microM-1 mM). The ability of catalase to inhibit hydrogen peroxide-induced relaxation was partially blocked following incubation with 3-amino-1,2, 4-triazole (AT, 50 mM) for 30 min and completely blocked at 90 min. 4. Pretreatment of endothelium-denuded rings with methylene blue (MeB, 30 microM) inhibited relaxation induced by hydrogen peroxide (10 microM-1 mM), sodium azide (1-300 nM), hydroxylamine (1-300 nM) and glyceryl trinitrate (1-100 nM) suggesting that each acted by stimulation of soluble guanylate cyclase. 5. Pretreatment of endothelium-denuded rings with AT (1-50 mM, 90 min) to inhibit endogenous catalase blocked relaxation induced by sodium azide (1-300 nM) and hydroxylamine (1-300 nM) but had no effect on relaxation induced by hydrogen peroxide (10 microM-1 mM) or glyceryl trinitrate (1-100 nM). 6. In a cell-free system, incubation of sodium azide (10 microM-3 mM) and hydroxylamine (10 microM-30 mM) but not glyceryl trinitrate (10 microM-1 mM) with catalase (1000 u ml-1) in the presence of hydrogen peroxide (1 mM) led to production of nitrite, a major breakdown product of nitric oxide. AT (1-100 mM) inhibited, in a concentration-dependent manner, the formation of nitrite from azide in the presence of hydrogen peroxide. 7. These data suggest that metabolism by catalase plays an important role in the relaxation induced by hydroxylamine and sodium azide in isolated rings of rat aorta. Relaxation appears to be due to formation of nitric oxide and activation of soluble guanylate cyclase. In contrast, metabolism by catalase does not appear to be involved in the relaxant actions of hydrogen peroxide or glyceryl trinitrate.

Amitrole↗
PubMed1999

Concentration dependent effects of hydrogen peroxide on lens epithelial cells.

AIMS: To evaluate the effects of hydrogen peroxide exposure on the survival and proliferation of cultured lens epithelial cells. METHODS: TOTL-86 cells, a line of rabbit lens epithelial cells, were used. The survival and proliferation of TOTL-86 cells were quantified by a rapid colorimetric assay (MTT assay). To determine the effects of hydrogen peroxide, TOTL-86 cells were exposed to different concentrations of hydrogen peroxide. To determine the effect of cell numbers on the survival and proliferation of TOTL-86 cells at a fixed concentration of hydrogen peroxide, different numbers of cells were plated and exposed to hydrogen peroxide. To determine whether there is a synergistic effect between hydrogen peroxide and EGF, bFGF, PDGF-AA, and insulin, TOTL-86 cells were exposed to hydrogen peroxide combined with one of these growth factors. RESULTS: High levels (1 mM) of hydrogen peroxide killed TOTL-86 cells and sublethal levels (100 microM) suppressed their proliferation. From 1 nM to 1 microM of hydrogen peroxide, there was a dose dependent increase in the cell numbers. The initial seeded cell number dramatically affected the response to hydrogen peroxide. Although growth factors showed no synergistic effects with hydrogen peroxide on proliferation, both EGF and insulin, but not bFGF or PDGF, rescued TOTL-86 cells from the sublethal effect. CONCLUSION: Hydrogen peroxide in cooperation with some growth factors plays an important role in the proliferation of lens epithelial cell.

Animals↗
PubMed2006

[Establishment of DNA oxidative damage model in colorectal crypt cells by hydrogen peroxide].

OBJECTIVE: To induce DNA oxidative damage in colorectal crypt cells by hydrogen peroxide in vitro. METHODS: Hydrogen peroxide was diluted into 100, 50, 10, 5 and 1 micromol/L with RPMI 1640. Colorectal crypt cells were treated with peroxide for 10 min, 30 min, 1 h, 1.5 h, 12 h and 24 h respectively. The survival of colorectal crypt cell was measured by MTT method, and the DNA oxidative damage special product, 8-OhdG was detected with immunohistochemical staining. Liner regression was used to measure the time trend of survival rate with SPSS 10.0 software. RESULT: Survival rate of colorectal crypt cell was 60% and 80% after 10 min of hydrogen peroxide treatment. The longer treatment of hydrogen peroxide, the lower survival rate; the survival rate was reduced to 30% in 24 h. After 10 or 30 min treatment of 100 or 50 micromol/L hydrogen peroxide, the survival rates of colorectal crypt cells were reduced by 20% compared with those of 10, 5 and 1 micromol/L hydrogen peroxide. However, while cells were treated with different concentrations of hydrogen peroxide for 1.0 h or above, there were no differences in cell survival rates. The time trend test results demonstrated that the survival rates of colorectal crypt cells treated with 10, 5 and 1 micromol/L hydrogen peroxide were significantly decreased with the time length of treatment. Colorectal crypt cells treated with different concentrations of hydrogen peroxide for 15 minutes were positively stained brown in cytoplasm and nuclear by immunohistochemistry with 8-OhdG monoclonal antibody. CONCLUSION: Hydrogen peroxide could induce DNA oxidative damage in colorectal crypt cells. And treated with 1 - 10 micromol/L hydrogen peroxide for 10 - 30 min, DNA oxidative damage is apt to be induced in colorectal crypt cell.

Carbazoles↗
PubMed2001

Hydrogen peroxide decomposition in the oral cavity.

PURPOSE: To determine the clearance of hydrogen peroxide from the oral cavity of infants (3-4 yrs of age), juveniles (7-12 yrs of age), adults (35-66 yrs of age), and adults with impaired salivary flow (34-71 yrs of age). MATERIALS AND METHODS: In all subjects, the amount of H2O2 present in the oral cavity was assessed following a 1-min brushing period with an experimental dentifrice formulated with 3% hydrogen peroxide for up to 9 mins postbrushing. In addition, the oral clearance of 3% hydrogen peroxide delivered in an experimental dentifrice formulated with 5% baking soda was determined in a control population of adults and adult subjects with impaired salivary flow. RESULTS: Most of the hydrogen peroxide decomposed during brushing, with less than 30% of the prebrushing dose of hydrogen peroxide remaining in the oral cavity after 1 min of brushing. No differences between infants, juveniles, and adults were seen in levels of hydrogen peroxide recovered from the oral cavity after tooth brushing. When a mixture of hydrogen peroxide and baking soda was used for brushing, less than 5% of the hydrogen peroxide was recovered from the oral cavity after 1 min of brushing. In conclusion, clearance of hydrogen peroxide from the oral cavity was very rapid in children, adults, and adults with impaired salivary flow. Decomposition of hydrogen peroxide was enhanced approximately six-fold in adults by the presence of baking soda in the dentifrice. No substantial amount of hydrogen peroxide survived beyond the brushing period, and very little material would be present to interact with soft tissues in the oral cavity after expectorating any remaining dentifrice containing hydrogen peroxide.

Adolescent↗
PubMed1992

Membrane peroxidative damage enhancement by the ether lipid class of antineoplastic agents.

The ether lipid antineoplastic agents have no known interaction with DNA, but rather they appear to target membranes. The primary mechanism of action is unknown but effects on membrane biology are documented. We have studied the effect of two ether lipids on membrane lipids and examined the hypothesis that membrane peroxidative damage may be involved in their mechanism of action. With the use of cells having membranes enriched in polyunsaturated fatty acids of the omega-3 family of fatty acids, we have demonstrated that the prototypical ether lipid 1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphocholine and a thioether lipid analogue, 1-O-hexadecylmercapto-2-methoxymethyl-rac-glycero-3-phosphocholine , increase membrane lipid peroxidation and cytotoxicity in a time- and drug concentration-dependent manner. The oxidative cofactors Fe2+ and ascorbic acid were required. The pattern of cell death did not fully correspond to the peroxidation, since cofactors were required for peroxidation but not cytotoxicity. However, the rate of decrease in cell viability after exposure to the drug and cofactors corresponded to the peroxidation rate. In addition, when L1210 cells modified with the monounsaturated fatty acid oleic acid or unmodified cells were used, there was no ether lipid-enhanced peroxidation, and the cells were significantly less sensitive to the drug, with or without cofactors. The lipid-soluble antioxidant vitamin E inhibited 1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphocholine peroxidation and cytotoxicity in a concentration-dependent manner in the presence of cofactors but not consistently without them. Depletion of cellular glutathione content of L1210 cells using L-buthionine-(SR)-sulfoximine resulted in 40% augmentation of cofactor-facilitated cytotoxicity of 1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphocholine and a borderline effect on peroxidation. Another ether lipid, the thio compound 1-O-hexadecylmercapto-2-methoxymethyl-rac-glycero-3-phosphocholine , enhanced peroxidation in the presence of cofactors with kinetics corresponding to those of cytotoxicity. In the presence of ether lipid and cofactors the intensity of ascorbate free radical increased, consistent with oxidative stress. We conclude that the ether lipids stimulate membrane lipid peroxidation in a time- and drug concentration-dependent manner in the presence of oxidative cofactors. Even though peroxidation may not fully explain the cytotoxic effect of the ether lipid class of anticancer drugs, this observation provides further information on the nature of the membrane damage induced by the drugs. Since the ether lipids generate no known free radical intermediates directly, this suggests that membrane damage indirectly results in a process involving a peroxidative reaction.

Animals↗
PubMed2005

Sodium bicarbonate and hydrogen peroxide: the effect on the growth of Streptococcus mutans.

PURPOSE: This in vitro experiment studied the effects of sodium bicarbonate and hydrogen peroxide on the cariogenic bacteria Streptococcus mutans through analysis with a spectrophotometer. METHODS: The growth of S. mutans was analyzed using seven different environments. Twelve wells in each of the seven rows of a multi-well plate were used to incubate the test materials. In combinations of 10 microl distilled water, 100 microl broth, 10 microl 10% sucrose, 10 microl S. mutans, 10 microl 10% sodium bicarbonate, and 10 microl 3% hydrogen peroxide, seven different environments were created for testing. Environments had either sodium bicarbonate or hydrogen peroxide with S. mutans, or a combination of sodium bicarbonate and hydrogen peroxide with S. mutans. The plate was incubated at 37 degrees C and measured at 0, 18, 20, 22, 24, 26, 28, 30, and 42 hours by optical density with a spectrophotometer. RESULTS: Results showed bacterial growth was prevented by sodium bicarbonate, hydrogen peroxide, and the combination of sodium bicarbonate and hydrogen peroxide. Although hydrogen peroxide is bacteriocidal and sodium bicarbonate is bacteriostatic, there were no significant differences among the three treatment groups in spectrophotometer readings at any of the nine readings over 42 hours. CONCLUSION: There was no significant difference among the effects of hydrogen peroxide, sodium bicarbonate, or the sodium bicarbonate and hydrogen peroxide combination, as measured by optical density. The hydrogen peroxide, sodium bicarbonate, and the sodium bicarbonate and hydrogen peroxide combination prevented bacterial growth of S. mutans. The results show that products containing these agents have the ability to stop the growth of S. mutans. Products containing sodium bicarbonate and/or hydrogen peroxide may be useful to caries-prone patients. More studies are needed to confirm these results on patients.

Dentifrices↗
PubMed1986

Hydrogen peroxide enhances the activity of monoamine oxidase type-B but not of type-A: a pilot study.

The effect of hydrogen peroxide on monoamine oxidase (MAO) activity has been determined in homogenates of human brain areas taken postmortem. It could be shown that hydrogen peroxide enhances significantly the activity of MAO-B after short-term incubation (2 min), while no changes have been noted after long-term preincubation (60 min) indicating reversibility of this effect. MAO-A activity was not changed or decreased after preincubation with hydrogen peroxide. Freezing and thawing procedures did not change hydrogen peroxide stimulation of MAO in the caudate nucleus, while MAO-A activity dose dependently decreased. Inhibition of hydrogen peroxide stimulated MAO-B activity in human cortex by (-)deprenyl was found to be of similar potency compared to hydrogen peroxide free estimations. Glutathione, ascorbic acid and mannitol did not block MAO stimulation by hydrogen peroxide, while sodium azide led to a complete inhibition of hydrogen peroxide derived MAO activitation. Interorgan comparison showed increase of MAO-B activity in crude mitochondrial fractions of rat liver after preincubation with hydrogen peroxide, while with rat heart a reduction of MAO activity was detectable. As a conclusion these data indicate a possible role of hydrogen peroxide in the age-dependent increase of MAO-B in platelets and brain. Furthermore, increase of cytotoxic hydrogen peroxide via combined L-dopa therapy cannot be excluded to be of importance in the appearance of adverse reactions after long-term treatment with high doses. To reduce hydrogen peroxide production due to MAO activity, a combined treatment of L-dopa plus a selective MAO inhibitor and eventually additional administration of radical scavengers (ascorbic acid, vitamin E etc.) seems to be indicated.

Adult↗
PubMed2005

High levels of hydrogen peroxide in overnight tooth-whitening formulas: effects on enamel and pulp.

PURPOSE: Limited data are available to assess the safety of high levels of hydrogen peroxide in overnight tooth-whitening formulas. The purpose of this study was to assess the effects of hydrogen peroxide on enamel microhardness, pulp penetration, and enamel morphology. MATERIALS AND METHODS: Colgate Platinum Professional Overnight Whitening System (Colgate Oral Pharmaceuticals, Inc., Canton, MA, USA) (10% carbamide peroxide, equivalent to 3.5% hydrogen peroxide) was compared with two prototype formulations containing either 7.0% or 12.0% hydrogen peroxide. In the pulp chamber studies, human extracted teeth were exposed to 3.5%, 7.0%, or 12.0% hydrogen peroxide for 30 minutes, 4 hours, or 7 hours. Microhardness, electron spectroscopy for chemical analysis, and atomic force microscopy evaluations were made from enamel blocks cut from human extracted molars. The enamel blocks were evaluated following 14 7-hour treatments (98 h total). RESULTS: At 7 hours' post-treatment, hydrogen peroxide penetrated the pulp chamber at 23.12 +/- 10.09, 24.58 +/- 6.90, and 26.39 +/- 5.43 microg for 3.5%, 7.0%, and 12.0% hydrogen peroxide, respectively. With regard to enamel morphology, pulp penetration, microhardness, and elemental composition, no statistically significant differences were observed between treatment groups following 98 hours of treatment. CONCLUSIONS: Hydrogen peroxide does not adversely affect enamel morphology or microhardness. The levels recovered in pulp indicate that hydrogen peroxide is not expected to inhibit pulpal enzymes. CLINICAL SIGNIFICANCE: Overnight tray products containing levels of hydrogen peroxide of 3.5%, 7.0%, and 12.0% are not expected to adversely affect the enamel or pulpal enzymes. Additional safety studies are needed to assess the potential for tooth sensitivity and gingival irritation.

Analysis of Variance↗
PubMed2001

The quest for beryllium peroxides.

There is no experimental proof documented in the literature for the existence of any beryllium peroxide compound. All recent pertinent preparative attempts described in this work, using a range of beryllium salts with various peroxides as reagents under mild conditions, were equally unsuccessful. (1)H and (9)Be NMR investigations of aqueous solutions containing beryllium salts and hydrogen peroxide in a broad pH range also gave no definite evidence for the presence of peroxoberyllates as components of the manifold equilibria in such solutions. Quantum chemical calculations have therefore been carried out to delineate the energetics and structures of various beryllium peroxide model compounds. Standard Hartree-Fock and density functional methods were employed at various levels of sophistication. The series of prototypes considered consists of [BeOH](+), Be(OH)(2), Be(OH)(OOH), Be(OOH)(2), [Be(O(2))(2)](2-), [BeO(2)(OH(2))(2)], and [Be(2)(O(2))(2)(OH(2))(4)] (all in the gas phase). Surprisingly, the triatomic cation [BeOH](+) has been found to have a linear structure. All the Be-O(peroxide) bonds are found to be rather long, suggesting weaker bonding compared to the Be-O bonds in aquo, hydroxo, or oxo complexes. Hydrogen peroxide or anions derived therefrom are therefore not able to compete successfully with water (hydroxide anions) in aqueous solution. In the mononuclear beryllium peroxide molecules, the peroxide groups form chelating units at tetrahedrally 4-coordinate metal atoms. The binuclear compound [Be(2)(O(2))(2)(OH(2))(4)] has a puckered six-membered-ring structure, close to the standard chair conformation. A significant lengthening of the O-O bonds upon coordination to the Be(2+) centers has been calculated, but it is unlikely that the polarization of the peroxide group by the high positive charge density at Be(2+) is significant to cause an intrinsic instability of beryllium peroxides. All structures represent distinct local minima on the potential energy surface and are predicted to be (meta)stable species in nonaqueous media. The field of aluminum peroxides is a similar gray area on the map of metal and metalloid peroxides and is reminiscent of the well-established "diagonal-relation" of Be and Al in the periodic table of the elements.

Journal Article↗
PubMed2006

Ergosterol peroxide from an edible mushroom suppresses inflammatory responses in RAW264.7 macrophages and growth of HT29 colon adenocarcinoma cells.

BACKGROUND AND PURPOSE: 5alpha,8alpha-Epidioxy-22E-ergosta-6, 22-dien-3beta-ol (ergosterol peroxide) is a major antitumour sterol produced by edible or medicinal mushrooms. However, its molecular mechanism of action has yet to be determined. Here, we examine the anticancer and anti-inflammatory effects of ergosterol peroxide. EXPERIMENTAL APPROACH: After treating RAW264.7 macrophages with LPS and purified ergosterol peroxide or ergosterol, we determined LPS-induced inflammatory cytokines, nuclear DNA binding activity of transcription factors and phosphorylation of MAP kinases (MAPKs). HT29 colorectal adenocarcinoma cells were treated with ergosterol peroxide for 5 days. To investigate the antitumour properties of ergosterol peroxide, we performed DNA microarray and RT-PCR analyses and determined the reactive oxygen species (ROS) in HT29 cells. KEY RESULTS: Ergosterol peroxide suppressed LPS-induced TNF-alpha secretion and IL-1alpha/beta expression in RAW264.7 cells. Ergosterol peroxide and ergosterol suppressed LPS-induced DNA binding activity of NF-kappaB and C/EBPbeta, and inhibited the phosphorylation of p38, JNK and ERK MAPKs. Ergosterol peroxide down-regulated the expression of low-density lipoprotein receptor (LDLR) regulated by C/EBP, and HMG-CoA reductase (HMGCR) in RAW264.7 cells. In addition, ergosterol peroxide showed cytostatic effects on HT29 cells and increased intracellular ROS. Furthermore, ergosterol peroxide induced the expression of oxidative stress-inducible genes, and the cyclin-dependent kinase inhibitor CDKN1A, and suppressed STAT1 and interferon-inducible genes. CONCLUSION AND IMPLICATION: Our results suggest that ergosterol peroxide and ergosterol suppress LPS-induced inflammatory responses through inhibition of NF-kappaB and C/EBPbeta transcriptional activity, and phosphorylation of MAPKs. Moreover, ergosterol peroxide appears to suppress cell growth and STAT1 mediated inflammatory responses by altering the redox state in HT29 cells.

Adenocarcinoma↗