Sarcoplasmic reticulum Ca2+-pump dysfunction in rat cardiomyocytes briefly exposed to hydroxyl radicals

Free Radical Biology and Medicine

Volumn 22, Issue 1-2, 1997, Pages 37-47

  Morris, Thomas E ^a   Sulakhe, Prakash V ^a  

^a UNIVERSITY OF SASKATCHEWAN   (Canada)

Author keywords

Calcium pump; Cardiomyocytes; Lipid oxidation; Oxygen derived free radicals; Phospholamban; Sarcoplasmic reticulum; Sulfhydryl group

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); ADENOSINE TRIPHOSPHATASE (CALCIUM); CALMODULIN; CATALASE; CYCLIC AMP DEPENDENT PROTEIN KINASE; FERROUS CHLORIDE; FERROUS SULFATE; HYDROGEN PEROXIDE; HYDROXYL RADICAL; MALONALDEHYDE; MANNITOL; N ETHYLMALEIMIDE;

ANIMAL CELL; ARTICLE; CALCIUM TRANSPORT; CELL DAMAGE; CONTROLLED STUDY; HEART MUSCLE CELL; ISOLATED HEART; LIPID OXIDATION; MALE; NONHUMAN; PRIORITY JOURNAL; RAT; SARCOPLASMIC RETICULUM;

ANIMALIA;

EID: 0029859988     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(96)00238-9     Document Type: Article

References (40)

1. Jennings R. B., Reimer K. A., Steenbergen C. Myocardial ischemia revisted. The osmolar load, membrane damage and reperfusion. J. Mol. Cell. Cardiol. 18:1986;769-780.
2. Burton K. P. Evidence of direct toxic effects of free radicals on the myocardium. Free Radic. Biol. Med. 4:1988;15-24.
3. Kloner R. A. Introduction of the role of oxygen radicals in myocardial ischemia and infarction. Free Radic. Biol. Med. 4:1988;5-7.
4. Hess M. L., Manson N. H. Molecular oxygen: Friend or foe: The role of the oxygen free radical system in the calcium paradox, the oxygen paradox and ischemia/reperfusion injury. J. Mol. Cell. Cardiol. 16:1984;969-985.
5. Kukreja R. C., Hess M. L. The oxygen free radical system: From equations through membrane/protein interactions to cardiovascular injury and protection. Cardiovasc. Res. 26:1992;641-655.
6. Singal P. K., Dhalla A. K., Hill M., Thomas T. P. Endogenous antioxidant changes in the myocardium in response to acute and chronic stress conditions. Mol. Cell. Biochem. 129:1993;179-186.
7. Okabe E., Hess M. L., Oyama M., Ito H. Characterization of free radical-mediated damage of canine sarcoplasmic reticulum. Arch. Biochem. Biophys. 225:1983;164-177.
8. 2+-ATPase. Arch. Biochem. Biophys. 246:1986;589-610.
9. Okabe E., Odajima C., Taga R., Kukreja R. C., Hess M. L., Ito H. The effect of oxygen free radicals on calcium permeability and calcium loading at steady state in cardiac sarcoplasmic reticulum. Mol. Pharmacol. 34:1988;388-394.
10. 2+-activity by oxygen free radicals. Am. J. Physiol. 256:1989;H368-H374.
11. 2+ pump by oxygen free radicals. Am. J. Physiol. 257:1989;H804-H811.
12. Kaneko M., Matsumoto Y., Hayashi H., Kobayashi A., Yamazaki N. Oxygen free radicals and calcium homeostasis in the heart. Mol. Cell. Biochem. 139:1994;91-100.
13. Yanagashita T., Matsuoka T., Kako K. J. Pharmacological intervention in oxidant-induced calcium pump dysfunction of dog heart. Biochem. Int. 18:1989;1111-1119.
14. Maupoil V., Rochette L. Evaluation of free radical and lipid peroxide formation during global ischemia and reperfusion in isolated perfused rat heart. Cardiovasc. Drugs Ther. 2:1988;615-621.
15. Zweier J. L., Flaherty J. T., Weisfeldt M. L. Direct measurement of free radical generation following reperfusion of ischemic myocardium. Proc. Natl. Acad. Sci. USA. 84:1987;1404-1407.
16. Garlick P. B., Davies M. J., Hearse D. J., Slater T. F. Direct detection of free radicals in the reperfused rat heart using electron spin resonance spectroscopy. Circ. Res. 61:1987;757-760.
17. Bolli R., Patel B. S., Jeroudi M. O., Lai E. K., McCay P. B. Demonstration of free radical generation in "stunned" myocardium of intact dogs with the use of spin trap alpha-phenyl N-tert-butyl nitrone. J. Clin. Invest. 82:1988;476-485.
18. Arroyo C. M., Kramer J. H., Dickens B. F., Weglicki W. B. Identification of free radicals in myocardial ischemia/reperfusion by spin trapping with nitrone DMPO. FEBS Lett. 221:1987;101-104.
19. Kryski A., Kenno K. A., Severson D. L. Stimulation of lipolysis in rat heart myocytes by isoproterenol. Am. J. Physiol. 248:1985;H208-H216.
20. Sulakhe P. V., Vo X. T. Regulation of phospholamban and troponin-I phosphorylation in the intact rat cardiomyocytes by adrenergic and cholinergic stimuli: Roles of cyclic nucleotides, calcium, protein kinases and phosphatases and depolarization. Mol. Cell. Biochem. 149194/:1995;103-126.
21. Sulakhe P. V., Drummond G. I., Ng D. C. Calcium binding to skeletal muscle sarcolemma. J. Biol. Chem. 248:1973;4150-4157.
22. Boyne A. F., Ellman G. L. A methodology for analysis of tissue sulfhydryls. Anal. Biochem. 46:1972;639-653.
23. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. Protein measurement with the Folin reagent. J. Biol. Chem. 193:1950;265-275.
24. Buege J. A., Aust S. D. Microsomal lipid peroxidation. Methods Enzymol. 52:1978;302-310.
25. Wong S. H. Y., Knight J. A., Hopfer S. M., Zaharia O., Leach C. N., Sunderman F. W. Lipoperoxides in plasma as measured by liquid-chromatographic separation of malonyldialdehyde-thiobarbituic acid adduct. Clin. Chem. 33:1987;214-220.
26. Sulakhe P. V., Drummond G. I. Protein kinase-catalyzed phosphorylation of muscle sarcolemma. Arch. Biochem. Biophys. 161:1974;448-455.
27. Hammond B., Kontos H. A., Hess M. L. Oxygen radicals in the adult respiratory distress syndrome, in myocardial ischemia and reperfusion injury, and in cerebral vasculature damage. Can. J. Physiol. Pharmacol. 63:1984;173-187.
28. Koller P. T., Bergmann S. R. Reduction of lipid peroxidation in reperfused isolated rabbit heart by diltiazem. Circ. Res. 65:1987;838-846.
29. Kaneko M., Lee S. L., Wolf C. M., Dhalla N. S. Reduction of calcium channel antagonist binding sites by oxygen free radicals in rat heart. J. Mol. Cell. Cardiol. 21:1989;935-943.
30. 2 vs. HOCl. Am. J. Physiol. 256:1989;C598-C607.
31. 2+-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 253:1978;6801-6807.
32. 2+-dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Binding of N-ethylmaleimide to sarcoplasmic reticulum, evidence for sulfhydryl groups in the active site of ATPase and for conformational changes induced by adenosine tri and diphosphate. J. Biochem. 79:1976;649-654.
33. Tada M., Katz A. M. Phosphorylation of the sarcoplasmic reticulum and sarcolemma. Annu. Rev. Physiol. 44:1982;401-423.
34. Wegener A. D., Simmerman H. K. B., Lindemann J. P., Jones L. R. Phospholamban phosphorylation in intact ventricles: Phosphorylation of serine 16 and threonine 17 in response to B-adrenergic stimulation. J. Biol. Chem. 264:1989;11468-11474.
35. Miki S., Ashraf M., Salka S., Sperelakis N. Myocardial dysfunction and ultrastructural alterations mediated by oxygen metabolites. J. Mol. Cell. Cardiol. 20:1988;1009-1024.
36. Schwaiger M., Fishbein M. C., Block M., Wijns W., Selin C., Phelps M. E., Schelbert H. R. Metabolic and ultrastructural abnormalities during ischemia in canine myocardium: Noninvasive assessment by positron emission tomography. J. Mol. Cell. Cardiol. 19:1987;259-269.
37. Sulakhe P. V., Jagadeesh G., Braun A. P. Cardiac autonomic receptors and adenylate cyclase in health and desease. Rupp H. The regulation of heart function. 1986;71-94 George Thieme Verlag, Stuggart.
38. 2 species on the β -receptor-adenylyl cyclase system. Mol. Cell. Biochem. 110:1992;41-46.
39. Narayanan N. Differential alterations in ATP-supported calcium transport activities of sarcoplasmic reticulum and sarcolemma of aging myocardium. Biochem. Biophys. Acta. 678:1981;442-459.
40. Taffet G. E., Tate C. A. The MgATPase activity of rat cardiac sarcoplasmic reticulum is a function of the calcium ATPase protein. Arch. Biochem. Biophys. 299:1992;287-294.