Journal of free radicals in biology & medicine最新文献

{"title":"Use of salicylate with high pressure liquid chromatography and electrochemical detection (LCE) as a sensitive measure of hydroxyl free radicals in adriamycin treated rats","authors":"Robert A. Floyd ,&nbsp;Richard Henderson ,&nbsp;Julia J. Watson ,&nbsp;Peter K. Wong","doi":"10.1016/0748-5514(86)90118-2","DOIUrl":"10.1016/0748-5514(86)90118-2","url":null,"abstract":"<div><p>Hydroxyl free radicals react with salicylate to form 2,3-dihydroxybenzoic acid (2,3-DHBA) and 2,5-dihydroxybenzoic acid (2,5-DHBA). Utilizing the technique of high pressure liquid chromatography with electrochemical detection (LCED), it is possible to detect DHBAs at the level of femtomoles. Since salicylate is relatively non-toxic, we have administered it as a trapping agent in a first attempt to examine the use of the LCED method as a sensitive measure of in vivo OH production. Utilizing adriamycin administration as a model to induce oxygen free radical tissue damage, we found that the level of DHBAs present in drug treated rats versus controls was increased 100-fold in heart and muscle, 30-fold in lung, and 3- and 4-fold in brain and blood, respectively. These first observations support the theory that adriamycin induced OH in tissue and indicates that the LCED method may prove to be useful to measure oxygen free radical production in vivo.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 1","pages":"Pages 13-18"},"PeriodicalIF":0.0,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0748-5514(86)90118-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14154813","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 in ocular inflammation: Human and experimental uveitis","authors":"Mitsunori Yamada ,&nbsp;Hitoshi Shichi ,&nbsp;Takenosuke Yuasa ,&nbsp;Yoshihito Tanouchi ,&nbsp;Yasuo Mimura","doi":"10.1016/S0748-5514(86)80059-9","DOIUrl":"10.1016/S0748-5514(86)80059-9","url":null,"abstract":"<div><p>A possible involvement of Superoxide in the pathogenesis of uveal inflammation in man and experimental animals was investigated. Superoxide production by the leukocytes of Behcet patients was significantly higher in the attack phase than in the remission phase. Leukocyte Superoxide generation was also enhanced in guinea pigs with S-antigen-induced experimental autoimmune uveoretinitis (EAU). If the animals were treated with Superoxide dismutase (SOD) at the onset of EAU, aqueous humor cell count was significantly lower than that of control (i.e., without SOD treatment). Infiltration of the inflammatory cells in the anterior retina was markedly reduced in SOD-treated animals. A similar protective effect of SOD against tissue damage was also observed in a bovine serum albumin-induced passive Arthus type uveitis in rabbits. These results suggest that Superoxide may play a role in causing tissue damage in animal models of ocular inflammation and possibly in Behcet disease.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 2","pages":"Pages 111-117"},"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)80059-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14161701","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":"Purity of catalase preparations: Contamination by endotoxin and its role in the inhibition of airway inflammation","authors":"Terry Gordon","doi":"10.1016/S0748-5514(86)80039-3","DOIUrl":"10.1016/S0748-5514(86)80039-3","url":null,"abstract":"","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 5","pages":"Pages 373-375"},"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)80039-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14169710","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":"Free-radical-mediated postischemic reperfusion injury in the kidney","authors":"Roman E. Ratych ,&nbsp;Gregory B. Bulkley","doi":"10.1016/S0748-5514(86)80030-7","DOIUrl":"10.1016/S0748-5514(86)80030-7","url":null,"abstract":"<div><p>Acute tubular necrosis is a frequent occurrence following hypovolemic shock and human renal transplantation. Although this postischemic injury was originally thought to result from ischemia alone, it has recently been recognized that significant tissue injury can occur during the period of reperfusion. The demonstration of the oxygen free-radical-mediated postischemic reperfusion injury by Granger, Rutili, and McCord in ischemic cat intestine suggested that this mechanism might also be operative following renal ischemia. In the kidney, postischemic injury results in necrosis of the proximal renal tubule and accumulation of erythrocytes in the outer renal medulla. It has been proposed that the primary event leading to these pathologic changes is a free-radical-mediated injury to the endothelial cells in the inner stripe of the outer medulla. Experimental evidence in animals subjected to warm and cold ischemia supports a free-radical-mediated mechanism. The clinical significance of these findings is demonstrated in preclinical animal studies of renal transplantation in which approximately two-thirds of the injury following cold ischemia could be ablated by superoxide dismutase administered just prior to reperfusion or by allopurinol when administered both at the time of preservation and reperfusion or at the time of preservation alone.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 5","pages":"Pages 311-319"},"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)80030-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14426779","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":"Halogenated hydrocarbon and hydroperoxide-induced peroxidation in rat tissue slices","authors":"Mitsuaki Sano,&nbsp;Paul A. Motchnik,&nbsp;Al L. Tappel","doi":"10.1016/0748-5514(86)90122-4","DOIUrl":"10.1016/0748-5514(86)90122-4","url":null,"abstract":"<div><p>Tissue slices were used to compare relative peroxidation capacity of bromotrichloromethane (BrCCl₃) and <em>t</em>-butyl hydroperoxide (BHP) by measurement of both peroxidation products and biochemical indices of damage. In liver and testes slices, BHP increased thiobarbituric acid reactive-substances (TBARS) and total aldehydes, measured as cyclohexanedione-reactive substances (CHDRS), to a greater extent than did an equimolar amount of BrCCl₃. GSH was decreased more by BHP than by BrCCl₃. Neither compound released lactate dehydrogenase or glutamic-pyruvicf transaminase from liver slices. Treatment of rats with cynamide, an aldehyde dehydrogenase inhibitor, increased the total CHDRS in liver slices and medium after incubation with BHP or BrCCl₃. HPLC of the CHDRS showed hexanal and propanal increased to the greatest extent. The hydroperoxide, BHP, which does not require metabolism to an active species, was a better initiator of peroxidation than the halogenated hydrocarbon, BrCCl₃, which must be metabolized to a radical species before it can initiate peroxidation.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 1","pages":"Pages 41-48"},"PeriodicalIF":0.0,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0748-5514(86)90122-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14889397","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":"Thioredoxin and glutaredoxin systems: Structure and function","authors":"Henry Jay Forman Ph.D.","doi":"10.1016/0748-5514(86)90128-5","DOIUrl":"https://doi.org/10.1016/0748-5514(86)90128-5","url":null,"abstract":"","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 1","pages":"Page 83"},"PeriodicalIF":0.0,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0748-5514(86)90128-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137344746","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":"Hemolysis and membrane lipid changes induced by xanthine oxidase in vitamin E deficient red cells","authors":"Hiroshi Tamai,&nbsp;Masayuki Miki,&nbsp;Makoto Mino","doi":"10.1016/0748-5514(86)90123-6","DOIUrl":"10.1016/0748-5514(86)90123-6","url":null,"abstract":"<div><p>A procedure to induce homolysis by the hypoxanthine-xanthine oxidase reaction was developed and applied to vitamin E deficient red blood cells (RBCs) in rats. The reaction system was as follows: 0. 16 mM hypoxanthine, 0.05 U/ml xanthine oxidase in 2.5% RBC suspensions with an isotonic buffer (pH 7.4) containing 10 mM phosphate buffer and 125 mM saline (227 mOsm). Hemolysis was observed to depend on the vitamin E concentrations in the RBCs. Hemolysis was inhibited by catalase but not by SOD. After the reaction with vitamin E deficient RBCs, an increase in TBARS in the aqueous phase of the reaction mixture was observed. This accompanied the increase in fluorescent substances in the lipid extracts, in associatioon with a significant decrease in the PE and PS of the RBCs, and a decrease in arachidonic acid in membrane lipids. The above changes were almost completely inhibited by tocopherol incorporated into vitamin E deficient RBCs.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 1","pages":"Pages 49-56"},"PeriodicalIF":0.0,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0748-5514(86)90123-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14154117","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":"Stimuli-induced superoxide radical generation in vitro by human alveolar macrophages from smokers: Modulation by n-acetylcysteine treatment in vivo","authors":"Hkan Bergstrand ,&nbsp;Anette Björnson ,&nbsp;Anders Eklund ,&nbsp;Roine Hernbrand ,&nbsp;Kjell Larsson ,&nbsp;Margareta Linden ,&nbsp;Annika Nilsson","doi":"10.1016/S0748-5514(86)80060-5","DOIUrl":"10.1016/S0748-5514(86)80060-5","url":null,"abstract":"<div><p>Bronchoalveolar lavage (BAL) was performed on nine healthy nonsmoking subjects and on 11 healthy smokers; in the last mentioned group lavage was performed before and after eight weeks treatment with N-acetyl-cysteine (NAC; 200 mg t.i.d.). The BAL cells were cultured for 2 h or overnight. Adherent cells were examined for their capacity to generate Superoxide radicals (determined by Superoxide dismutase (SOD)-inhibitable cytochrome C-reduction) at stimulation with phorbol 12-myristate 13-acetate (PMA), serum-treated zymosan (STZ), the calcium ionophore A23187, or the chemotactic tripeptide formyl-methionylleucylphenylalanine (FMLP). Cells from nonsmokers responded with a very low degree of O₂⨪-generation to any of the stimuli employed whether cultured for 2 h or overnight. Cells from smokers also responded with low O₂⨪-generation after 2 h of culture. However, cells from smokers cultured overnight responded with marked O₂⨪-generation to PMA and STZ but the responses to FMLP and A23187 were low. NAC-treatment of the smokers resulted in a reduced degree of both PMA- and STZ-induced O₂⨪-generation in five individuals. In two other subjects, PMA-induced (but not STZ-induced) O₂⨪-generation was reduced. Two individuals showed increased O₂⨪-generation to PMA- and to STZ-stimulation after NAC-treatment. Mean values of O₂⨪-generation induced by A23l87orby FMLP were significantly reduced for cells harvested after NAC-treatment. Mean values for PMA-induced O₂⨪ -generation also tended to be reduced by the treatment. We conclude that smoking leads to an increased capacity of alveolar adherent cells to generate O₂⨪ at appropriate stimulation and propose that treatment with NAC may reduce this capacity in a substantial number of the examined individuals.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 2","pages":"Pages 119-127"},"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)80060-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14161702","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":"Transferrin-dependent lipid peroxidation","authors":"Morio Saito ,&nbsp;Lee A. Morehouse ,&nbsp;Steven D. Aust","doi":"10.1016/S0748-5514(86)80057-5","DOIUrl":"10.1016/S0748-5514(86)80057-5","url":null,"abstract":"<div><p>The potential for iron bound to transferrin to be released and promote the peroxidation of phospholipid liposomes was investigated using ADP as a low molecular weight chelator and Superoxide generated by the xanthine/ xanthine oxidase system as the reducing agent. Lipid peroxidation in this system was dependent upon transferrin as the source of iron; increasing the transferrin concentration resulted in increased rates of lipid peroxidation. Increasing the xanthine oxidase activity also caused increased rates of peroxidation. Catalase stimulated rates of peroxidation at all xanthine oxidase activities tested. Conditions resulting in the most rapid release of iron from transferrin (low pH, high ADP) did not promote the greatest rates of lipid peroxidation, indicating that at neutral pH, rates of lipid peroxidation may be limited by the availability of iron. It is concluded that transferrin is not a likely source of iron for catalysis of deleterious biological oxidations such as lipid peroxidation in vivo.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 2","pages":"Pages 99-105"},"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)80057-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14162197","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":"Effect of degranulation on superoxide dismutase activity in human neutrophils","authors":"Trung Pham Huu ,&nbsp;Claude Marquetty ,&nbsp;Norma Amit ,&nbsp;Jacques Hakim","doi":"10.1016/S0748-5514(86)80072-1","DOIUrl":"10.1016/S0748-5514(86)80072-1","url":null,"abstract":"<div><p>Resting neutrophils possess cytosolic cyanide-sensitive (CNs) Superoxide dismutase (SOD) and cyanide-insensitive (CNi) SOD, located in an undefined organelle of the 27,000 g sedimentable fraction of its homogenate. Stimulated neutrophils generate large amounts of Superoxide anion, part of which is released in the extracellular medium and contributes to changes that occur in inflammatory foci. Our purpose was to assess whether or not the neutrophil upon stimulation secreted either or both CNs and CNi SOD activity, because the process could protect against the release of Superoxide anion. Human neutrophils stimulated in vitro with phorbol myristate acetate released 32.6% and 53% of their content in myeloperoxidase (an azurophilic granule marker) and vitamin B₁₂ binding activity, respectively. The CNi SOD was not secreted at all, whereas 16% and 23% of CNs SOD were released by resting and stimulated neutrophils, respectively. In contrast, lactate dehydrogenase, a cytosolic marker, was released by both resting and stimulated cells (∼-9%). These results suggest that CNi SOD is not located in the granules but in another organelle that does not degranulate upon stimulation and consequently does not protect against Superoxide anion formed by neutrophils in the extracellular medium. In contrast, CNs SOD is slightly but significantly released (<em>P</em> &lt;.02) and may be protective. Neutrophils from two patients with chronic granulomatous disease behaved similarly to control neutrophils but their content of both types of SOD was higher than that of the controls.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 3","pages":"Pages 213-217"},"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)80072-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14693703","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}