Fatty acids as modulators of the cellular production of reactive oxygen species

Free Radical Biology and Medicine

Volumn 45, Issue 3, 2008, Pages 231-241

  Schönfeld, Peter ^a   Wojtczak, Lech ^b  

^a OTTO VON GUERICKE UNIVERSITY   (Germany)

^b NENCKI INSTITUTE OF EXPERIMENTAL BIOLOGY   (Poland)

Author keywords

Fatty acid; Mild uncoupling; Mitochondria; NADPH oxidase; Reactive oxygen species

Indexed keywords

ACYL COENZYME A; CERAMIDE; CYTOCHROME C; ETHANOLAMINE DERIVATIVE; GLUTATHIONE; HYDROGEN PEROXIDE; LONG CHAIN FATTY ACID; PHOSPHOLIPASE A2; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; THIOESTER;

APOPTOSIS; ELECTRON TRANSPORT; ENZYME ACTIVITY; FATTY ACID OXIDATION; HUMAN; MEMBRANE FLUIDITY; MEMBRANE POTENTIAL; MITOCHONDRIAL MEMBRANE; NEUTROPHIL; OXIDATIVE STRESS; PHAGOCYTOSIS; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; RESPIRATORY CHAIN; REVIEW;

ANIMALS; CELL RESPIRATION; ELECTRON TRANSPORT; FATTY ACIDS; HUMANS; MITOCHONDRIA; REACTIVE OXYGEN SPECIES;

EID: 46449087496     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2008.04.029     Document Type: Review

References (182)

1. Halliwell B., and Gutterridge J.M.C. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J. 219 (1984) 1-14
2. Harman D. Aging: a theory based on free radical and radiation chemistry. J. Gerontol. 11 (1956) 298-300
3. McCord J.M., and Fridovich I. Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244 (1969) 6049-6055
4. Pryor W.A., Houk K.N., Foote C.S., Fukuto J.M., Ignarro L.J., Squadrito G.L., and Davies K.J.A. Free radical biology and medicine: it's a gas, man!. Am. J. Physiol. Regul. Integr. Comp. Physiol. 291 (2006) R491-R511
5. Andreyev A.Y., Kushnareva Y.E., and Starkov A.A. Mitochondrial metabolism of reactive oxygen species. Biochemistry (Moscow) 70 (2005) 200-214
6. Adam-Vizi V., and Chinopoulos C. Bioenergetics and the formation of mitochondrial reactive oxygen species. Trends Pharm. Sci. 27 (2006) 639-645
7. Fiskum G., Murphy A., and Beal M.F. Mitochondria in neurodegeneration: acute ischemia and chronic neurodegenerative diseases. J. Cereb. Blood Flow Metab. 19 (1999) 351-369
8. Navarro A., and Boveris A. Rat brain and liver mitochondria develop oxidative stress and lose enzymatic activities on aging. Am. J. Physiol. Regul. Integr. Comp. Physiol. 287 (2004) R1244-R1249
9. Staniek K., and Nohl H. Are mitochondria a permanent source of reactive oxygen species? Biochim. Biophys. Acta 1460 (2000) 268-275
10. Hille R., and Nishino T. Xanthine oxidase and xanthine dehydrogenase. FASEB J. 9 (1995) 995-1003
11. Schrader M., and Fahimi H.D. Peroxisomes and oxidative stress. Biochim. Biophys. Acta 1763 (2006) 1755-1766
12. Dahlgren C., and Karlsson A. Respiratory burst in human neutrophils. J. Immunol. Methods 232 (1999) 3-14
13. Gottlieb R.A. Cytochrome p450: major player in reperfusion injury. Arch. Biochim. Biophys. 420 (2003) 262-267
14. Kuehl F.A., and Egan R.N. Prostaglandins, arachidonic acid and inflammation. Science 210 (1980) 978-984
15. Samuelsson B. Leucotrienes: mediators of immediate hypersensitivity reactions and inflammation. Science 220 (1983) 568-575
16. Lin M.T., and Beal M.F. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443 (2006) 787-795
17. Madamanchi N.R., and Runge M.S. Mitochondrial dysfunction in atherosclerosis. Circ. Res. 100 (2007) 460-473
18. Lesnefsky E.J., Moghaddas S., Tandler B., Kerner J., and Hoppel C.L. Mitochondrial dysfunction in cardiac disease: Ischemia-reperfusion, aging, and heart failure. J. Mol. Cell. Cardiol. 33 (2001) 1065-1089
19. Newsholme P., Haber E.P., Hirabara S.M., Rebelato E.L.O., Procopio J., Morgan D., Oliveira-Emilio H.C., Carpinelli A.R., and Curi R. Diabetes associated cell stress and dysfunction: role of mitochondrial and non-mitochondrial ROS production and activity. J. Physiol. 583 (2007) 9-24
20. Beckman K.B., and Ames B.N. The free radical theory of aging matures. Physiol. Rev. 78 (1998) 547-581
21. Skulachev V.P. The programmed death phenomena, aging, and the Samurai law of biology. Exp. Gerontol. 36 (2001) 995-1024
22. Navarro A., and Boveris A. The mitochondrial energy transduction system and the aging process. Am. J. Physiol. Cell Physiol. 292 (2007) C670-C686
23. Dröge W. Free radicals in physiological control of cell function. Physiol. Rev. 82 (2002) 47-95
24. Stone J.R., and Yang S.P. Hydrogen peroxide: a signaling messenger. Antioxid. Redox Signal. 8 (2006) 243-270
25. Reth M. Hydrogen peroxide as second messenger in lymphocyte activation. Nat. Immunol. 3 (2002) 1129-1134
26. Chandel N.S., McClintock D.S., Feliciano C.E., Wood T.M., Melendez J.A., Rodriguez A.M., and Schumacker P.T. Reactive oxygen species generated at mitochondrial complex III stabilize hypoxia-inducible factor-1α during hypoxia: a mechanism of O2 sensing. J. Biol. Chem. 275 (2000) 25130-25138
27. Wojtczak L., and Schönfeld P. Effect of fatty acids on energy coupling processes in mitochondria. Biochim. Biophys. Acta 1183 (1993) 41-57
28. Bernardi P., Penzo D., and Wojtczak L. Mitochondrial energy dissipation by fatty acids. Mechanisms and implications for cell death. Vitam. Horm. 65 (2002) 97-126
29. Bazan N. Effect of ischemia and electro-convulsive shock on free fatty acid pool in the brain. Biochim. Biophys. Acta 218 (1970) 1-16
30. Gardiner M., Nilsson B., Rehncrona S., and Siesjö B.K. Free fatty acids in the rat brain in moderate and severe hypoxia. J. Neurochem. 36 (1981) 1500-1505
31. Skulachev V.P. Fatty acid circuit as a physiological mechanism of uncoupling of oxidative phosphorylation. FEBS Lett. 294 (1991) 158-162
32. Di Paola M., and Lorusso M. Interaction od free fatty acids with mitochondria: coupling, uncoupling and permeability transition. Biochim. Biophys. Acta 1757 (2006) 1330-1337
33. Wojtczak L., and Załuska H. The inhibition of translocation of adenine nucleotides through mitochondrial membranes by oleate. Biochem. Biophys. Res. Commun. 28 (1967) 76-81
34. Takeuchi Y., Morii H., Tamura M., Hayaishi O., and Watanabe Y. A possible mechanism of mitochondrial dysfunction during cerebral ischemia: Inhibition of mitochondrial respiration by arachidonic acid. Arch. Biochem. Biophys. 289 (1991) 33-38
35. Skulachev V.P. Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductans. Q. Rev. Biophys. 29 (1996) 169-202
36. Moser H.W., and Moser A.B. X-linked adrenoleukodystrophy. In: Scriver C.R., Beaudet A.L., Sly W.S., and Valle D. (Eds). The metabolic basis of inherited diseases, sixth ed (1989), McGraw Hill, New York 1511-1532
37. Van den Brink D.M., and Wanders R.J.A. Phytanic acid: production from phytol, its breakdown and role in human disease. Cell. Mol. Life Sci. 63 (2006) 1752-1765
38. Azevedo-Martins A.K., and Curi R. Fatty acids decrease catalase activity in human leukaemia cell lines. Cell Biochem. Funct. 26 (2008) 87-94
39. 2 production in pigeon heart mitochondria. FEBS Lett. 18 (1971) 261-264
40. Boveris A., and Chance B. The mitochondrial generation of hydrogen peroxide. General properties and the effect of hyperbaric oxygen. Biochem. J. 134 (1973) 707-716
41. Kwong L.K., and Sohal R.S. Substrate and site specificità of hydrogen peroxide generation in mouse mitochondria. Arch. Biochem. Biophys. 350 (1998) 118-126
42. Liu Y., Fiskum G., and Schubert D. Generation of reactive oxygen species by the mitochondrial electron transport chain. J. Neurochem. 80 (2002) 780-787
43. Panov A., Dikalov S., Shalbuyeva N., Hemendinger R., Greenamyre J.T., and Rosenfeld J. Species- and tissue-specific relationships between mitochondrial permeability transition and generation of ROS in brain and liver mitochondria of rats and mice. Am. J. Physiol. Cell Physiol. 292 (2007) C708-C718
44. Herrero A., and Barja G. Sites and mechanisms responsible for the low rate of free radical production of heart mitochondria in the long-lived pigeon. Mech. Ageing Dev. 98 (1997) 95-111
45. Turrens J.F., Alexandre A., and Lehninger A.L. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch. Biochem. Biophys. 237 (1985) 408-414
46. Chen Q., Vazquez E.J., Moghaddas S., Hoppel C.L., and Lesnefsky E.L. Production of reactive oxygen species by mitochondria: central role of complex III. J. Biol. Chem. 278 (2003) 36027-36031
47. Zang L., Yu L., and Yu C.A. Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria. J. Biol. Chem. 273 (1998) 33972-33976
48. Drahota Z., Chowdhury S.K., Floryk D., Mráček T., Wilhelm J., Rauchová H., Lenaz G., and Houštěk J. Glycerophosphate-dependent hydrogen peroxide production by brown adipose tissue mitochondria and its activation by ferrocyanide. J. Bioenerg. Biomembr. 34 (2002) 105-113
49. Han D., Antunes F., Canali R., Retorri D., and Cadenas E. Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol. J. Biol. Chem. 278 (2003) 5557-5563
50. St-Pierre J., Buckinham J.A., Roebuck S.J., and Brand M.D. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J. Biol. Chem. 277 (2002) 44784-44790
51. Muller F.L., Liu Y., and Van Remmen H. Complex III releases superoxide to both sides of the inner mitochondrial membrane. J. Biol. Chem. 279 (2004) 49064-49073
52. Starkov A.A., Fiskum G., Chinopoulos C., Lorenzo B.J., Browne S.E., Patel M.S., and Beal M.F. Mitochondrial a-ketoglutarate dehydrogenase complex generates reactive oxygen species. J. Neurosci. 24 (2004) 7779-7788
53. Tretter L., and Adam-Vizi V. Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress. Philos. Trans. R. Soc. Lond. B Biol. Sci. 360 (2005) 2335-2345
54. Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell 122 (2005) 221-233
55. Shc regulates mitochondrial metabolism. J. Biol. Chem. 281 (2006) 10555-10560
56. Nemoto S., and Finkel T. Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway. Science 295 (2002) 2450-2452
57. Hauptmann N., Grimsby J., Shih J.C., and Cadenas E. The metabolism of tyramine by monoamine oxidase A/B causes oxidative damage to mitochondrial DNA. Arch. Biochem. Biophys. 335 (1996) 295-304
58. Görlach A., Klappa P., and Kietzmann T. The endoplasmic reticulum: folding, calcium homeostasis, signaling, and redox control. Antioxid. Redox Signal. 8 (2006) 1391-1418
59. Kukreja R.C., Kontos H.A., Hess M., and Ellis E.F. PGH synthase and lipoxygenase generate superoxide in the presence of NADH or NADPH. Circ. Res. 59 (1986) 612-619
60. Lambert A.J., and Brand M.D. Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Biol. Chem. 279 (2004) 39414-39420
61. 2 production by membrane potential and NAD(P)H redox state. J. Neurochem. 86 (2003) 1101-1107
62. Gyulkhandanyan A.V., and Pennefather P.S. Shift in the localization of sites of hydrogen peroxide production in brain mitochondria by mitochondrial stress. J. Neurochem. 90 (2004) 405-421
63. Kushnareva Y., Murphy A.N., and Andreyev A. Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation-reduction state. Biochem. J. 368 (2002) 545-553
64. Han D., Canali R., Rettori D., and Kaplowitz N. Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria. Mol. Pharmacol. 64 (2003) 1136-1144
65. Brand M.D., Affourtit C., Esteves T.C., Green K., Lambert A.J., Miwa S., Pakay J.L., and Parker N. Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins. Free Radic. Biol. Med. 37 (2004) 755-767
66. + leak and ROS generation: an odd couple. Free Radic. Biol. Med. 38 (2005) 12-23
67. Korshunov S.S., Skulachev V.P., and Starkov A.A. High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 416 (1997) 15-18
68. 2 by mitochondria in the resting state. FEBS Lett. 435 (1998) 215-218
69. Sipos I., Tretter L., and Adam-Vizi V. The production of reactive oxygen species in intact isolated nerve terminals is independent of the mitochondrial membrane potential. Neurochem. Res. 28 (2003) 1575-1581
70. m in isolated brain mitochondria supported by NADH-linked substrates. Neurochem. Res. 32 (2007) 569-575
71. ATP channel activation. Cardiovasc. Res. 72 (2006) 313-321
72. Johnson-Cadwell L.I., Jekabsons M.B., Wang A., Polster B.M., and Nicholls D.G. Mild uncoupling does not decrease mitochondrial superoxide levels in cultured cerebellar granule neurons but decreases spare respiratory capacity and increases toxicity to glutamate and oxidative stress. J. Neurochem. 101 (2007) 1619-1631
73. Stöckl P., Zankl C., Hütter E., Unterluggauer H., Laun P., Heeren G., Bogengruber E., Herndler-Brandstetter D., Breitenbach M., and Jansen-Dürr P. Partial uncoupling of oxidative phosphorylation induces premature senescence in human fibroblasts and yeast mother cells. Free Radic. Biol. Med. 43 (2007) 947-958
74. Votyakova T.V., and Reynolds I.J. ΔΨm-Dependent and -independent production of reactive oxygen species by rat brain mitochondria. J. Neurochem. 79 (2001) 266-277
75. Schönfeld P., and Wojtczak L. Fatty acids decrease mitochondrial generation of reactive oxygen species at the reverse electron transport but increase it at the forward transport. Biochim. Biophys. Acta 1767 (2007) 1032-1040
76. 2 generation in brain mitochondria. J. Neurochem. 100 (2006) 650-663
77. Miwa S., and Brand M.D. Mitochondrial matrix reactive oxygen species production is very sensitive to mild uncoupling. Biochem. Soc. Trans. 31 (2003) 1300-1301
78. Lambert A.J., and Brand M.D. Superoxide production by NADH:ubiquinone oxidireductase (complex I) depends on the pH gradient across the mitochondrial inner membrane. Biochem. J. 382 (2004) 511-517
79. Liu S.S. Generating, partitioning, targeting and functioning of superoxide in mitochondria. Biosci. Rep. 17 (1997) 259-272
80. Ohnishi S.T., Ohnishi T., Muranaka S., Fujita H., Rimura H., Uemura K., Yoshida K., and Utsumi K. A possible site of superoxide generation in the complex I segment of rat heart mitochondria. J. Bioenerg. Biomembr. 37 (2005) 1-15
81. Frerman F.E. Reaction of electron-transfer flavoprotein ubiquinone oxidoreductase with the mitochondrial respiratory chain. Biochim. Biophys. Acta 893 (1987) 161-169
82. Anderson E.J., Yamazaki H., and Neufer P.D. Induction of endogenous uncoupling protein 3 suppresses mitochondrial oxidant emission during fatty acid-supported respiration. J. Biol. Chem. 282 (2007) 31257-31266
83. Cannon B., Shabalina I.G., Kramarova T.V., Petrovic N., and Nedergaard J. Uncoupling proteins: a role in protection against reactive oxygen species-or not ? Biochim. Biophys. Acta 1757 (2006) 449-458
84. Cannon B., and Nedergaard J. Brown adipose tissue: function and physiological significance. Physiol. Rev. 84 (2004) 277-359
85. Ježek P., Žáčková M., Růžička M., Škobisová E., and Jabůrek M. Mitochondrial uncoupling proteins-facts and fantasies. Physiol. Res. 53 Suppl. 1 (2004) S199-S211
86. Nicholls D.G. The physiological regulation of uncoupling proteins. Biochim. Biophys. Acta 1757 (2006) 459-466
87. Schrauwen P., Saris W.W., and Hesselink M.K. An alternative function for human uncoupling protein 3: protection of mitochondria against accumulation of nonesterified fatty acids inside the mitochondrial matrix. FASEB J. 15 (2001) 2497-2502
88. Goglia F., and Skulachev V.P. A function for novel uncoupling proteins: antioxidant defense of mitochondrial matrix by translocating fatty acid peroxides from the inner to the outer membrane leaflet. FASEB J. 17 (2003) 1585-1591
89. Bézaire V., Seifert E.L., and Harper M.E. Uncoupling protein-3: clues in an ongoing mitochondrial mystery. FASEB J. 21 (2007) 312-324
90. Echtay K.S. Mitochondrial uncoupling proteins-what is their physiological role? Free Radic. Biol. Med. 43 (2007) 1351-1371
91. Muller F.L., Liu Y., Abdul-Ghani M.A., Lustgarten M.S., Bhattacharya A., Jang Y.C., and Van Remmen H. High rates of superoxide production in skeletal-muscle mitochondria respiring on both complex I- and complex II-linked substrates. Biochem. J. 409 (2008) 491-499
92. Cocco T., Di Paola M., Papa S., and Lorusso M. Arachidonic acid interaction with the mitochondrial electron transport chain promotes reactive oxygen species generation. Free Radic. Biol. Med. 27 (1999) 51-59
93. Loskovich M.V., Grivennikova V.G., Cecchini G., and Vinogradov A.D. Inhibitory effect of palmitate on the mitochondrial NADH:ubiquinone oxidoreductase (complex I) as related to the active-de-active enzyme transition. Biochem. J. 387 (2005) 677-683
94. Schönfeld P., and Reiser G. Rotenone-like action of the branched-chain phytanic acid induces oxidative stress in mitochondria. J. Biol. Chem. 281 (2006) 7136-7142
95. Andreyev A.Y.u., Bondareva T.O., Dedukhova V.I., Mokhova E.N., Skulachev V.P., Tsofina L.M., and Volkov N.I. The ATP/ADP-antiporter is involved in the uncoupling effect of fatty acids on mitochondria. Eur. J. Biochem. 182 (1989) 585-592
96. Duval C., Augé N., Frisach M.F., Casteilla L., Salvayre R., and Nègre-Salvayre A. Mitochondrial oxidative stress is modulated by oleic acid via an epidermal growth factor receptor-dependent activation of glutathione peroxidase. Biochem. J. 367 (2002) 889-894
97. Schägger H. Respiratory chain supercomplexes. IUBMB Life 52 (2001) 119-128
98. Schägger H., and Pfeiffer K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 19 (2000) 1777-1783
99. Di Paola M., Cocco T., and Lorusso M. Arachidonic acid causes cytochrome c release from heart mitochondria. Biochem. Biophys. Res. Commun. 277 (2000) 128-133
100. Korge P., Honda H.M., and Weiss J.N. Effects of fatty acids in isolated mitochondria: implications for ischemic injury and cardioprotection. Am. J. Physiol. Circ. Physiol. 285 (2003) H259-H269
101. Reiser G., Schönfeld P., and Kahlert S. Mechanism of toxicity of the branched-chain fatty acid phytanic acid, a marker of Refsum disease, in astrocytes involves mitochondrial impairment. Int. J. Dev. Neurosci. 24 (2006) 113-122
102. Li Q., Sato E.F., Kira Y., Nishikawa M., Utsumi K., and Inoue M. A possible cooperation of SOD1 and cytochrome c in mitochondria-dependent apoptosis. Free Radic. Biol. Med. 40 (2006) 173-181
103. Friedman K.J., and Glick D. Role of lipids in the Neurospora crassa membrane. IV. Biochemical and electrophysiological changes caused by growth on phytanic acid. J. Membr. Biol. 64 (1982) 1-9
104. Stillwell W., Jenski L.J., Crump F.T., and Ehringer W. Effect of docosahexaenoic acid on mouse mitochondrial membrane properties. Lipids 32 (1997) 497-506
105. Schönfeld P., and Struy H. Refsum disease diagnostic marker phytanic acid alters the physical state of membrane proteins of liver mitochondria. FEBS Lett. 457 (1999) 179-183
106. Gille L., and Nohl H. The ubiquinol/bc1 redox couple regulates mitochondrial oxygen radical formation. Arch. Biochem. Biophys. 388 (2001) 34-38
107. O'Brien J.S. Cell membranes-composition, structure, function. J. Theor. Biol. 15 (1967) 307-324
108. Pande S.V., and Blanchaer M.C. Reversible inhibition of mitochondrial adenosine diphosphate phosphorylation by long chain acyl coenzyme A esters. J. Biol. Chem. 246 (1971) 402-411
109. Shug A., Lerner E., Elson C., and Shrago E. The inhibition of adenine nucleotide translocase activity by oleoyl CoA and its reversal in rat liver mitochondria. Biochem. Biophys. Res. Commun. 43 (1971) 557-563
110. Halperin M.L., Robinson B.H., and Fritz I.B. Effects of palmitoyl CoA on citrate and malate transport by rat liver mitochondria. Proc. Natl. Acad. Sci. USA 69 (1972) 1003-1007
111. Bakker S.J.L., Ijzerman R.G., Teerlink T., Westerhoff H.V., Gans R.O.B., and Heine R.J. Cytosolic triglycerides and oxidative stress in central obesity: missing link between excessive atherosclerosis, endothelial dysfunction, and β-cell failure?. Atherosclerosis 148 (2000) 17-21
112. Ciapaite J., Bakker S.J.L., Diamant M., van Eikenhorst G., Heine R.J., Westerhoff H.V., and Krab K. Metabolic control of mitochondrial properties by adenine nucleotide translocator determines palmitoyl-CoA effects. FEBS J. 273 (2006) 5288-5302
113. Stewart J.M., Blakely J.A., and Johnson M.D. The interaction of ferrocytochrome c with long-chain fatty acids and their CoA and carnitine esters. Biochem. Cell Biol. 78 (2000) 675-681
114. 2 release at mitochondrial complex I. J. Bioenerg. Biomembr. 40 (2008) 9-18
115. Hansen H.S., Moesgaard B., Hansen H.H., and Petersen G. N-Acylethanolamines and precursor phospholipids-relation to cell injury. Chem. Phys. Lipids 108 (2000) 135-150
116. Devane W.A., Hanuš L., Breuer A., Pertwee R.G., Stevenson L.A., Griffin G., Gibson D., Mandelbaum A., Etinger A., and Mechoulam R. Isolation and structure of a brain constituent that binds to the cannabinoid receptor. Science 258 (1992) 1946-1949
117. Wasilewski M., Wie{ogonek}ckowski M.R., Dymkowska D., and Wojtczak L. Effects of N-acylethanolamines on mitochondrial energetics and permeability transition. Biochim. Biophys. Acta 1657 (2004) 151-163
118. Wasilewski M., and Wojtczak L. Effects of N-acylethanolamines on the respiratory chain and production of reactive oxygen species in heart mitochondria. FEBS Lett. 579 (2005) 4724-4728
119. Sarker K.P., Obara S., Nakata M., Kitajima I., and Maruyama I. Anandamide induces apoptosis of PC-12 cells: involvement of superoxide and caspase-3. FEBS Lett. 472 (2000) 39-44
120. 9-tetrahydrocannabinol. Eur. J. Pharmacol. 395 (2000) 1-7
121. Won J.S., and Singh I. Sphingolipid signaling and redox regulation. Free Radic. Biol. Med. 40 (2006) 1875-1888
122. Gudz T.I., Tserng K.Y., and Hoppel C.L. Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide. J. Biol. Chem. 272 (1997) 24151-24158
123. García-Ruiz C., Colell A., Marí M., Morales A., and Fernández-Checa J.C. Direct effect of ceramide on the mitochondrial electron transport chain leads to generation of reactive oxygen species. J. Biol. Chem., 272 (1997) 11369-11377
124. Ghafourifar P., Klein S.D., Schucht O., Schenk U., Pruschy M., Rocha S., and Richter C. Ceramide induces cytochrome c release from isolated mitochondria. J. Biol. Chem. 274 (1999) 6080-6084
125. Di Paola M., Cocco T., and Lorusso M. Ceramide interaction with the respiratory chain of heart mitochondria. Biochemistry 39 (2000) 6660-6668
126. Hannun A.Y. Functions of ceramide in coordinating cellular responses to stress. Science 274 (1996) 1855-1859
127. Kolesnick R., and Golde D.W. The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling. Cell 77 (1994) 325-328
128. Corda S., Laplace C., Vicaut E., and Duranteau J. Rapid reactive oxygen species production by mitochondria in endothelial cells exposed to tumor necrosis factor-α is mediated by ceramide. Am. J. Respir. Cell Mol. Biol. 24 (2001) 762-768
129. Therade-Matharan S., Laemmel E., Carpentier S., Obata Y., Levade T., Duranteau J., and Vicaut E. Reactive oxygen species production by mitochondria in endothelial cells exposed to reoxygenation after hypoxia and glucose depletion is mediated by ceramide. Am. J. Physiol. Regul. Integr. Comp. Physiol. 289 (2005) R1756-R1762
130. Six D.A., and Dennis E.A. The expanding superfamily of phospholipase A2 enzymes: classification and characterization. Biochim. Biophys. Acta 1488 (2000) 1-19
131. Adibhatla R.M., and Hatcher J.F. Phospholipase A2, reactive oxygen species, and lipid peroxidation in cerebral ischemia. Free Radic. Biol. Med. 40 (2006) 376-387
132. Mathisen G.H., Thorkildsen I.H., and Paulsen R.E. Secretory PLA2-IIA and ROS generation in peripheral mitochondria are critical for neuronal death. Brain Res. 1153 (2007) 45-51
133. 2 localizes in and protects mitochondria during apoptotic induction by staurosporine. J. Biol. Chem. 281 (2006) 22275-22288
134. Chan P.H., and Fishman R.A. Transient formation of superoxide radicals in polyunsaturated fatty acid-induced brain swelling. J. Neurochem. 35 (1980) 1004-1007
135. Chan P.H., Chen S.F., and Yu A.C.H. Induction of intracellular superoxide radical formation by arachidonic acid and by polyunsaturated fatty acids in primary astrocytic cultures. J. Neurochem. 50 (1988) 1185-1193
136. Lu G., Greene E.L., Nagai T., and Egan B.M. Reactive oxygen species are critical in the oleic acid-mediated mitogenic signalling pathway in vascular smooth muscle cells. Hypertension 32 (1998) 1003-1010
137. Rachek L.I., Musiyenko S.I., LeDoux S.P., and Wilson G.L. Palmitate induced mitochondrial deoxyribonucleic acid damage and apoptosis in L6 rat skeletal muscle cells. Endocrinology 148 (2007) 293-299
138. 2+ handling in adult control and ob/ob cardiomyocytes: Impact of mitochondrial reactive oxygen species. Diabetes 56 (2007) 1136-1142
139. Ishola Jr. D.A., Post J.A., van Timmeren M.M., Bakker S.J.L., Goldschmedding R., Koomans H.A., Braam B., and Joles J.A. Albumin-bound fatty acids induce mitochondrial oxidant stress and impair antioxidant responses in proximal tubular cells. Kidney Int. 70 (2006) 724-731
140. Dymkowska D., Szczepanowska J., Wie{ogonek}ckowski M.R., and Wojtczak L. Short-term and long-term effects of fatty acids in rat hepatoma AS-30D cells: the way to apoptosis. Biochim. Biophys. Acta 1763 (2006) 152-163
141. Srivastava S., and Chan C. Hydrogen peroxide and hydroxyl radicals mediate palpitate-induced cytotoxicity to hepatoma cells: relation to mitochondrial permeability transition. Free Radic. Res. 41 (2007) 38-49
142. Guo W., Xie W., and Han J. Modulation of adipocyte lipogegenesis by octanoate: involvement of reactive oxygen species. Nutr. Metab. (London) 3 (2006) 30-38
143. Aitken R.J., Wingate J.K., De Iuliis G.N., Koppers A.J., and McLaughlin E.A. Cis-unsaturated fatty acid stimulate reactive oxygen species generation and lipid peroxidation in human spermatozoa. J. Clin. Endocrinol. Metab. 91 (2006) 4151-4163
144. Brash A.R. Lipoxygenases: occurrence, functions, catalysis, and acquisition of substrate. J. Biol. Chem. 274 (1999) 23679-23682
145. Cosgrove J.P., Church D.F., and Pryor W.A. The kinetics of the autoxidation of polyunsaturated fatty acids. Lipids 22 (1987) 299-304
146. Toborek M., Malecki A., Garrido R., Mattson M.P., Hennig B., and Young B. Arachidonic acid-induced oxidative injury to cultured spinal cord neurons. J. Neurochem. 73 (1999) 684-692
147. Curnutte J.T., Badwey J.A., Robinson J.M., Karnovsky M.J., and Karnovsky M.L. Studies on the mechanism of superoxide release from human neutrophils stimulated with arachidonate. J. Biol. Chem. 259 (1984) 11852-11857
148. Myers M.A., McPhail L.C., and Snyderman R. Redistribution of protein kinase C activity in human monocytes: correlation with activation of the respiratory burst. J. Immunol. 135 (1985) 3411-3416
149. Corley S.J., and Rosoff P.M. Unsaturated fatty acids and lipoxygenase products regulate phagocytic NADPH oxidase activity by a nondetergent mechanism. J. Lab. Clin. Med. 118 (1991) 343-351
150. Hardy S.J., Ferrante A., Poulus A., Robinson B.S., Johnson D.W., and Murray A.W. Effect of exogenous fatty acids with greater than 22 carbon atoms (very long chain fatty acids) on superoxide production by human neutrophils. J. Immunology 153 (1994) 1754-1761
151. Kakinuma K. Effects of fatty acids on the oxidative metabolism of leukocytes. Biochim. Biophys. Acta 348 (1974) 76-85
152. Kakinuma K., and Minakami S. Effects of fatty acids on superoxide radical generation in leukocytes. Biochim. Biophys. Acta 538 (1978) 50-59
153. Inoguchi T., Li P., Umeda F., Yu H.Y., Kakimoto M., Imamura M., Aoki T., Etoh T., Hashimoto T., Naruse M., Sano H., Utsumi H., and Nawata H. High glucose level and free fatty acid stimulate reactive oxygen species production through protein kinase C-dependent activation of NAD(P)H oxidase in cultured vascular cells. Diabetes 49 (2000) 1939-1945
154. Rossary A., Arab K., and Steghens J.P. Polyunsaturated fatty acids modulate NOX4 anion superoxide production in human fibroblasts. Biochem. J. 406 (2007) 77-83
155. 18 fatty acids in Jurkat and Raji cells. Clin. Sci. 108 (2005) 245-253
156. Babior B.M. The NADPH oxidase of endothelial cells. IUBMB Life 50 (2002) 267-269
157. Lassègue B., and Clempus R.E. Vascular NAD(P)H oxidases: specific features, expression, and regulation. Am. J. Physiol. Regul. Integr. Comp. Physiol. 285 (2003) R277-R297
158. Gonzalez C., Agapito M.T., Rocher A., Gonzalez-Martin M.C., Vega-Agapito V., Gomez-Niño A., Rigual R., Castañeda J., and Obeso A. Chemoreception in the context of the general biology of ROS. Respir. Physiol. Neurobiol. 157 (2007) 30-44
159. Li J.M., and Shah A.M. Endothelial cell superoxide generation: regulation and relevance for cardiovascular pathophysiology. Am. J. Physiol. Regul. Integr. Comp. Physiol. 287 (2004) R1014-R1030
160. Shiose A., and Sumimoto H. Arachidonic acid and phosphorylation synergistically induce a conformational change of p47phos to activate phagocyte NADPH oxidase. J. Biol. Chem. 275 (2000) 13793-13801
161. Nigorikawa K., Okamura N., and Hazeki O. The effect of anionic amphiphiles on the recruitment of Rac in neutrophils. J. Biochem. (Tokyo) 136 (2004) 463-470
162. Taylor R.M., Foubert T.R., Burritt J.B., Baniulis D., McPhail L.C., and Jesaitis A.J. Anionic amphiphile and phospholipid-induced conformational changes in human neutrophil flavocytochrome b observed by fluorescence resonance energy transfer. Biochim. Biophys. Acta 1663 (2004) 201-213
163. Doussiere J., Bouzidi F., Poinas A., Gaillard J., and Vignais P.V. Kinetic study of the activation of the neutrophil NADPH oxidase by arachidonic acid. Antagonistic effects of arachidonic acid and phenylarsine oxide. Biochemistry 38 (1999) 16394-16406
164. Zhang X., Dong F., Ren J., Driscoll M.J., and Culver B. High dietary fat induces NADPH oxidase-associated oxidative stress and inflammation in rat cerebral cortex. Exp. Neurol. 191 (2005) 318-325
165. Kalmijn S. Fatty acid intake and the risk of dementia and cognitive decline: a review of clinical and epidemiological studies. J. Nutr. Health Aging 4 (2000) 202-207
166. Grant W.B., Campbell A., Itzhaki R.F., and Savory J. The significance of environmental factors in the etiology of Alzheimer's disease. J. Alzheimer's Dis. 44 (2002) 179-189
167. Mazière C., Conte M.A., Degonville J., Ali D., and Mazière J.C. Cellular enrichment with polyunsaturated fatty acids induces an oxidative stress and activates the transcription factors AP1and NFkB. Biochem. Biophys. Res. Commun. 265 (1999) 116-122
168. Benani A., Troy S., Carmona M.C., Fioramonti X., Lorsignol A., Leloup C., Casteilla L., and Pénicaud L. Role for mitochondrial reactive oxygen species in brain lipid sensing. Diabetes 56 (2007) 152-160
169. Simon H.U., Haj-Yehia H., and Levi-Schaffer F. Role of reactive oxygen species (ROS) in apoptosis induction. Apoptosis 5 (2000) 415-418
170. Bauer G. Signaling and proapoptotic functions of transformed cell-derived reactive oxygen species. Prostaglandins Leukot. Essent. Fat. Acids 66 (2002) 41-56
171. Fleury C., Mignotte G., and Vayssière J.L. Mitochondrial reactive oxygen species in cell death signaling. Biochimie 84 (2002) 131-141
172. Arita K., Kobuchi H., Utsumi T., Takehara Y., Akiyama J., Horton A.A., and Utsumi K. Mechanism of apoptosis in HL-60 cells induced by n-3 and n-6 polyunsaturated fatty acids. Biochem. Pharmacol. 62 (2001) 821-828
173. Pompeia C., Freitas J.J., Kim J.S., Zyngier S.B., and Curi R. Arachidonic acid cytotoxicity in leukocytes: implications of oxidative stress and eicosanoid synthesis. Biol. Cell 94 (2002) 251-265
174. Yi S.J., Choi H.J., Yoo J.O., Yuk J.S., Jung H.I., Lee S.H., Han J.A., Kim Y.M., and Ha K.S. Arachidonic acid activates tissue transglutaminase and stress fiber formation via intracellular reactive oxygen species. Biochem. Biophys. Res. Commun. 325 (2004) 819-826
175. Giulivi C., Boveris A., and Cadenas E. Hydroxyl radical generation during mitochondrial electron transfer and the formation of 8-hydroxydesoxyguanosine in mitochondrial DNA. Arch. Biochem. Biophys. 316 (1995) 909-916
176. Grishko V., Rachek L., Musiyenko S., LeDoux S.P., and Wilson G.L. Involvement of mtDNA damage in free fatty acid-induced apoptosis. Free Radic. Biol. Med. 38 (2005) 755-762
177. Bell E.L., Emerling B.M., and Chandel N.S. Mitochondrial regulation of oxygen sensing. Mitochondrion 5 (2005) 322-332
178. Chandel N.S., and Schumacker P.T. Cellular oxygen sensing by mitochondria: old questions, new insight. J. Appl. Physiol. 88 (2000) 1880-1889
179. Ueno K., Tanaka Y., and Ando S. Release of free fatty acids from rat cerebral synaptosomes under in vitro hypoxia. Neurosci. Lett. 84 (1988) 297-301
180. Sun D., and Gilboe D.D. Ischemia-induced changes in cerebral mitochondrial free fatty acids, phospholipids, and respiration in the rat. J. Neurochem. 62 (1994) 1921-1928
181. Guzy R.D., and Schumacker P.T. Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia. Exp. Physiol. 91 (2006) 807-819
182. Hoffman D.L., Salter J.D., and Brookes P.S. Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: implications for hypoxic cell signalling. Am. J. Physiol. Circ. Physiol. 292 (2007) H101-H108