{"title":"Announcements and calendar","authors":"","doi":"10.1016/S0748-5514(86)80014-9","DOIUrl":"https://doi.org/10.1016/S0748-5514(86)80014-9","url":null,"abstract":"","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 4","pages":"Page 299"},"PeriodicalIF":0.0,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0748-5514(86)80014-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92139667","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Treatment of lymphocyte cultures with a hypoxanthine-xanthine oxidase system induces the formation of transferable clastogenic material","authors":"Ingrid Emerit , Shahid H. Khan , Peter A. Cerutti","doi":"10.1016/0748-5514(85)90029-7","DOIUrl":"10.1016/0748-5514(85)90029-7","url":null,"abstract":"<div><p>Culture medium of lymphocyte cultures that have been exposed to the superoxide generating system hypoxanthine plus xanthine oxidase (XXO) contains substances with chromosome damaging properties. This is demonstrated by the ability of ultrafiltrates of such culture media to induce chromosomal aberrations and sister chromatid exchanges in the lymphocytes of blood test cultures. Culture medium becomes active about 15 hours after the addition of XXO and stimulation by phytohemagglutinin. Concomitant with the accumulation of clastogenic material, assays for conjugated dienes and thiobarbituric acid-reactive material which measure lipid-peroxidation become positive in the culture media. When cells are pretreated with superoxide dismutase or glutathione peroxidase before the addition of XXO neither clastogenic substances nor lipid peroxidation products are detected. Catalase is a less efficient protector.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 1","pages":"Pages 51-57"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0748-5514(85)90029-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14146651","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Iron-induced lipid peroxidation in spinal cord: Protection with mannitol and methylprednisolone","authors":"Douglas K. Anderson , Eugene D. Means","doi":"10.1016/0748-5514(85)90030-3","DOIUrl":"10.1016/0748-5514(85)90030-3","url":null,"abstract":"<div><p>The ability of the free radical scavenger, mannitol, and the synthetic glucocorticoid, methylprednisolone sodium succinate (MPSS) to reverse the effects of iron catalyzed free radical induced lipid peroxidation was assessed in the feline spinal cord. Ferrous chloride (100 mM) was infused into the gray matter of lumbar spinal cord, the region frozen in situ, removed, and homogenates of the gray matter analyzed for activity of Na<sup>+</sup>, K<sup>+</sup>- ATPase and levels of malondialdehyde (MDA). ATPase activity had declined to approximately 30% of control by 2 h after FeCl<sub>2</sub> infusion and remained at this level through 24 h. Malondialdehyde values were elevated almost twofold at 2 h. Mannitol essentially reversed the effects of FeCl<sub>2</sub> infusion on Na<sup>+</sup>,K<sup>+</sup>-ATPase activity and MDA production. These results may implicate the hydroxyl radical (·OH), or an oxidizing species with ·OH-like reactivity, as the initiating radical species in this model of lipid peroxidation. Similarly, MPSS prevented the decline in spinal cord Na<sup>+</sup>, K<sup>+</sup>-ATPase activity and rise in MDA levels that were induced by FeCl<sub>2</sub> infusion. This demonstrated that at the dosage levels used in this study, MPSS was an effective antioxidant. This finding provides presumptive evidence suggesting that, at least in experimental animals, the effectiveness of MPSS in preventing the tissue necrosis and paralysis that is the sequelae of spinal cord trauma may reside, in part, in the capacity of this glucocorticord to quench peroxidative reactions in the injured tissue.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 1","pages":"Pages 59-64"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0748-5514(85)90030-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14146652","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Superoxide radical scavenging ability of centrophenoxine and its salt dependence in vitro","authors":"Imre Semsei, Imre Zs.-Nagy","doi":"10.1016/0748-5514(85)90153-9","DOIUrl":"10.1016/0748-5514(85)90153-9","url":null,"abstract":"<div><p>The superoxide radical scavenging ability of centrophenoxine (CPH) and its components (dimethylaminoethanol = DMAE, <em>p</em>-chlorophenoxyacetic acid = PCPA) was studied in vitro using the method of pyrogallol autoxidation, cytochrome c reduction and photoxidation of <em>o</em>-dianisidine in salt free assay media and in the presence of increasing NaCl or KCl concentrations. The CPH proved to be a superoxide radical scavenger in all three systems used, however, the rate constant for this reaction was rather low (1.7 × 10<sup>2</sup> M<sup>−1</sup> s<sup>−1</sup>). This scavenging ability decreased linearly with increasing ionic strength. DMAE and PCPA behaved in a somewhat contradictory manner. The former proved to be a weak superoxide radical generating compound being partially sensitive to the ionic strength. The latter showed either superoxide radical scavenging or generating effects on various assays depending on the actual salt concentrations of the media. On the basis of the results one has to assume that the superoxide radical scavenger ability of CPH may hardly be responsible for the in vivo effects of this compound, therefore, its OH· radical scavenger reactions the rate constant of which is about 10<sup>9</sup> M<sup>−1</sup> s<sup>−1</sup> (See Ref. 28.) may be of much greater importance.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 5","pages":"Pages 403-408"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0748-5514(85)90153-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14151019","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Michael P. Doyle, James G. Herman, Russell L. Dykstra
{"title":"Autocatalytic oxidation of hemoglobin induced by nitrite: Activation and chemical inhibition","authors":"Michael P. Doyle, James G. Herman, Russell L. Dykstra","doi":"10.1016/0748-5514(85)90019-4","DOIUrl":"10.1016/0748-5514(85)90019-4","url":null,"abstract":"<div><p>The nitrite ion is a direct causative agent for methomoglobinemia. Oxidation of hemoglobin to methemoglobin under aerobic conditionsis induced by nitrite, catalyzed by methomoglobin in the presence of hydrogen peroxide, and inhibited by chemical reagents ranging from cysteine and ascorbic acid to sulfite. The stoichiometry of nitrate production is dependent on the initial <span><math><mtext>[</mtext><mtext>NO</mtext><msub><mi></mi><mn>2</mn></msub><msup><mi></mi><mn>−</mn></msup><mtext>]</mtext><mtext>[</mtext><mtext>HbO</mtext><msub><mi></mi><mn>2</mn></msub><mtext>]</mtext></math></span> ratio, but reaches a limiting value of <span><math><mtext>1:1[</mtext><mtext>NO</mtext><msub><mi></mi><mn>3</mn></msub><msup><mi></mi><mn>−</mn></msup><mtext>]: [</mtext><mtext>Hb</mtext><msup><mi></mi><mn>+</mn></msup><mtext> </mtext><mtext>when</mtext><mtext> </mtext><mtext>[</mtext><mtext>NO</mtext><mtext>]</mtext><msub><mi></mi><mn>2</mn></msub><msup><mi></mi><mn>−</mn></msup><mtext>]</mtext><mtext>[</mtext><mtext>HbO</mtext><msub><mi></mi><mn>2</mn></msub><mtext>]</mtext><mtext> > 8</mtext></math></span>. Ascorbic acid is an exceptionally effective inhibitor for the autocatalytic oxidation, but its use does not affect the stoichiometry of nitrate formation. Sulfite reduces nitrate production to a level that is half that observed in its absence. These chemical inhibitors act upon the rapid autocatalytic stage for hemoglobin oxidation, but they do not influence the slow direct oxidation of hemoglobin by nitrite. The autocatalytic stage for hemoglobin oxidation results from nitrogen dioxide formed from nitrite through the peroxidase activity of methemoglobin. Peroxide and methemoglobin are formed during the initiation stage by electron transfer from nitrite that is kinetically first order in oxyhemoglobin and in nitrite.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 2","pages":"Pages 145-153"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0748-5514(85)90019-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14951597","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Mechanisms of lipid peroxidation","authors":"Albert W. Girotti","doi":"10.1016/0748-5514(85)90011-X","DOIUrl":"10.1016/0748-5514(85)90011-X","url":null,"abstract":"<div><p>This article provides an overview of how peroxidation of unsaturated lipids takes place and how it can be measured. Several different aspects of free-radical-mediated lipid peroxidation are discussed, including: (a) the catalytic role of chelated iron and other redox metal ions; (b) induction by reducing agents such as superoxide, ascorbate, and xenobiotic free radicals; (c) suppression by antioxidant chemicals and enzymes; and (d) how peroxidation that depends on pre-existing hydroperoxides (lipid hydroperoxide-dependent initiation of lipid peroxidation) can be distinguished from that which does not (lipid hydroperoxide-independent initiation of lipid peroxidation). Attention is also given to non-radical, singlet oxygen-driven peroxidation and how this can be resolved from radical-driven processes.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 2","pages":"Pages 87-95"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0748-5514(85)90011-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15028413","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Lipid peroxidation products and clastogenic material in culture media of human leukocytes exposed to the tumor promoter phorbol-myristate-acetate","authors":"Shahid H. Khan, Ingrid Emerit","doi":"10.1016/0748-5514(85)90159-X","DOIUrl":"10.1016/0748-5514(85)90159-X","url":null,"abstract":"<div><p>The chromosome-damaging effect of PMA in blood cultures is mediated by secondary products which are formed by the cells in response to the interaction with this tumor promoter. Since this effect could be influenced by antioxidant enzymes and by inhibitors of arachidonic acid metabolism, the present study was undertaken in order to determine whether the formation of these clastogenic substances is concomitant with the formation of AA metabolites and other lipid peroxidation products. Besides the clastogenic effect of ethyl-acetate extracts, the similarities of cytogenetic and biochemical results (conjugated dienes and TBA-reactive material) obtained for the influence of other blood cells than lymphocytes in the culture system, the importance of PHA stimulation and the protective effect of antioxidant enzymes were arguments in favour of a causal relationship between chromosome damage and lipid peroxidation (enzymatic or nonenzymatic). If AA release from membrane phospholipids was prevented by inhibition of phospholipase A<sub>2</sub>, neither conjugated dienes nor TBA-reactive material were found, and chromosome damage was reduced considerably. However, the results obtained with inhibitors of the cyclo- and lipoxygenase pathway were not conclusive, and discrepancies were also observed in the time course of appearance of clastogenic material and lipid peroxidation products.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 5","pages":"Pages 443-449"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0748-5514(85)90159-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15053760","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Steven W. Werns M.D. , Michael J. Shea M.D. , Benedict R. Lucchesi M.D., Ph.D.
{"title":"Free radicals in ischemic myocardial injury","authors":"Steven W. Werns M.D. , Michael J. Shea M.D. , Benedict R. Lucchesi M.D., Ph.D.","doi":"10.1016/0748-5514(85)90013-3","DOIUrl":"10.1016/0748-5514(85)90013-3","url":null,"abstract":"<div><p>Myrocardial ischemia causes release of chemotactic factors, migration of neutrophils, peroxidation of lipids, and depletion of free radical scavengers. The invading neutrophils may injure the myrocardial vasculature and sarcolemma by generating oxygen free radicals. Several agents that affect neutrophils or oxygen radicals were evaluated in a canine model of regional myocardial ischemia and reperfusion. Anesthetized dogs underwent occlusion and reperfusion of the left circumflex coronary artery. Infarct zone, area at risk infarction, and total left ventricle were quantified by gravimetric and planimetric analysis. Limitation of infarct size by ibuprofen was associated with marked suppression of leukocyte accumulation within the ischemic myocardium. Neutrophil depletion by antiserum resulted in similar reductions of infarct size and was accompanied by a reduction in leukocyte infiltration. A combination of oxygen radical scaverngers, superoxide dismutase plus catalase, decreased myocardial injury whether infusion began before occlusion or 75 min after occlusion. None of the treatments significantly altered hemodynamic indices of myocardial oxygen demand. Reduction of infarct size by ibuprofen, neutrophil antiserum, and free radical scavengers indicates that neutrophils and oxygen radicals participate in producing the irreversible damage to the myocardium during ischemia and reperfusion.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 2","pages":"Pages 103-110"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0748-5514(85)90013-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15053962","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Myoglobin-catalyzed hydrogen peroxide dependent arachidonic acid peroxidation","authors":"Matthew B. Grisham","doi":"10.1016/0748-5514(85)90122-9","DOIUrl":"10.1016/0748-5514(85)90122-9","url":null,"abstract":"<div><p>Hemeproteins promote lipid hydroperoxide-dependent lipid peroxidation in vitro. Only recently have studies demonstrated that certain hemeproteins peroxidize lipids in a lipid-hydroperoxide-independent manner. To understand fully the interaction between reactive oxygen metabolites, myoglobin and lipid, we investigate the possibility that myoglobin may use xanthine oxidase-generated superoxide and/or hydrogen peroxide to catalyze peroxidation of a polyunsaturated fatty acid. Our studies demonstrate that myoglobin, in the presence of hypoxanthine and xanthine oxidase, catalyze the peroxidation of arachidonic acid. Oxy (ferrous) myoglobin appears to be the most effective catalyst for arachidonic acid peroxidation when compared to metmyglobin, hemoglobin, or ADP-iron chelates. Inhibition studies reveal that myoglobin uses hydrogen peroxide, not superoxide to form either an oxo-heme-oxidant or caged radical that initiates arachidonate peroxidation. The reactivity of this oxidant is similar to that of ferryl iron or hydroxyl free radical. Our results suggest that this reaction may be important in myocardial reperfusion injury since reoxygenation of ischemic myocardium results in a burst of xanthine oxidase-generated superoxide and hydrogen peroxide in proximity to cellular myoglobin.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 3","pages":"Pages 227-232"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0748-5514(85)90122-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15053965","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}