Oxidative stress increases glyceraldehyde-3-phosphate dehydrogenase mRNA levels in isolated rabbit aorta

American Journal of Physiology - Heart and Circulatory Physiology

Volumn 270, Issue 1 39-1, 1996, Pages

  Ito, Yasushi ^a   Pagano, Patrick J ^a   Tornheim, Keith ^a   Brecher, Peter ^a   Cohen, Richard A ^a  

^a BOSTON UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

free radicals; nitric oxide; superoxide dismutase

Indexed keywords

FREE RADICAL; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MESSENGER RNA; NITRIC OXIDE; SUPEROXIDE DISMUTASE;

ANIMAL TISSUE; AORTA; ARTICLE; CELL MEMBRANE PERMEABILITY; CELL METABOLISM; ENDOTHELIUM CELL; ENZYME ACTIVITY; ISOLATED ORGAN; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; RABBIT; VASCULAR ENDOTHELIUM; VASCULAR RING;

EID: 0030022523     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.1996.270.1.h81     Document Type: Article

References (35)

1. Ames, B. N., M. K. Shigenaga, and T. M. Hagen. Oxidants, antioxidants, and the degenerative diseases of aging. Proc. Natl. Acad. Sci. USA 90: 7915-7922, 1993.
2. Beckman, J. S., T. W. Beckman, J. Chen, P. A. Marshall, and B. A. Freeman. Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc. Natl. Acad. Sci. USA 87: 1620-1624, 1990.
3. Bergmeyer, H. V., K. Gawehn, and M. Grassl. Enzymes as biochemical reagents. In: Methods of Enzymatic Analysis (2nd ed.), edited by H. V. Bergmeyer. New York: Academic, 1974, p. 466-467.
4. Biemond, P., H. G. van Eijk, J. G. Swaak, and J. F. Koster. Iron mobilization from ferritin by superoxide derived from stimulated polymorphonuclear leukocytes: possible mechanism in inflammation diseases. J. Clin. Invest. 73: 1576-1579, 1984.
5. Bond, J., and S. Farmer. Regulation of tubulin and actin mRNA production in rat brain: expression of a new beta-tubulin mRNAwith development. Mol. Cell. Biol. 3: 1333-1342, 1983.
6. Bros, W., M. Saran, and C. Michel. Pulse-radiolytic investigation of catechols and catecholamines. II. Reactions of Tiron with oxygen radical species. Biochim. Biophys. Acta 582: 537-542, 1979.
7. Chao, C. C.-K., W.-C. Yam, and S. Lin-Chao. Coordinated induction of two unrelated glucose-regulated protein genes by a calcium ionophore: human BiP/GRP78 and GAPDH, Biochem. Biophys. Res. Commun. 171: 431-438, 1990.
8. Chomczynski, P., and N. Sacchi. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156-159, 1987.
9. Coats, W. D., Jr., and P. Brecher. Cyclic AMP suppresses fibronectin expression in the rabbit aorta in vitro. Arteriosclerosis Thromb. 13: 1668-1679, 1993.
10. Freeman, B. A., and J. D. Crapo. Biology of diseases: free radicals and tissue injury. Lab. Invest. 47: 412-426, 1982.
11. Fucci, L., C. N. Oliver, M. J. Coon, and E. R. Stadtman. Inactivation of key metabolic enzymes by mixed-function oxidation reactions: possible implication in protein turnover and aging. Proc. Natl. Acad. Sci USA 80: 1521-1525, 1983.
12. Greenberg, J. T., P. Monach, J. H. Chou, P. D. Josephy, and B. Demple. Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc. Natl. Acad. Sci. USA 87: 6181-6185, 1990.
13. Greenstock, C. L., and R. W. Miller. The oxidation of Tiron by superoxide anion: kinetics of the reaction in aqueous solution and in chloroplasts. Biochim. Biophys. Acta 396: 11-16, 1975.
14. Gryglewski, R. J., R. M. J. Palmer, and S. Moncada. Superoxide anion is involved in the breakdown of endothelium-derived vascular relaxing factor. Nature Lond. 320: 454-456, 1986.
15. Halliwell, B., and O. I. Aruoma. DNA damage by oxygen-derived species: its mechanism and measurement in mammalian systems. FEBS Lett. 281: 9-19, 1991.
16. Halliwell, B., and J. M. C. Gutteridge. Oxygen free radicals and iron in relation to biology and medicine: some problems and concepts. Arch. Biochem. Biophys. 246: 501-514, 1986.
17. Halliwell, B., and J. M. C. Gutteridge. Biologically relevant metal ion-dependent hydroxyl radical generation: an update. FEBS Lett. 307: 108-112, 1992.
18. Heikkila, R. E., F. S. Cabbat, and G. Cohen. In vivo inhibition of superoxide dismutase in mice by diethyldithiocarbamate. J. Biol. Chem. 251: 2182-2185, 1976.
19. Hiraishi, H., A. Terano, M. Razandi, T. Sugimoto, T. Harada, and K. J. Ivey. Role of cellular superoxide dismutase against reactive oxygen metabolite injury in cultured bovine aortic endothelial cells. J. Biol. Chem. 267: 14812-14817, 1992.
20. Janero, D. R., D. Hreniuk, and H. M. Sharif. Hydroperoxide-induced oxidative stress impairs heart muscle cell carbohydrate metabolism. Am. J. Physiol. 266 (Cell Physiol. 35): C179-C188, 1994.
21. Kletzien, R. F., P. K. Harris, and L. A. Foelimi. Glucose-6-phosphate dehydrogenase: a "housekeeping" enzyme subject to tissue specific regulation by hormones, nutrients, and oxidant stress. FASEB J. 8: 174-181, 1994.
22. Mao, G. D., P. D. Thomas, G. D. Lopaschuk, and M. J. Poznansky. Superoxide dismutase (SOD)-catalase conjugates: role of hydrogen peroxide and the Fenton reaction in SOD toxicity. J. Biol. Chem. 268: 416-420, 1993.
23. Mello Filho, A. C., M. E. Hoffmann, and R. Meneghini. Cell killing and DNA damage by hydrogen peroxide are mediated by intracellular iron. Biochem. J. 218: 273-275, 1984.
24. Mello Filho, A. C., and R. Meneghini. In vivo formation of single-strand breaks in DNA by hydrogen peroxide is mediated by the Haber-Weiss reaction. Biochim. Biophys. Acta 781: 56-63, 1984.
25. Meyer-Siegler, K., D. J. Mauro, G. Seal, J. Wurzer, J. K. DeRiel, and M. A. Sirover. A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase. Proc. Natl. Acad. Sci. USA 88: 8460-8464, 1991.
26. Moncada, S., D. D. Rees, R. Schulz, and R. M. J. Palmer. Development and mechanism of a specific supersenitivity to nitrovasodilators after inhibition of vascular nitric oxide synthesis in vivo. Proc. Natl. Acad. Sci. USA 88: 2166-2170, 1991.
27. Mugge, A., J. H. Elwell, T. E. Peterson, and D. G. Harrison. Release of intact endothelium-derived relaxing factor depends on endothelial superoxide dismutase activity. Am. J. Physiol. 260 (Cell Physiol. 29): C219-C225, 1991.
28. Omar, H. A., P. D. Cherry, M. P. Mortelliti, T. Burke-Wolin, and M. S. Wolin. Inhibition of coronary artery superoxide dismutase attenuates endothelium-dependent and -independent nitrosovasodilator relaxation. Circ. Res. 69: 601-608, 1991.
29. 2 toxicity. Proc. Natl. Acad. Sci. USA 89: 9715-9719, 1992.
30. Pagano, P. J., K. Tornheim, and R. A. Cohen. Superoxide anion production by rabbit thoracic aorta: effect of endothelium-derived nitric oxide. Am. J. Physiol. 265 (Heart Circ. Physiol. 34): H707-H712, 1993.
31. Roos, D., R. S. Weening, A. A. Voetman, M. L. J. Van Schik, A. A. M. Bot, L. J. Meerhof, and J. A. Loos. Protection of phagocytic leukocytes by endogenous glutathione: studies in a family with glutathione reductase deficiency. Blood 53: 851-866, 1979.
32. Rubanyi, G. M., and P. M. Vanhoutte. Superoxide anions and hyperoxia inactivate endothelium-derived relaxing factor. Am. J. Physiol. 250 (Heart Circ. Physiol. 19): H822-H827, 1986.
33. Schraufstaetter, I., P. A. Hyslop, J. H. Jackson, and C. G. Cochrane. Oxidant-induced DNA damage of target cells. J. Clin. Invest. 82: 1040-1050, 1988.
34. 2+-ATPase of vascular smooth muscle sarcoplasmic reticulum by reactive oxygen intermediates. Am. J. Physiol. 261 (Heart Circ. Physiol. 30): H568-H574, 1991.
35. Yu, B. P. Cellular defenses against damage from reactive oxygen species. Physiol Rev. 74: 139-162, 1994.