Influence of pulmonary arterial endothelial cells on quinone redox status: Effect of hyperoxia-induced NAD(P)H:quinone oxidoreductase

American Journal of Physiology - Lung Cellular and Molecular Physiology

Volumn 290, Issue 3, 2006, Pages

  Merker, Marilyn P ^a,d   Audi, Said H ^a,b,d   Bongard, Robert D ^a   Lindemer, Brian J ^a   Krenz, Gary S ^c  

^a MEDICAL COLLEGE OF WISCONSIN   (United States)

^b Medical College of Wisconsin and Marquette University   (United States)

^c MARQUETTE UNIVERSITY   (United States)

^d CLEMENT J ZABLOCKI VETERANS AFFAIRS MEDICAL CENTER   (United States)

Author keywords

Duroquinone; Mathematical modeling; Pulmonary endothelial cells

Indexed keywords

DUROQUINOL; DUROQUINONE; OXYGEN; POTASSIUM FERRICYANIDE; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; BENZOQUINONE DERIVATIVE; DIAGNOSTIC AGENT; FERRICYANIDE; HYDROQUINONE DERIVATIVE; NQO1 PROTEIN, HUMAN;

ANIMAL CELL; ARTERY ENDOTHELIUM; ARTICLE; CELL FUNCTION; CONTROLLED STUDY; CYTOSOL; ENDOTHELIUM CELL; ENZYME ACTIVITY; HYPEROXIA; MATHEMATICAL MODEL; MITOCHONDRIAL ENERGY TRANSFER; NONHUMAN; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PULMONARY ARTERY; ANIMAL; CATTLE; CHEMISTRY; DOMINANT GENE; ENZYMOLOGY; HUMAN; LUNG CIRCULATION; METABOLISM; OXIDATION REDUCTION REACTION; OXYGEN CONSUMPTION; VASCULAR ENDOTHELIUM;

ANIMALS; BENZOQUINONES; CATTLE; CYTOSOL; ENDOTHELIUM, VASCULAR; FERRICYANIDES; GENES, DOMINANT; HUMANS; HYDROQUINONES; HYPEROXIA; NAD(P)H DEHYDROGENASE (QUINONE); OXIDATION-REDUCTION; OXYGEN CONSUMPTION; PULMONARY ARTERY; PULMONARY CIRCULATION;

EID: 33644947752     PISSN: 10400605     EISSN: 15221504     Source Type: Journal    
DOI: 10.1152/ajplung.00302.2005     Document Type: Article

References (72)

1. Anusevicius Z, Sarlauskas J, and Cenas N. Two-electron reduction of quinones by rat liver NAD(P)H:quinone oxidoreductase: quantitative structure-activity relationships. Arch Biochem Biophys 404: 254-262, 2002.
2. Audi SH, Bongard R, Krenz GS, Rickaby DA, Haworth ST, Eisenhauer J, Roerig DL, and Merker MP. Effect of chronic hyperoxic exposure on duroquinone reduction in adult rat lungs. Am J Physiol Lung Cell Mol Physiol 289: L788-L797, 2005.
3. Audi SH, Bongard RD, Dawson CA, Siegel D, Roerig DL, and Merker MP. Duroquinone reduction during passage through the pulmonary circulation. Am J Physiol Lung Cell Mol Physiol 285: L1116-L1131, 2003.
4. Audi SH, Bongard RD, Okamoto Y, Merker MP, Roerig DL, and Dawson CA. Pulmonary reduction of an intravascular redox polymer. Am J Physiol Lung Cell Mol Physiol 280: L1290-L1299, 2001.
5. Audi SH, Zhao H, Bongard RD, Hogg N, Kettenhofen NJ, Kalyanaraman B, Dawson CA, and Merker MP. Pulmonary arterial endothelial cells affect the redox status of coenzyme Q0. Free Radic Biol Med 34: 892-907, 2003.
6. Badary OA, Awad AS, Abdel-Maksoud S, and Hamada FM. Cardiac DT-diaphorase contributes to the detoxification system against doxorubicin-induced positive inotropic effects in guinea-pig isolated atria. Clin Exp Pharmacol Physiol 31: 856-861, 2004.
7. Beyer RE, Segura-Aguilar J, di Bernardo S, Cavazzoni M, Fato R, Fiorentini D, Galli MC, Setti M, Landi L, and Lenaz G. The two-electron quinone reductase DT-diaphorase generates and maintains the antioxidant (reduced) form of coenzyme Q in membranes. Mol Aspects Med 18, Suppl: S15-S23, 1997.
8. Bongard RD, Merker MP, Shundo R, Okamoto Y, Roerig DL, Linehan JH, and Dawson CA. Reduction of thiazine dyes by bovine pulmonary arterial endothelial cells in culture. Am J Physiol Lung Cell Mol Physiol 269: L78-L84, 1995.
9. Boveris A, Oshino R, Erecinska M, and Chance B. Reduction of mitochondrial components by durohydroquinone. Biochim Biophys Acta 245: 1-16, 1971.
10. Britigan BE, Roeder TL, and Shasby DM. Insight into the nature and site of oxygen centered free radical generation by endothelial cell monolayers using a novel spin trapping technique. Blood 79: 699 -707, 1992.
11. Brunmark A and Cadenas E. Redox and addition chemistry of quinoid compounds and its biological implications. Free Radic Biol Med 7: 435-477, 1989.
12. Cadenas E. Antioxidant and prooxidant functions of DT-diaphorase in quinone metabolism. Biochem Pharmacol 49: 127-140, 1995.
13. Cadenas E, Boveris A, Ragan CI, and Stoppani AOM. Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria. Arch Biochem Biophys 180: 248-257, 1997.
14. Cadenas E, Hochstein P, and Ernster L. Pro- and antioxidant functions of quinones and quinone reductases in mammalian cells. Adv Enzymol Relat Areas Mol Biol 65: 97-146, 1992.
15. Chan TS, Teng S, Wilson JX, Galati G, Khan S, and O'Brien PJ. Coenzyme Q cytoprotective mechanisms for mitochondrial complex I cytopathies involves NAD(P)H: quinone oxidoreductase 1(NQO1). Free Radic Res 36: 421-427, 2002.
16. Chen XL, Varner SE, Rao AS, Grey JY, Thomas S, Cook CK, Wasserman MA, Medford RM, Jaiswal AK, and Kunsch C. Laminar flow induction of antioxidant response element-mediated genes in endothelial cells. A novel anti-inflammatory mechanism. J Biol Chem 278: 703-711, 2003.
17. Cho HY, Jedlicka AE, Reddy SP, Kensler TW, Yamamoto M, Zhang LY, and Kleeberger SR. Role of NRF2 in protection against hyperoxic lung injury in mice. Am J Respir Cell Mol Biol 26: 175-182, 2002.
18. Cho HY, Reddy SP, Debiase A, Yamamoto M, and Kleeberger SR. Gene expression profiling of NRF2-mediated protection against oxidative injury. Free Radic Biol Med 38: 325-343, 2005.
19. Crapo JD, Barry BE, Foscue HA, and Shelburne J. Structural and biochemical changes in rat lungs occurring during exposures to lethal and adaptive doses of oxygen. Am Rev Respir Dis 122: 123-143, 1980.
20. De Haan LHJ, Boerboom AMJF, Rietjens IMCM, van Capelle D, De Ruijter AJM, Jaiswal AK, and Aarts JMMJ. A physiological threshold for protection against menadione toxicity by human NAD(P)H:quinone oxidoreductase (NQO1) in Chinese hamster ovary (CHO) cells. Biochem Pharmacol 64: 1597-1603, 2002.
21. De Keulenaer GW, Chappell DC, Ishizaka N, Nerem RM, Alexander RW, and Griendling KK. Oscillatory and steady laminar shear stress differentially affect human endothelial redox state: role of a superoxide-producing NADH oxidase. Circ Res 82: 1094-1101, 1998.
22. Dinkova-Kostova AT and Talalay P. Persuasive evidence that quinone reductase type I (DT diaphorase) protects cells against the toxicity of electrophiles and reactive forms of oxygen. Free Radic Biol Med 29: 231-240, 2001.
23. Floreani M, Napoli E, and Palatini P. Protective action of cardiac DT-diaphorase against menadione toxicity in guinea pig isolated atria. Biochem Pharmacol 60: 601-605, 2000.
24. Freeman BA and Crapo JD. Hyperoxia increases oxygen radical production in rat lungs and lung mitochondria. J Biol Chem 256: 10986-10992, 1981.
25. Gaikwad A, Long DJ, Stringer JL, and Jaiswal AK. In vivo role of NAD(P)H:quinone oxidoreductase 1 (NQO1) in the regulation of intracellular redox state and accumulation of abdominal adipose tissue. J Biol Chem 276: 22559-22564, 2001.
26. Gille L, Staniek K, and Nohl H. Effects of tocopheryl quinone on the heart: model experiments with xanthine oxidase, heart mitochondria, and isolated perfused rat hearts. Free Radic Biol Med 30: 865-876, 2001.
27. Gustafson DL and Pritsos CA. Oxygen radical generation and alkylating ability of mitomycin C bioactivated by xanthine dehydrogenase. Proc West Pharmacol Soc 35: 147-151, 1992.
28. Hassoun PM, Yu FS, Shedd AL, Zulueta JJ, Thannickal VJ, Lanzillo JJ, and Fanburg BL. Regulation of endothelial cell xanthine dehydrogenase xanthine oxidase gene expression by oxygen tension. Am J Physiol Lung Cell Mol Physiol 266: L163-L171, 1994.
29. Ho YS. Transgenic and knockout models for studying the role of lung antioxidant enzymes in defense against hyperoxia. Am J Respir Crit Care Med 166: S51-S56, 2002.
30. Hosoya T, Maruyama A, Kang MI, Kawatani Y, Shibata T, Uchida K, Warabi E, Noguchi N, Itoh K, and Yamamoto M. Differential responses of the Nrf2-Keap1 system to laminar and oscillatory shear stresses in endothelial cells. J Biol Chem 280: 27244-27250, 2005.
31. Jaiswal AK. Antioxidant response element. Biochem Pharmacol 48: 439-444, 1994.
32. Jaiswal AK. Regulation of genes encoding NAD(P)H:quinone oxidoreductases. Free Radic Biol Med 29: 254-262, 2000.
33. James AM, Cocheme HM, Smith RAJ, and Murphy MP. Interactions of mitochondria-targeted and untargeted ubiquinones with the mitochondrial respiratory chain and reactive oxygen species: implications for the use of exogenous ubiquinones as therapies and experimental tools. J Biol Chem 280: 21295-21312, 2005.
34. Jones W, Li X, Qu ZC, Perriott L, Whitesell RR, and May JM. Uptake, recycling, and antioxidant actions of α-lipoic acid in endothelial cells. Free Radic Biol Med 33: 83-93, 2002.
35. Jornot L and Junod AF. Response of human endothelial cell antioxidant enzymes to hyperoxia. Am J Respir Cell Mol Biol 6: 107-115, 1992.
36. Joseph P, Long DJ, Klein-Szanto AJ, and Jaiswal AK. Role of NAD(P)H:quinone oxidoreductase 1 (DT diaphorase) in protection against quinone toxicity. Biochem Pharmacol 60: 207-214, 2000.
37. Lind C, Cadenas E, Hochstein P, and Ernster L. DTdiaphorase: purification, properties, and function. Methods Enzymol 186: 287-301, 1990.
38. Lind C, Hochstein P, and Ernster L. DT-diaphorase as a quinone reductase: a cellular control device against semiquinone and superoxide radical formation. Arch Biochem Biophys 216: 178-185, 1982.
39. Long DJ, Gaikwad A, Multani A, Pathak S, Montgomery CA, Gonzalez FJ, and Jaiswal AK. Disruption of the NAD(P)H:quinone oxidoreductase 1 (NQO1) gene in mice causes myelogenous hyperplasia. Cancer Res 62: 3030-3036, 2002.
40. Manchenko GP. Handbook of Detection of Enzymes in Electrophoretic Gels. Washington, DC: CRC, 2003.
41. May JM, Qu Z, Neel DR, and Li X. Recycling of vitamin C from its oxidized forms by human endothelial cells. Biochim Biophys Acta 1640: 153-161, 2003.
42. Merker MP, Audi SH, Brantmeier BM, Nithipatikom K, Goldman RS, Roerig DL, and Dawson CA. Proline in vasoactive peptides: consequences for peptide hydrolysis in the lung. Am J Physiol Lung Cell Mol Physiol 276: L341-L350, 1999.
43. Merker MP, Bongard RD, Kettenhofen NJ, Okamoto Y, and Dawson CA. Intracellular redox status affects transplasma membrane electron transport in pulmonary arterial endothelial cells. Am J Physiol Lung Cell Mol Physiol 282: L36-L43, 2002.
44. Merker MP, Bongard RD, Krenz GS, Zhao H, Fernandes V, Kalyanaraman B, Hogg N, and Audi SH. Impact of pulmonary arterial endothelial cells on duroquinone redox status. Free Radic Biol Med 37: 86-103, 2004.
45. Merker MP, Bongard RD, Linehan JH, Okamoto Y, Vyprachticky D, Brantmeier BM, Roerig DL, and Dawson CA. Pulmonary endothelial thiazine uptake: separation of cell surface reduction from intracellular reoxidation. Am J Physiol Lung Cell Mol Physiol 272: L673-L680, 1997.
46. Merker MP, Olson LE, Bongard RD, Patel MK, Linehan JH, and Dawson CA. Ascorbate-mediated transplasma membrane electron transport in pulmonary arterial endothelial cells. Am J Physiol Lung Cell Mol Physiol 274: L685-L693, 1998.
47. Moody EJ, Simon BA, and Johns RA. Therapeutic gases. In: The Pharmacological Basis of Therapeutics, edited by Hardman JG, Limbird LE, and Gilman AG. New York: McGraw-Hill, 2001, p. 385-397.
48. 2+ release induced by benzoquinone derivatives. Arch Biochem Biophys 259: 283-295, 1987.
49. Nemeikaite A and Cenas N. The changes of prooxidant and antioxidant enzyme activities in bovine leukemia virus-transformed cells. Their influence on quinone cytotoxicity. FEBS Lett 326: 65-68, 1993.
50. Neuzil J, Witting PK, and Stocker R. α-Tocopheryl hydroquinone is an efficient multifunctional inhibitor of radical-initiated oxidation of low density lipoprotein lipids. Proc Natl Acad Sci USA 94: 7885-7890, 1997.
51. O'Brien PJ. Molecular mechanisms of quinone cytotoxicity. Chem Biol Interact 80: 1-41, 1991.
52. Okamura T, Fujioka H, Ayajiki K, and Toda N. Modifications by superoxide-generating agent, neurotransmitters and neuromodulators of nitroxidergic nerve function in monkey cerebral arteries. J Pharmacol Exp Ther 286: 1321-1325, 1998.
53. Parinandi NL, Kleinberg MA, Usatyuk PV, Cummings RJ, Pennathur A, Cardounel AJ, Zweier JL, Garcia JG, and Natarajan V. Hyperoxia-induced NAD(P)H oxidase activation and regulation by MAP kinases in human lung endothelial cells. Am J Physiol Lung Cell Mol Physiol 284: L26-L38, 2003.
54. Perkowski S, Sun J, Singhal S, Santiago J, Leikauf GD, and Albelda SM. Gene expression profiling of the early pulmonary response to hyperoxia in mice. Am J Respir Cell Mol Biol 28: 682-696, 2003.
55. Prestera T and Talalay P. Electrophile and antioxidant regulation of enzymes that detoxify carcinogens. Proc Natl Acad Sci USA 92: 8965-8969, 1995.
56. Rosen GM and Freeman BA. Detection of superoxide generated by endothelial cells. Proc Natl Acad Sci USA 81: 7269-7273, 1988.
57. Ross D. Quinone reductases multitasking in the metabolic world. Drug Metab Rev 36: 639-654, 2004.
58. Ruzicka FJ and Crane FL. Quinone interaction with the respiratory chain-linked NADH dehydrogenase of beef heart mitochondria. II. Duroquinone reductase activity. Biochim Biophys Acta 226: 221-233, 1971.
59. Sanders SP, Zweier JL, Kuppusamy P, Harrison SJ, Bassett DJ, Gabrielson EW, and Sylvester JT. Hyperoxic sheep pulmonary microvascular endothelial cells generate free radicals via mitochondrial electron transport. J Clin Invest 91: 46-52, 1993.
60. Schmalix WA, Lang D, Schneider A, Bocker R, Greim H, and Doehmer J. Stable expression and coexpression of human cytochrome P450 oxidoreductase and cytochrome P450 1A2 in V79 Chinese hamster cells: sensitivity to quinones and biotransformation of 7-alkoxyresorufins and triazines. Drug Metab Dispos 24: 1314-1319, 1996.
61. Shaw PM, Reiss A, Adesnik M, Nebert DW, Schembri J, and Jaiswal AK. The human dioxin-inducible NAD(P)H: quinone oxidoreductase cDNA-encoded protein expressed in COS-1 cells is identical to diaphorase 4. Eur J Biochem 195: 171-176, 1991.
62. Shi MM, Iwamoto T, and Forman HJ. γ-Glutamylcysteine synthetase and GSH increase in quinone-induced oxidative stress in BPAEC. Am J Physiol Lung Cell Mol Physiol 267: L414-L421, 1994.
63. Siegel D, Bolton EM, Burr JA, Liebler DC, and Ross D. The reduction of α-tocopherolquinone by human NAD(P)H:quinone oxidoreductase: the role of α-tocopherolhydroquinone as a cellular antioxidant. Mol Pharmacol 52: 300-305, 1997.
64. Siegel D, Franklin WA, and Ross D. Immunohistochemical detection of NAD(P)H:quinone oxidoreductase in human lung and lung tumors. Clin Cancer Res 4: 2065-2070, 1998.
65. Siegel D, Gustafson DL, Dehn DL, Han JY, Boonchoong P, Berliner LJ, and Ross D. NAD(P)H:quinone oxidoreductase 1: role as a superoxide scavenger. Mol Pharmacol 65: 1238-1247, 2004.
66. Tampo Y, Tsukamoto M, and Yonaha M. Superoxide production from paraquat evoked by exogenous NADPH in pulmonary endothelial cells. Free Radic Biol Med 27: 588-595, 1999.
67. Tanaka T, Okamura T, Handa J, and Toda N. Neurogenic vasodilation mediated by nitric oxide in porcine cerebral arteries. J Cardiovasc Pharmacol 33: 56-64, 1999.
68. Terada LS, Beehler CJ, Banerjee A, Brown JM, Grosso MA, Harken AH, McCord JM, and Repine JE. Hyperoxia and self- or neutrophil-generated O2 metabolites inactivate xanthine oxidase. J Appl Physiol 65: 2349-2353, 1988.
69. Whitney PL and Frank L. Does lung NAD(P)H:quinone reductase (DT-diaphorase) play an antioxidant enzyme role in protection from hyperoxia? Biochim Biophys Acta 1156: 275-282, 1993.
70. Wroblewski F and LaDue JS. Lactic dehydrogenase activity in blood. Proc Soc Exp Biol Med 90: 210-213, 1955.
71. Yee SB and Pritsos CA. Comparison of oxygen radical generation from the reductive activation of doxorubicin, streptonigrin, and menadione by xanthine oxidase and xanthine dehydrogenase. Arch Biochem Biophys 347: 235-241, 1997.
72. Zar JH. Biostatistical Analysis. Englewood Cliffs, NJ: Prentice-Hall, 1984, p. 292-305.