{"title":"Peroxidation of liposomes promoted by human polymorphonuclear leucocytes","authors":"Gunnar Carlin , Karl E. Arfors","doi":"10.1016/0748-5514(85)90158-8","DOIUrl":"10.1016/0748-5514(85)90158-8","url":null,"abstract":"<div><p>Human polymorphonuclear leucocytes were found to promote peroxidation of phospholipid liposomes upon stimulation by phorbol myristate acetate. Peroxidation required the presence of either pyrophosphate-chelated or ADP-chelated iron, whereas iron chelated to EDTA or ATP had no effect. Peroxidation was also catalyzed by ferritin, but not by transferrin. Superoxide dismutase abolished the peroxidation, whereas catalase and apparently also the hydroxyl radical scavenger dimethyl sulphoxide were inactive, indicating that the peroxidation was mediated by superoxide radicals but not by hydrogen peroxide or hydroxyl radicals. Xanthine oxidase-promoted peroxidation was studied for comparison and showed similar characteristics except that transferrin catalyzed the peroxidation. Peroxidation of membrane lipids may be a mechanism whereby granulocytes cause tissue damage in inflammation. The drugs paracetamol, gentisic acid and 5-aminosalicylic acid inhibited lipid peroxidation, probably through their ability to react with the superoxide anion.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 5","pages":"Pages 437-442"},"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)90158-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14151022","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}
Narsimha R. Nayini Ph.D. , Blaine C. White M.D. , Steven D. Aust Ph.D. , Raywin R. Huang Ph.D. , Richard J. Indrieri D.V.M. , A.Thomas Evans D.V.M. , Howard Bialek M.D. , William A. Jacobs M.D. , James Komara D.O.
{"title":"Post resuscitation iron delocalization and malondialdehyde production in the brain following prolonged cardiac arrest","authors":"Narsimha R. Nayini Ph.D. , Blaine C. White M.D. , Steven D. Aust Ph.D. , Raywin R. Huang Ph.D. , Richard J. Indrieri D.V.M. , A.Thomas Evans D.V.M. , Howard Bialek M.D. , William A. Jacobs M.D. , James Komara D.O.","doi":"10.1016/0748-5514(85)90014-5","DOIUrl":"10.1016/0748-5514(85)90014-5","url":null,"abstract":"<div><p>Assays for brain tissue malondialdehyde (MDA) and low molecular weight chelated (LMWC) iron were used to examine samples of the cerebral cortex obtained from dogs 2 h after resuscitation from a 15-min cardiac arrest. The effect of post-resuscitation treatment with lidoflazine and/or desferrioxamine was similarly examined. Non-ischemic brain samples had LMWC iron levels (in nmol/100 mg tissue) of 12.32 + 2.60 and MDA levels (in nmol/100 mg tissue) of 8.46 + 1.35. Animals subjected to cardiac arrest and resuscitation and standard intensive care (SIC) had LMWC iron levels of 37.04 +_4.58 (<em>p</em> < .01 against non-ischemic controls) and MDA levels of 12.24 + 1.9 (<em>p</em> < .05 against non-ischemic controls). All treatment interventions significantly reduced the LMWC iron (<em>p</em> < .05), but only treatment with desferrioxamine alone significantly reduced MDA (<em>p</em> < .05), although a trend toward reduction of the MDA was also evident in animals treated with both desferrioxamine and lidoflazine. LMWC iron levels are increased in the post-ischemic brain, and this increase may be related to lipid peroxidation in the brain following resuscitation from cardiac arrest. These changes are probably pathologic and are amenable to pharmacologic intervention.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 2","pages":"Pages 111-116"},"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)90014-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14951593","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":"Repair of tryptophan radicals by antioxidants","authors":"Slobodan V. Jovanovic, Michael G. Simic","doi":"10.1016/0748-5514(85)90016-9","DOIUrl":"10.1016/0748-5514(85)90016-9","url":null,"abstract":"<div><p>Oxidizing free radicals with redox potential greater than 1 V generate indole radicals, R-Ind<sup>⨥</sup> and R-Ind·, as in tryptophan. These resonance-stabilized free radicals can be repaired efficiently with electron donors (<em>k</em> = 5 × 10<sup>6</sup> − 1.3 × 10<sup>9</sup> dm<sup>3</sup> mol<sup>−</sup> s<sup>−</sup>) such as ascorbate, <em>N</em>,<em>N</em>,<em>N</em>′,<em>N</em>′-tetramethyl-<em>p</em>-phenylenediamine dihydrochloride (TMPD), and phenolic antioxidants. Sulfhydryl compounds, which are good H-atom donors, were found to be relatively unreactive (<em>k</em> < 10<sup>6</sup> dm<sup>3</sup> mol<sup>−1</sup>s<sup>−1</sup>). These indole radicals were also found to be unreactive with oxygen (<em>k</em> < 10<sup>6</sup> dm<sup>3</sup> mol<sup>−1</sup> s<sup>−1</sup>).</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 2","pages":"Pages 125-129"},"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)90016-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14951595","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":"Initial observations on the role of glutathione peroxidases in Euglena","authors":"Julie M. Overbaugh","doi":"10.1016/0748-5514(85)90117-5","DOIUrl":"10.1016/0748-5514(85)90117-5","url":null,"abstract":"<div><p>The algae <em>Euglena gracilis</em> possesses two glutathione (GSH) peroxidase: a GSH peroxidase that reduces organic hydroperoxides as well as hydrogen peroxide (GSH peroxidase 1); and a GSH peroxidase associated with GSH transferase that is active only with organic hydroperoxide substrates (GSH peroxidase 2). Preliminary experiments with <em>Euglena</em> were conducted to explore the in vivo role of the GSH peroxidases. The enzymes were not induced in response to the stimulation of cellular processes that generate oxidant species, such as β-oxidation or photosynthesis. The levels of GSH peroxidase 1 were approximately twofold higher in autotrophic cultures containing the herbicide DCMU. GSH peroxidase 1 was most active in stationary phase cells; while the levels of GSH peroxidase 2 were fairly constant throughout growth. Under conditions where lipid peroxidation was induced in <em>Euglena</em>, the addition of either GSH peroxidase plus GSH reduced the lipid peroxide levels more than tenfold.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 3","pages":"Pages 187-193"},"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)90117-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14951598","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":"Antipsoriatic drug action of anthralin: Oxidation reactions with peroxidizing lipids","authors":"F. Ducret, P. Lambelet, J. Löliger, M.-C. Savoy","doi":"10.1016/0748-5514(85)90135-7","DOIUrl":"10.1016/0748-5514(85)90135-7","url":null,"abstract":"<div><p>Reactions of anthralin with peroxidizing lipid were investigated. Using ESR spectroscopy and quantitative HPLC analysis radical species and decomposition products respectively were analysed in the reaction mixture as a function of time. Directly after mixing anthralin with peroxidized lipids, the 1,8-dihydroxy-9-anthron-10-yl radicals (primary radical) and small amounts of 1,8-dihydroxy-anthraquinone (AQ) were formed. After a few days of reaction, two secondary radicals were observed in addition to the primary radical. At the same time, 1,8,1′8′-tetrahydroxy-10,10′-bis-9(10H)-anthrone (DI) and an increasing amount of AO and other nonidentified decomposition products were found. As the reaction proceeded further on the amount of AQ and the nonidentified decomposition products increased, the primary radical disappeared (within about 40 d) and the concentration of DI decreased to zero (within 1 yr). Nonidentified decomposition products are tentatively assigned to polymeric degradation product (anthralin brown) formed from DI via the observed secondary radical species. These radical reactions of anthralin with peroxidized lipids help to elucidate speculations on radical type reactions of anthralin in psoriasis indications, e.g., the role of peroxidized skin lipids as radical reaction initiators.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 4","pages":"Pages 301-306"},"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)90135-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14952585","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":"Cutaneous thermal burn and oxidant-mediated acute lung injury: Appearance in serum of lung-related LDH isoenzyme","authors":"Thomas M. Annesley, Gerd O. Till, Peter A. Ward","doi":"10.1016/0748-5514(85)90154-0","DOIUrl":"10.1016/0748-5514(85)90154-0","url":null,"abstract":"<div><p>Previous studies from our laboratory have demonstrated that thermal injury to the skin of rats is associated with the production of oxygen radicals by complement-activated blood neutrophils, resulting in acute lung injury as demonstrated by increases in lung vascular permeability and morphological evidence of vascular endothelial cell damage, interstitial edema, and alveolar hemorrhage. In the present study, the analysis of sera from thermally injured rats reveals an isoenzyme profile for lactate dehydrogenase (LDH;EC 1.1.1.27) that is compatible with origin from lung. The appearance of LDH-4 isoenzyme in serum of thermally injured rats correlates linearly with indices of lung damage, supporting the results of previous studies suggesting that thermal trauma to the skin can cause oxygen radical production by complement-activated blood neutrophils with resultant acute microvascular injury in the lung interstitium. Furthermore, interventions that protect from oxidant-mediated lung injury (catase, scavengers of hydroxyl radical, iron chelators or neutrophil depletion) result in significant reductions in serum levels of the LDH-4 isoenzyme following thermal injury to the skin. Thus, measurements of LDH isoenzyme patterns in serum to be useful in monitoring tissue damage such as oxygen radical-mediated acute lung injury.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 5","pages":"Pages 409-414"},"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)90154-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15053759","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":"Oxygen radicals in complement and neutrophil-mediated acute lung injury","authors":"Gerd O. Till, Peter A. Ward","doi":"10.1016/0748-5514(85)90021-2","DOIUrl":"10.1016/0748-5514(85)90021-2","url":null,"abstract":"<div><p>The development of experimental acute lung injury following systemic complement activation is closely related to availability of blood neutrophils. Although tissue-destructive neutrophil-derived may play a supportive role in acute pulmonary injury, it appears that oxygen radical constitute the major neutrophil product responsible for acute damage of lung tissues and cells. Intravascular activation of neutrophils by the chemotactic complement peptide C5a is related to the generation os superoxide anion. Dismutation of superoxide to hydrogen peroxide and its iron-mediated conversion to hydroxyl radical appear to constitute in vivo events that ultimately lead to acute lung microvascular injury.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 2","pages":"Pages 163-168"},"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)90021-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15028412","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}
Robert A. Greenwald, Susan A. Moak, Steven E. Carsons, Scott Rush
{"title":"Inhibition of the proteolytic contaminant in commercial xanthine oxidase preparations by serum protein fractions","authors":"Robert A. Greenwald, Susan A. Moak, Steven E. Carsons, Scott Rush","doi":"10.1016/0748-5514(85)90160-6","DOIUrl":"10.1016/0748-5514(85)90160-6","url":null,"abstract":"<div><p>Commercial xanthine oxidase, widely used for generation of oxygen radicals in vitro, is usually contaminated by proteolytic activity, which limits its utility in studies of oxygen radical damage to protease sensitive substrates. An easily prepared fraction of fetal calf serum was found to inhibit virtually all of the proteolytic contaminant without affecting superoxide generation. The effects attainable with the “purified” enzyme were demonstrated with two protease sensitive targets: proteoglycan subunit from cartilage and fibronectin from human plasma.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"1 5","pages":"Pages 451-457"},"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)90160-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15029068","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}