ALTERATIONS IN CARDIAC CONTRACTILE PROTEINS DUE TO OXYGEN FREE RADICALS
作者： Shingo Suzuki , Masanori Kaneko , Donald C. Chapman , Naranjan S. Dhalla
DOI: 10.1016/0304-4165(91)90045-I
关键词: Superoxide 、 Xanthine 、 Catalase 、 Biochemistry 、 Superoxide dismutase 、 Xanthine oxidase 、 Hypochlorous acid 、 Chemistry 、 DTNB 、 ATPase
摘要: In view of the potential role free radicals in genesis cardiac abnormalities under different pathophysiological conditions and importance contractile proteins determining heart function, this study was undertaken to examine effects oxygen on rat myofibrils. Xanthine plus xanthine oxidase (X + XO) which is known generate superoxide anions (O 2 − ) hydrogen peroxide (H O ), an activated species oxygen, found decrease Ca 2+ -stimulated ATPase activity, increase Mg -ATPase activity reduce sulfhydryl (SH) group contents myofibrils; these were completely prevented by dismutase (SOD) catalase (CAT). Both H hypochlorous acid (HOCl), oxidant, produced actions myofibrils similar those observed X XO. The HOCl CAT l -methionine, respectively. N -ethylmaleimide (NEM) 5,5′-dithiobis(2-nitrobenzoic acid) (DTNB), inhibitors SH groups, also seen with Dithiothreitol (DTT), a well sulfhydryl-reducing agent, XO, , HOCl, NEM DTNB. These results suggest that marked changes myofibrillar activities may be mediated oxidation groups.
sci-hub.se 参考文章(31)
J D Crapo, B A Freeman, Biology of disease: free radicals and tissue injury. Laboratory Investigation. ,vol. 47, pp. 412- 426 ,(1982)
J P Reeves, C A Bailey, C C Hale, Redox modification of sodium-calcium exchange activity in cardiac sarcolemmal vesicles. Journal of Biological Chemistry. ,vol. 261, pp. 4948- 4955 ,(1986) , 10.1016/S0021-9258(19)89197-4
Hertha H. Taussky, Ephraim Shorr, Gloria Kurzmann, A microcolorimetric method for the determination of inorganic phosphorus. Journal of Biological Chemistry. ,vol. 202, pp. 675- 685 ,(1953) , 10.1016/S0021-9258(18)66180-0
A. Lewis Farr, Oliver H. Lowry, Rose J. Randall, Nira J. Rosebrough, Protein Measurement with the Folin Phenol Reagent Journal of Biological Chemistry. ,vol. 193, pp. 265- 275 ,(1951)
Terrence R. Green, Jack H. Fellman, Alisa L. Eicher, Myeloperoxidase oxidation of sulfur-centered and benzoic acid hydroxyl radical scavengers. FEBS Letters. ,vol. 192, pp. 33- 36 ,(1985) , 10.1016/0014-5793(85)80037-5
Laimonis Gailis, Winifred G. Nayler, Sian E. Harding, Reversible elimination of myofibrillar Ca2+ sensitivity by diamide and other sulfhydryl reagents: comparison with reversible contracture produced in intact cells. Canadian Journal of Physiology and Pharmacology. ,vol. 68, pp. 1170- 1175 ,(1990) , 10.1139/Y90-175
S R Jolly, W J Kane, M B Bailie, G D Abrams, B R Lucchesi, Canine myocardial reperfusion injury. Its reduction by the combined administration of superoxide dismutase and catalase. Circulation Research. ,vol. 54, pp. 277- 285 ,(1984) , 10.1161/01.RES.54.3.277
Rakesh C. Kukreja, Ann B. Weaver, Michael L. Hess, Stimulated human neutrophils damage cardiac sarcoplasmic reticulum function by generation of oxidants Biochimica et Biophysica Acta. ,vol. 990, pp. 198- 205 ,(1989) , 10.1016/S0304-4165(89)80034-0
Imre Zs.-Nagy, Robert A. Floyd, Hydroxyl free radical reactions with amino acids and proteins studied by electron spin resonance spectroscopy and spin-trapping. Biochimica et Biophysica Acta. ,vol. 790, pp. 238- 250 ,(1984) , 10.1016/0167-4838(84)90028-1
S KRAUSE, M HESS, The effect of short term normothermic global ischemia and acidosis on cardiac myofibrillar Ca2+−Mg2+ ATPase activity Journal of Molecular and Cellular Cardiology. ,vol. 17, pp. 523- 526 ,(1985) , 10.1016/S0022-2828(85)80058-4