{"title":"Photodamage to the lens in vitro: Implications of the Haber-Weiss reaction","authors":"S.D. Varma, J.M. Mooney","doi":"10.1016/0748-5514(86)90124-8","DOIUrl":"10.1016/0748-5514(86)90124-8","url":null,"abstract":"<div><p>Studies have been conducted to examine the implications of photochemical of O<sub>2</sub><sup>−</sup> and its derivatization to H<sub>2</sub>O<sub>2</sub> and OH· in the physiology of the lens in vitro. Physiological status was determined by measuring the uptake of rubidium by the intact tissue when cultured in riboflavin-containing medium, in dark and light, and in the presence and absence of various scanvengers. In the presence of light, the uptake of rubidium in the lens was greatly diminished; this suggests photodamage to the tissue. MnSOD and ferricyanide protected against this photochemical damage. The damaging process was thus initiated by the generation of O<sub>2</sub><sup>−</sup>. The tissue damage was also attenuated by catalase, ferrocyanide, and mannitol. These results, therefore, suggest the participation of hydrogen peroxide and the subsequent Haber-Weiss reaction in the photodamaging process.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 1","pages":"Pages 57-62"},"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)90124-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13577328","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}
Joanne Blondin , Vijaykumar Baragi , Edith Schwartz , James A. Sadowski , Allen Taylor
{"title":"Delay of uv-induced eye lens protein damage in guinea pigs by dietary ascorbate","authors":"Joanne Blondin , Vijaykumar Baragi , Edith Schwartz , James A. Sadowski , Allen Taylor","doi":"10.1016/S0748-5514(86)80010-1","DOIUrl":"10.1016/S0748-5514(86)80010-1","url":null,"abstract":"<div><p>Large accumulations of postsynthetically oxidized proteins are observed in the aged and cataractous eye lens. Ascorbate has previously been used to delay photooxidative damage in vitro. The goals of this study were (1) to confirm that dietary ascorbate can be used to enhance lens ascorbate levels and (2) to determine if lenses with enhanced ascorbate can better withstand photooxidative stress in the form of ultraviolet (UV) light exposure. Guinea pigs were placed on high dietary ascorbate (HDA), 50 mg/day, and low dietary ascorbate (LDA), 2 mg/day, for 21 weeks. Lenses from HDA animals were found to contain 3.3 times more ascorbate than LDA animals. Prior to irradiation, SDS-PAGE protein profiles and exopeptidase activity in HDA and LDA lens soluble proteins were indistinguishable. However upon exposure to UV light, more protein damage (e.g., high-molecular-weight aggregates and enhanced loss of exopeptidase activity) was seen in lens preparations from LDA as compared to HDA animals. These results suggest that ascorbate protects lens components against cataract-like and agerelated postsynthetic changes in vivo. As in previous tests on lens preparations, attenuated exopeptidase activity was observed before protein aggregation.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 4","pages":"Pages 275-281"},"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)80010-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14421706","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}
Gisela Witz , Nancy J. Lawrie , Alan Zaccaria , Herbert E. Ferran Jr.
{"title":"The reaction of 2-thiobarbituric acid with biologically active alpha, beta-unsaturated aldehydes","authors":"Gisela Witz , Nancy J. Lawrie , Alan Zaccaria , Herbert E. Ferran Jr.","doi":"10.1016/0748-5514(86)90121-2","DOIUrl":"10.1016/0748-5514(86)90121-2","url":null,"abstract":"<div><p>The standard assay for lipid peroxidation is the measurement of the pink, 532 n, absorbing chromogen which is formed upon reaction of 2-thiobarbituric acid (TBA) with the lipid peroxidation product malonaldehyde (MDA). The present studies indicate that the toxic lipid peroxidation product trans-4-hydroxynonenal and its dehydration product trans, trans-nonadienal react with TBA to form chromogens which absorb maximally at 530 and 532 nm, respectively. Other biologically active alpha, beta-unsaturated aldehydes, such as acrolein and crotonaldehyde, short-chain homologs of alkenals formed during lipid peroxidation, and trans,trans-muconaldehyde, a novel diene dialdehyde, react with TBA to form products which absorb maximally at 495 nm. The molar extinction coefficients of the aldehyde: TBA chromogens formed were found to vary widely, suggesting that only small contributions to the 532 nm absorption by TBA adducts of reactive aldehydes other than MDA may be encountered during the use of the TBA assay.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 1","pages":"Pages 33-39"},"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)90121-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14889396","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}
Décio L. Eizric , Mara A. de Lúcio , Antonio C. Boschero , Maria E. Hoffmann
{"title":"1, 10 Phenanthroline, a metal chelator, protects against alloxan- but not streptozotocin-induced diabetes","authors":"Décio L. Eizric , Mara A. de Lúcio , Antonio C. Boschero , Maria E. Hoffmann","doi":"10.1016/S0748-5514(86)80069-1","DOIUrl":"10.1016/S0748-5514(86)80069-1","url":null,"abstract":"<div><p>The iron chelator, 1,10-phenanthroline (Phen), which inhibits hydroxyl radical formation, was tested in vitro and in vivo against alloxan and streptozotocin (STZ) cytotoxicity. Phen injection reduced the severity of alloxan-induced diabetes in rats and attenuated alloxan-induced toxicity in human fibroblastas (VA 13 line) in culture. These protective effects were not observed against STZ toxic action. These results are consistent with the hypothesis that hydroxyl radicals, generated via an iron-catalyzed reaction, induce the alloxan but not the STZ diabetogenic effects.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 3","pages":"Pages 189-192"},"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)80069-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14165745","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}
Brooke T. Mossman, Joanne P. Marsh, David Hardwick, Rhonda Gilbert, Scot Hill, Ann Sesko, Marie Shatos, Jacqueline Doherty, Ann Weller, Michael Bergeron
{"title":"Approaches to prevention of asbestos-induced lung disease using polyethylene glycol (PEG)-conjugated catalase","authors":"Brooke T. Mossman, Joanne P. Marsh, David Hardwick, Rhonda Gilbert, Scot Hill, Ann Sesko, Marie Shatos, Jacqueline Doherty, Ann Weller, Michael Bergeron","doi":"10.1016/S0748-5514(86)80033-2","DOIUrl":"10.1016/S0748-5514(86)80033-2","url":null,"abstract":"<div><p>Asbestos-associated damage to cells of the respiratory tract in vitro can be prevented by the simultaneous addition of scavengers of active oxygen species to cultures. To determine if administration of scavenger enzymes to animals and humans is a plausible approach to the prevention of asbestos-induced lung disease, osmotic pumps were filled with various concentrations of PEG-coupled catalase and implanted subcutaneously into Fischer 344 rats over a 28-day period. At 3, 14, and 28 days after implantation of the pumps, the animals were evaluated for levels of catalase in serum and lung. In addition, lung tissue and lavage fluids were examined at 28 days for biochemical and morphologic indications of cell injury, inflammation, and fibrotic lung disease. At all time points examined, the administration of PEG-catalase caused a dosage-dependent increase in serum levels of catalase. The levels of lung catalase were evaluated at 28 days but not at earlier time periods. In comparison to control rats, the amounts of enzymes (lactic dehydrogenase, alkaline phosphatase), protein, and cells in lavage fluids from treated animals were unaltered. Moreover, the lungs showed no evidence of inflammation or fibrotic disease as determined by differential cell counts in lavage and measurement of hydroxyproline. These studies suggest that administration of PEG-catalase does not cause injury or other alterations in lung tissue and can be pursued as a feasible approach to prevention of asbestosis.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 5","pages":"Pages 335-338"},"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)80033-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14169709","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}
Krysztof Reszka, Pawel Kolodziejczyk, J. William Lown
{"title":"Horseradish peroxidase-catalyzed oxidation of mitoxantrone: spectrophotometric and electron paramagnetic resonance studies","authors":"Krysztof Reszka, Pawel Kolodziejczyk, J. William Lown","doi":"10.1016/0748-5514(86)90120-0","DOIUrl":"10.1016/0748-5514(86)90120-0","url":null,"abstract":"<div><p>The clinical anticancer agent mitoxantrone is subject to irreversible oxidation by hydrogen peroxide catalyzed by horseradish peroxidase (HRP). the characteristic absorption changes that result provide evidence for an initial metabolite which is futher oxidized enzymatically. The formation of the metabolite is accompanied by the concomitant generation of a free radical species detected by EPR spectroscopy. The intensity of the latter is dependent on the ratio mitoxantrone to oxidant as well as on the pH of the medium. The metabolite in its oxidized form is a strong electrophile and can be reduced by biologically and physiologically relevant electron donors including ascorbic acid, L-cysteine and reduced glutathione. The results establish a new facile metabolic conversion of this clinically useful anticancer agent that may be relevant to its mode of action.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 1","pages":"Pages 25-32"},"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)90120-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14154115","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":"Treatment of inflammatory arthritis with oxygen radical scavengers","authors":"Robert A. Greenwald (Chief of Rheumatology)","doi":"10.1016/S0748-5514(86)80037-X","DOIUrl":"10.1016/S0748-5514(86)80037-X","url":null,"abstract":"","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 5","pages":"Pages 367-368"},"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)80037-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14719407","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 dismutase: Rationale for use in reperfusion injury and inflammation","authors":"Joe M. McCord","doi":"10.1016/S0748-5514(86)80029-0","DOIUrl":"10.1016/S0748-5514(86)80029-0","url":null,"abstract":"","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 5","pages":"Pages 307-310"},"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)80029-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14719145","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":"Announcements and calendar","authors":"","doi":"10.1016/S0748-5514(86)80065-4","DOIUrl":"https://doi.org/10.1016/S0748-5514(86)80065-4","url":null,"abstract":"","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 2","pages":"Page 151"},"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)80065-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91694303","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":"Studies of the reactivity of trolox with Mn3+/Fe3+ complexes by pulse radiolysis","authors":"Diane E. Cabelli, Benon H.J. Bielski","doi":"10.1016/0748-5514(86)90126-1","DOIUrl":"10.1016/0748-5514(86)90126-1","url":null,"abstract":"<div><p>The rates and mechanisms for the reactions between Trolox (6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid), a synthetic analogue of α-tocopherol, Br<sub>1</sub><sup>−</sup> and Mn<sup>3+</sup>-phosphate were determined under aerobic and anaerobic conditions by fast kinetic methods. In addition, the reaction between Fe(OH)<sub>2</sub><sup>+</sup> and Trolox at pH 6.0 was shown not to occur under the conditions of the experiment, leading to a limiting rate for that reaction of <em>k</em> < 10<sup>3</sup>M<sup>−1</sup>s<sup>−1</sup>. These results are compared to studies of the reactivity of Trolox with HO<sub>2</sub>/O<sub>2</sub><sup>−</sup> and are discussed in light of the known antioxidant properties of vitamin E.</p></div>","PeriodicalId":77737,"journal":{"name":"Journal of free radicals in biology & medicine","volume":"2 1","pages":"Pages 71-75"},"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)90126-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14154118","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}