Pulmonary arterial endothelial cells affect the redox status of coenzyme Q0

Free Radical Biology and Medicine

Volumn 34, Issue 7, 2003, Pages 892-907

  Audi, Said H ^a,b   Zhao, Hongtao ^b   Bongard, Robert D ^b   Hogg, Neil ^b   Kettenhofen, Nicholas J ^b   Kalyanaraman, Balaraman ^b   Dawson, Christopher A ^a,b,c   Merker, Marilyn P ^a,b,c  

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

^b MEDICAL COLLEGE OF WISCONSIN   (United States)

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

Author keywords

Electron paramagnetic resonance; Endothelium; Free radicals; High performance liquid chromatography; Kinetic model; Quinone; Quinone reductases; Transplasma membrane electron transport

Indexed keywords

MEMBRANE PROTEIN; QUINOL; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (QUINONE); SEMIQUINONE; UBIQUINONE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTERY ENDOTHELIUM; ARTICLE; CELL CULTURE; CELL SURFACE; CULTURE MEDIUM; ELECTRON SPIN RESONANCE; ENDOTHELIUM CELL; EXTRACELLULAR SPACE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; LUNG ARTERY; LUNG ENDOTHELIUM; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN ISOLATION; SPECTROPHOTOMETRY;

EID: 0037376429     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(03)00025-X     Document Type: Article

References (72)

1. Gillis C.N. Pharmacological aspects of metabolic processes in the pulmonary microcirculation. Ann. Rev. Pharmacol. Toxicol. 26:1986;183-200.
2. Dawson C.A., Linehan J.H. Biogenic amines. Massaro D. Lung biology in health and disease, vol. 41, lung cell biology. 1989;1091-1139 Marcel Dekker, Inc, New York.
3. Audi S.H., Bongard R.D., Okamoto Y., Merker M.P., Roerig D.L., Dawson C.A. Pulmonary reduction of an intravascular redox polymer. Am. J. Physiol. Lung Cell Mol. Physiol. 280:2001;L1290-L1299.
4. Bongard R.D., Krenz G.S., Linehan J.H., Roerig D.L., Merker M.P., Widell J.L., Dawson C.A. Reduction and accumulation of methylene blue by the lung. J. Appl. Physiol. 77:1994;1480-1491.
5. Bongard R.D., Merker M.P., Shundo R., Okamoto Y., Roerig D.L., Linehan J.H., Dawson C.A. Reduction of thiazine dyes by bovine pulmonary arterial endothelial cells in culture. Am. J. Physiol. 269:(1 Part 1):1995;L78-L84.
6. Merker M.P., Bongard R.D., Dawson C.A. Pulmonary endothelial surface redox activities roles in propagation and protection from injury . Wong H.R., Shanley T.P. Molecular and cellular biology of critical care medicine. 2001;133-148 Kluwer Academic Publishers, New York.
7. Merker M.P., Olson L.E., Bongard R.D., Patel M.K., Linehan J.H., Dawson C.A. Ascorbate-mediated transplasma membrane electron transport in pulmonary arterial endothelial cells. Am. J. Physiol. 274:(5 Part 1):1998;L685-L693.
8. Jones W., Li X., Qu Z.C., Perriott L., Whitesell R.R., May J.M. Uptake, recycling, and antioxidant actions of α-lipoic acid in endothelial cells. Free Radic. Biol. Med. 33:2002;83-93.
9. May J.M., Qu Z., Li X. Requirement for GSH in recycling of ascorbic acid in endothelial cells. Biochem. Pharmacol. 62:2001;873-881.
10. Rosen G.M., Freeman B.A. Detection of superoxide generated by endothelial cells. Proc. Natl. Acad. Sci. USA. 81:1984;7269-7273.
11. Brunmark A., Cadenas E. Redox and addition chemistry of quinoid compounds and its biological implications. Free Radic. Biol. Med. 7:1989;435-477.
12. Kagan V.E., Serbinova E.A., Koynova G.M., Kitanova S.A., Tyurin V.A., Stoytchev T.S., Quinn P.J., Packer L. Antioxidant action of ubiquinol homologues with different isopreniod chain length in biomembranes. Free Radic. Biol. Med. 9:1990;117-126.
13. Powis G. Metabolism and reactions of quinoid anticancer agents. Pharmacol. Ther. 35:(1-2):1987;57-162.
14. Squidrito G., Cueto R., Dellinger B., Pryor W.A. Quinoid redox cycling as a mechanism for sustained free radical generation by inhaled airborne particulate matter. Free Radic. Biol. Med. 31:2001;1132-1138.
15. Bolton J.L., Trush M.A., Penning T.M., Dryhurst G., Monks T.J. Role of quinones in toxicology. Chem. Res. Toxicol. 13:2000;135-160.
16. Jaiswal A.K. Regulation of genes encoding NAD(P)H quinone oxidoreductases . Free Radic. Biol. Med. 29:2000;254-262.
17. Lind C., Cadenas E., Hochstein P., Ernster L. DT-diaphorase purification, properties, and function . Methods Enzymol. 186:1990;287-301.
18. Joseph P., Long D.J. II, Klein-Szanto A.J., Jaiswal A.K. Role of NAD(P)H:quinone oxidoreductase 1 (DT-diaphorase) in protection against quinone toxicity. Biochem. Pharmacol. 60:(2):2000;207-214.
19. Forthoffer N., Gomez-Diaz C., Bello R.I., Buron M.I., Martin S.F., Rodriguez-Aguilera J.C., Navas P., Villalba J.M. A novel plasma membrane quinone reductase and NAD(P)H quinone oxidoreductase 1 are upregulated by serum withdrawal in human promyelocytic HL-60 cells . J. Bioenerg. Biomembr. 34:2002;209-219.
20. Kumagai Y., Nakajima H., Midorikawa K., Homma-Takeda S., Shimojo N. Inhibition of nitric oxide formation by neuronal nitric oxide synthase by quinones nitric oxide synthase as a quinone reductase . Chem. Res. Toxicol. 11:1998;608-613.
21. Cadenas E. Antioxidant and pro-oxidant functions of DT-diaphorase in quinone metabolism. Biochem. Pharmacol. 49:1995;127-140.
22. Nakamura M., Hayashi T. One- and two-electron reduction of quinones by rat liver subcellular fractions. J. Biochem. 115:1994;1141-1147.
23. Merker M.P., Bongard R.D., Kettenhofen N.J., Okamoto Y., Dawson C.A. Intracellular redox status affects transplasma membrane electron transport in pulmonary arterial endothelial cells. Am. J. Physiol. Lung Cell Mol. Physiol. 282:2002;L36-L43.
24. Villalba J.M., Navarro F., Cordoba F., Serrano A., Arroyo A., Crane F.L., Navas P. Coenzyme Q reductase from liver plasma membrane purification and role in transplasma membrane electron transport . Proc. Natl. Acad. Sci. USA. 92:1997;4887-4891.
25. Berridge M.V., Tan A.S. High-capacity redox control at the plasma membrane of mammalian cells transmembrane, cell surface, and serum NADH oxidases . Antioxid. Redox Signal. 2:2000;231-242.
26. Baker M.A., Lawen A. Plasma membrane NADH oxidoreductase system a critical review of the structural and functional data . Antioxid. Redox Signal. 2:2000;197-212.
27. del Castillo-Olivares A., Nunez de Castro I., Medina M.A. Dual role of plasma membrane electron transport systems in defense. Crit. Rev. Biochem. Mol. Biol. 35:2000;197-2000.
28. Crane F.L., Sun I.L., Clark M.G., Grebing C., Low H. Transplasma membrane redox systems in growth and development. Biochim. Biophys. Acta. 811:1985;233-264.
29. Kaul N., Choi J., Forman J.H. Transmembrane redox signaling activates NF-κB in macrophages. Free Radic. Biol. Med. 24:1998;202-207.
30. Giulivi C., Cadenas E. Extracellular activation of fluorinated aziridinylbenzoquinone in HT29 cells. EPR studies. Chem. Biol. Interact. 113:1998;191-204.
31. 2 production by NIH/3T3 cells. Biochem. Mol. Biol. Int. 44:1998;555-563.
32. Stocker R., Suarna C. Extracellular reduction of ubiquinone-1 and -10 by human Hep G2 and blood cells. Biochim. Biophys. Acta. 1158:1993;15-22.
33. Merker M.P., Bongard R.D., Linehan J.H., Okamoto Y., Vrprachticky D., Brantmeier B.M., Roerig D.L., Dawson C.A. Pulmonary endothelial thiazine uptake separation of cell surface reduction from intracellular reoxidation . Am. J. Physiol. Lung Cell Mol. Physiol. 272:1997;L673-L680.
34. Schopfer F., Riobo N., Carreras M.C., Alvarez B., Radi R., Boveris A., Cadenas E., Poderoso J.J. Oxidation of ubiquinol by peroxynitrite implications for protection of mitochondria against nitrosative damage . Biochem. J. 349:2000;35-42.
35. Duling D.R. Simulation of multiple isotropic spin trap EPR spectra. J. Magn. Reson. 104:1994;105-110.
36. Kooser R.G., Kirchman E., Matkov T. Measurements of spin concentrations in electron paramagnetic resonance spectroscopy. Concepts Magn. Reson. 4:1992;144-152.
37. Cadenas E., Boveris A., Ragan C.I., Stoppani A.O.M. Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef heart mitochondria. Arch. Biochem. Biophys. 180:1977;248-257.
38. Storrie B., Madden E.A. Isolation of subcellular organelles. Deutscher M.P. Guide to protein purification. 1990;203-225 Academic Press, San Diego.
39. Gafencu A., Stanescu M., Toderici A.M., Heltianiu C., Simionescu M. Protein and fatty acid composition of caveolae from apical plasmalemma of aortic endothelial cells. Cell Tissue Res. 293:1998;101-110.
40. Eyer P. Effects of superoxide dismutase on the autoxidation of 1,4-hydroquinone. Chem. Biol. Interact. 80:1991;159-176.
41. Fridovich I. Superoxide dismutases. An adaptation to a paramagnetic gas. J. Biol. Chem. 264:1989;7761-7764.
42. Schmidt-Nielsen K. Scaling why is animal size so important? 1984;Cambridge University Press, New York.
43. Giulvi C., Cadenas E. Extracellular activation of fluorinated aziridinylbenzoquinone in HT29 cells EPR studies. Chem. Biol. Interact. 113:1998;191-204.
44. Fato R., Castelluccio C., Palmer G., Lenaz G. A simple method for the determination of the kinetic constants of membrane enzymes utilizing hydrophobic substrates ubiquinol cytochrome c reductase . Biochim. Biophys. Acta. 932:1988;216-222.
45. + diffusion potentials on duroquinol-cytochrome c reductase activity catalyzed by complex III incorporated into liposomes. FEBS Lett. 93:1978;69-72.
46. Chan T.S., Teng S., Wilson J.X., Galati G., Khan S., O'Brien P.J. Coenzyme Q cytoprotective mechanisms for mitochondrial complex I cytopathies involves NAD(P)H quinone oxidoreductase 1 (NQO1) . Free Radic. Res. 36:2002;421-427.
47. Kishi T., Morre D.M., Morre D.J. The plasma membrane NADH oxidase of HeLa cells has hydroquinone oxidase activity. Biochim. Biophys. Acta. 1412:1999;66-77.
48. 11C] coenzyme Q-related compounds for in vivo estimation of mitochondrial electron transduction and redox state in brain. Nucl. Med. Biol. 26:1999;183-187.
49. 0 reductase generates semiquinone radicals and recycles vitamine E homolog in a superoxide-dependent reaction. FEBS Lett. 428:1998;43-46.
50. Ohkawa S., Terao T., Murakami M., Matsumoto T., Goto G. Reduction of 2,3,5-trimethyl-6-(3-pyridylmethyl)-1,4-benzoquinone by PB-3c cells and biological activity of its hydroquinone. Chem. Pharm. Bull. 39:1991;914-921.
51. Navarro F., Villalba J.M., Crane F.L., Mackellar W.C., Navas P. A phospholipid-dependent NADH-coenzyme Q reductase from liver plasma membrane. Biochem. Biophys. Res. Commun. 212:1995;138-143.
52. 5 reductase on the antioxidant function of coenzyme Q in the plasma membrane. Mol. Aspects Med. 18:1997;S7-S13.
53. Villalba J.M., Navas P. Plasma membrane redox system in the control of stress-induced apoptosis. Antioxid. Redox Signal. 2:2000;213-230.
54. Navarro F., Arroyo A., Martin S.F., Bello R.I., Decabo R., Burgess J.R., Navas P., Villalba J.M. Protective role of ubiquinone in vitamin E and selenium-deficient plasma. Biofactors. 9:1999;163-170.
55. Zurbriggen R., Dreyer J.L. An NADH-diaphorase is located at the cell plasma membrane in a mouse neuroblastoma cell line NB41A3. Biochim. Biophys. Acta. 1183:1994;513-520.
56. Cole S.R., Ashman L.K., Ey P.L. Biotinylation an alternative to radioiodination for the identification of cell surface antigens in immunoprecipitates . Molecular Immunol. 24:1987;699-705.
57. Yan R., Han P., Miao H., Greengard P., Xu H. The transmembrane domain of the Alzheimer's β-secretase (BACE1) determines its late Golgi localization and access to β-amyloid precursor (APP) substrate. J. Biol. Chem. 276:2001;36788-36796.
58. Ray W.J., Yao M., Mumm J., Schroeter E.H., Saftig P., Wolfe M., Selkoe D.J., Kopan R., Goate A.M. Cell surface presenilin-1 participates in the γ-secretase-like proteolysis of Notch. J. Biol. Chem. 274:1999;36801-36807.
59. Clark M.G., Partick E.J., Patten G.S., Crane F.L., Low H., Grebing C. Evidence for the extracellular reduction of ferricyanide by rat liver. Biochem. Int. 200:1981;565-572.
60. Griendling K.K., Sorescu D., Ushio-Fukai M. NAD(P)H oxidase role in cardiovascular biology and disease . Circ. Res. 86:2000;494-501.
61. Cross A.R. The inhibitory effects of some iodonium compounds on the superoxide-generating system of neutrophils and their failure to inhibit diaphorase activity. Biochem. Pharmacol. 36:1987;489-493.
62. O'Donnel V.B., Smith G.C.M., Jones O.T.G. Involvement of phenyl radicals in iodonium compound inhibition of flavoenzymes. Mol. Pharmacol. 46:1994;778-785.
63. Preusch P.C., Siegel D., Gibson N.W., Ross D. A note on the inhibition of DT-diaphorase by dicoumarol. Free Radic. Biol. Med. 11:1991;77-80.
64. Pullar J.M., Hampton M.B. Diphenyleneiodonium triggers the effux of glutathione from cultured cells. J. Biol. Chem. 277:2002;19402-19407.
65. O'Donnell V.B., Tew D.G., Jones O.T.G., England P.J. Studies on the inhibitory mechanism of iodonium compounds with special reference to neutrophil NADPH oxidase. Biochem. J. 290:1993;41-49.
66. Macarthur H., Westfall T.C., Riley D.P., Misko T.P., Salvemini D. Inactivation of catecholamines by superoxide gives new insights on the pathogenesis of septic shock. Proc. Natl. Acad. Sci. USA. 97:2000;9753-9758.
67. Bolton J.L., Shen L. p-Quinone methides are the major decomposition products of catechol estrogen o-quinones. Carcinogenesis. 17:1996;925-929.
68. Bindoli A., Rigobello M.P., Galzigna L. Reduction of adrenochrome by rat liver and brain DT-diaphorase. Free Radic. Res. Commun. 8:1990;295-298.
69. Tatar M., Rand D.M. Dietary advice on Q. Science. 295:2002;54-55.
70. Moridani M.Y., Scobie H., Jamshidzadeh A., Salehi P., O'Brien P.J. Caffeic acid, chlorogenic acid, and dihydrocaffeic acid metabolism glutathione conjugate formation . Drug Metab. Dispos. 29:2001;1432-1439.
71. Poderoso J.J., Carreras M.C., Schopfer F., Lisdero C.L., Riobo N.A., Giulivi C., Boveris A.D., Boveris A., Cadenas E. The reaction of nitric oxide with ubiquinol kinetic properties and biological significance . Free Radic. Biol. Med. 26:1999;925-935.
72. Guo Q., Corbett J.T., Yue G., Fann Y.C., Qian Y., Tomer K.B., Mason R.P. Electron spin resonance investigation of semiquinone radicals formed from the reaction of ubiquinone 0 with human oxyhemoglobin. J. Biol. Chem. 277:2001;6104-6110.