Sites and mechanisms responsible for the low rate of free radical production of heart mitochondria in the long-lived pigeon

Mechanisms of Ageing and Development

Volumn 98, Issue 2, 1997, Pages 95-111

  Herrero, A ^a   Barja, G ^a  

^a UNIVERSIDAD COMPLUTENSE DE MADRID   (Spain)

Author keywords

Aging; Free radicals; Heart; Hydrogen peroxide; Longevity; Mitochondria

Indexed keywords

4 CHLOROMERCURIBENZOIC ACID; ETHOXYFORMIC ANHYDRIDE; FERRICYANIDE; FORMIC ACID DERIVATIVE; FREE RADICAL; HYDROGEN PEROXIDE; MALIC ACID; PYRUVIC ACID; ROTENONE; SUCCINIC ACID; THENOYLTRIFLUOROACETONE; UNCLASSIFIED DRUG;

AGING; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ELECTRON; ELECTRON TRANSPORT; HEART MITOCHONDRION; LONGEVITY; MALE; NONHUMAN; OXYGEN CONSUMPTION; PIGEON; PRIORITY JOURNAL; RAT; RESPIRATORY CHAIN;

AGING; ANIMALS; COLUMBIDAE; ELECTRON TRANSPORT; EVOLUTION; FREE RADICALS; HYDROGEN PEROXIDE; LONGEVITY; MALE; MITOCHONDRIA, HEART; MITOSIS; OXYGEN CONSUMPTION; RATS; RATS, WISTAR; REACTIVE OXYGEN SPECIES; SPECIES SPECIFICITY;

ANIMALIA; AVES; COLUMBA;

EID: 0030793931     PISSN: 00476374     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0047-6374(97)00076-6     Document Type: Article

References (38)

1. D. Harman, Aging: prospects for further increases in the functional life span, Age 17 (1994) 119-146.
2. A. Boveris, B. Chance, The mitochondrial generation of hydrogen peroxide, General properties and effect of hyperbaric oxygen, Biochem. J. 134 (1973) 707-716.
3. H. Nohl, Generation of superoxide as a byproduct of cellular respiration, Ann. Biol. Clin. 52 (1994) 199-204.
4. R.S. Sohal, I. Svensson, B.H. Sohal, U.T. Brunk, Superoxide anion radical production in different species, Mech. Ageing Dev. 49 (1989) 129-135.
5. R.S. Sohal, I. Svensson, U.T. Brunk, Hydrogen peroxide production by liver mitochondria in different species, Mech. Ageing Dev. 53 (1990) 209-215.
6. H.H. Ku, U.T. Brunk, R.S. Sohal, Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian species, Free Rad. Biol. Med. 15 (1993) 621-627.
7. R. Pearl, The Rate of Living, University of London Press, London, 1928.
8. J. Prothero, K.D. Jürgens, Scaling of maximal life span in mammals: a review, in: Evolution of Longevity in Animals, Plenum Press, New York, 1987, pp. 49-79.
9. D.J. Holmes, S.N. Austad, The evolution of avian senescence patterns: implications for understanding primary aging processes, Am. Zool. 35 (1995) 307-317.
10. 2 consumption can explain the simultaneous presence of high longevity and high aerobic metabolic rate in birds, Free Rad. Res. 21 (1994) 317-328.
11. H.H. Ku, R.S. Sohal, Comparison of mitochondrial pro-oxidant and antioxidant defenses between rat and pigeon: possible basis of variation in longevity and metabolic potential, Mech. Ageing Dev. 72 (1993) 67-76.
12. A. Boveris, E. Cadenas, A.O.M. Stoppani, Role of ubiquinone in the mitochondrial generation of hydrogen peroxide, Biochem. J. 156 (1976) 435-444.
13. K. Takeshige, S. Minakami, NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NAD-ubiquinone-reductase preparation, Biochem. J. 180 (1979) 129-135.
14. L. Mela, S. Seitz, Isolation of mitochondria with emphasis on heart mitochondria from small amounts of tissue, Methods Enzymol. 55 (1979) 39-46.
15. 2 production by macrophages and neutrophils with homovanilic acid and horse-radish peroxidase, J. Immunol. Methods 63 (1983) 347-357.
16. E. Cadenas, A. Boveris, Enhancement of hydrogen peroxide formation by protophores and ionophores in antimycin-supplemented mitochondria, Biochem. J. 188 (1980) 31-37.
17. B. Chance, G.R. Williams, The respiratory chain and oxidative phosphorylation, Advances Enzymol. Relat. Subj. Biochem. 17 (1956) 65-134.
18. B. Chance, The reaction of oxygen with cytochrome oxidase, in: D. Gilbert (Ed.), Oxygen and Living Processes, Springer, New York, 1981, pp. 200-209.
19. J.F. Turrens, A. Boveris, Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria, Biochem. J. 191 (1980) 421-427.
20. H. Nohl, W. Jordan, The mitochondrial site of superoxide formation, Biochem. Biophys. Res. Comms. 138 (1986) 533-539.
21. H. Nohl, K. Stolze, Ubisemiquinones of the mitochondrial respiratory chain do not interact with molecular oxygen, Free Rad. Res. Comms. 16 (1992) 409-419.
22. J.F. Turrens, A. Alexandre, A.L. Lehninger, Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria, Arch. Biochem. Biophys. 237 (1985) 408-414.
23. H. Nohl, L. Gille, K. Schönheit, Y. Liu, Conditions allowing redox-cycling ubisemiquinone in mitochondria to establish a direct redox couple with molecular oxygen, Free Rad. Biol. Med. 20 (1996) 207-213.
24. J.M. Cooper, V.M. Mann, D. Krige, A.H.V. Schapira, Human mitochondrial Complex I dysfunction, Biochim. Biophys. Acta 1101 (1992) 198-203.
25. A.H.V. Shapira, Mitochondria, Free radicals, neurodegeneration and aging, in: R.G. Cutler, L. Packer, J. Bertram, A. Mori (Eds.), Oxidative Stress and Aging, Birkhäuser, Basel, 1995, pp. 159-169.
26. Ch. Richter, Role of mitochondrial DNA modifications in degenerative diseases and aging, Int. J. Biochem. Cell Biol. 27 (1995) 647-653.
27. K. Yamada, S. Sugiyama, K. Kosaka, M. Hayakawa, T. Ozawa, Early appearance of age-associated deterioration in mitochondrial function of diaphragm and heart in rats with doxorubicin, Exp. Gerontol. 30 (1995) 581-593.
28. G. Benzi, A. Moretti, Age- and peroxidative stress-related modifications of the cerebral enzymatic activities linked to mitochondria and the glutathione system, Free Rad. Biol. Med. 19 (1995) 77-101.
29. K. Veitchk, A. Hombroeckx, D. Caucheteux, H. Pouleur, L. Hue, Global ischemia induces a biphasic response of the mitochondrial respiratory chain, Biochem. J. 281 (1992) 709-715.
30. M. Filser, S. Werner, Pethidine analogues, a novel class of potent inhibitors of mitochondrial NADH:ubiquinone reductase, Biochem. Pharm. 37 (1988) 2251-2258.
31. R.E. Beyer, An analysis of the role of coenzyme Q in free radical generation and as an antioxidant, Biochem. Cell Biol. 70 (1992) 390-403.
32. Y. Eto, D. Kang, E. Hasegawa, K. Takeshige, S. Minakami, Succinate-dependent lipid peroxidation and its prevention by reduced ubiquinone in beef heart submitochondrial particles, Arch. Biochem. Biophys. 295 (1992) 101-106.
33. G. Ambrosio, J.L. Zweier, C. Duilio, P. Kuppusamy, G. Santoro, P.P. Elia, I. Tritto, P. Cirillo, M. Condorelli, M. Chiariello, J.T.E. Flaherty, Evidence that mitochondrial respiration is a source of potentially toxic oxygen free radicals in intact rabbit hearts subjected to ischemia and reflow, J. Biol. Chem. 268 (1993) 18532-18541.
34. D. Tyler, The Mitochondrion in Health and Disease, VCH, New York, 1992, pp. 172-173.
35. J.N. Williams, A comparative study of cytochrome ratios in mitochondria of the rat, chicken, and guinea pig, Biochim. Biophys. Acta 162 (1968) 175-181.
36. K. Schmidt-Nielsen, Scaling. Why is animal size so important?, Cambridge University Press, Cambridge, 1984, pp. 130-132.
37. K.M. Wyatt, C. Skene, K. Veitch, L. Hue, J.G. McCormack, The antianginal agent ranolazine is a weak inhibitor of the respiratory complex I, but with greater potency in broken or uncoupled than in coupled mitochondria, Biochem. Pharm. 50 (1995) 1599-1606.
38. S.B. Vik, Y. Hatefi, Inhibition of mitochondrial NADH:ubiquinone oxidoreductase by ethoxy-formic anhydride, Biochem. Int. 9 (1984) 547-555.