Antioxidant ascorbate is stabilized by NADH-Coenzyme Q10 reductase in the plasma membrane

Journal of Bioenergetics and Biomembranes

Volumn 29, Issue 3, 1997, Pages 251-257

  Gómez Díaz, Consuelo ^a   Rodríguez Aguilera, Juan Carlos ^a   Barroso, María P ^a   Villalba, José M ^a   Navarro, Francisco ^a   Crane, Frederick L ^a,b   Navas, Plácido ^a  

^a UNIVERSITY OF CÓRDOBA   (Spain)

^b PURDUE UNIVERSITY   (United States)

Author keywords

Ascorbate stabilization; Coenzyme Q; Eytochrome b5 reductase; Plasma membrane

Indexed keywords

ALKALINE PHOSPHATASE; ASCORBATE OXIDASE; ASCORBIC ACID; CAPSAICIN; CYTOCHROME B5 REDUCTASE; CYTOCHROME C OXIDASE; DICOUMAROL; GALACTOSYLTRANSFERASE; LIPOSOME; OXIDOREDUCTASE; PROTEIN P 34; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE; SUCCINATE DEHYDROGENASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANTIOXIDANT ACTIVITY; ARTICLE; CELL DIFFERENTIATION; CELL MEMBRANE; CELL STRAIN K 562; CONTROLLED STUDY; ENZYME ACTIVITY; EXTRACELLULAR SPACE; HUMAN; HUMAN CELL; LIVER CELL MEMBRANE; MEMBRANE VESICLE; MICROSOME; NONHUMAN; OXIDATION; SWINE;

ANIMALS; ANTIOXIDANTS; ASCORBIC ACID; CELL LINE; CELL MEMBRANE; ELECTRON TRANSPORT COMPLEX I; ENZYME STABILITY; HUMANS; NADH, NADPH OXIDOREDUCTASES; SWINE; TUMOR CELLS, CULTURED; UBIQUINONE;

ANIMALIA; SUS SCROFA;

EID: 0030777178     PISSN: 0145479X     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1022410127104     Document Type: Article

References (41)

1. Alcaín, F. J., Burón, M. I., Villalba, J. M., and Navas, P. (1991). Biochim. Biophys. Acta 1073, 380-385.
2. Beyer, R. E. (1994). J. Bioenerg. Biomembr 26, 349-358.
3. Briviba, K., and Sies, H. (1994). In Natural Antioxidants in Human Health and Disease (Frei, B., ed), Academic Press, London, pp. 107-128.
4. Buettner, G. R. (1993). Arch. Biochem. Biophys. 300, 535-543.
5. Burón, M. I., Rodríguez-Aguilera, J. C., Alcain, F. J., and Navas, P. (1993). Biochem. Biophys. Res. Commun. 192, 439-445.
6. Coassin, M., Tomasi, A., Vannini, V., and Ursini, F. (1991). Arch. Biochem. Biophys. 290, 458-462.
7. Crane, F. L., Low, H., and Clark, M. G. (1985). In The Enzymes of Biological Membranes, Vol. 4 (Martonosi, A. N., ed). Plenum Press, New York, pp. 465-510.
8. D'Arrigo, A., Manera, E., Longhi, R., and Borgese, N. (1993). J. Biol. Chem. 268, 2802-2808.
9. Fibach, E., Treves, A., and Rachmilewitz, E. A. (1983). Cancer Res. 43, 4136-4141.
10. Frei, B.(1994). Am J. Med. 97, 5S-13S.
11. Geiss, D., and Schulze, H. U. (1975). FEBS Lett. 60, 374-379.
12. Hossain, M. H., and Asada, K. (1985). J. Biol. Chem. 260, 12920-12926.
13. Ito, A., Hayashi, S.-I., and Yoshida, T. (1981). Biochem Biophys. Res. Commun. 101, 591-598.
14. Kant, J. A., and Steck, T. L. (1972). Nature 240, 26-28.
15. Kashiwamata, S., Goto, S., Semba, R. K., and Suzuki, F. N. (1979). J. Biol. Chem. 254, 4577-4584.
16. Kobayashi, K., Harada, Y., and Hayashi, K. (1991). Biochemistry 30, 8310-8315.
17. Lederer, F., Chrir, R., Guiard, B., Cortial, B., and Ito, A. (1983). Eur. J. Biochem. 132, 95-102.
18. Lenaz, G., Bovina, C., Castellucio, C., Cavazzoni, M., Estornell, E., Huertas, J. R., Pich, M. M., Pallotti, F., Castelli, G. P., and Rauchova, H. (1995). Protoplasma 184, 50-62.
19. Mahler, H. R. (1955). Methods Enzymol. 2, 688-693.
20. Medina, M. A. del Castillo-Olivares, A., and Schweigerer, L. (1992). FEBS Lett. 311, 99-101.
21. Meister, A. (1994). J. Biol. Chem. 269, 9397-9400.
22. Minetti, M., Forte, T., Sotiani, M., Quaresima, V., Menditto, A., and Ferrari, M. (1992). Biochem. J. 282, 459-465.
23. Navarro, F., Villalba, J. M., Crane, F. L., MacKellar, W. C., and Navas, P. (1995). Biochem. Biophys. Res. Commun. 212, 138-143.
24. Navas, P., Nowack, D. D., and Morré, D. J. (1989). Cancer Res. 49, 2147-2156.
25. Navas, P., Alcaín, F. J., Burón, M. I., Rodríguez-Aguilera, J. C., Villalba, J. M., Morré, D. M., and Morré, D. J. (1992). FEBS Lett. 299, 223-226.
26. Norling, B., Glazek, E., Nelson, B. D., and Ernster, L. (1974). Eur. J. Biochem. 47, 475-482.
27. Palmiter, R. D. (1969). Biochim. Biophys. Acta 178, 35-46.
28. Pennington, R. J. (1961). Biochem. J. 80, 649-654.
29. Pethig, R., Gascoyne, P. R. C., McLaughlin, J. A., and Szent-Györgyi, A. (1985). Proc. Natl. Acad. Sci. USA 82, 1439-1442.
30. Remacle, J. (1980). Biochim. Biophys. Acta 597, 564-576.
31. Rodríguez-Aguilera, J. C., and Navas, P. (1994). J. Bioenerg. Biomembr. 26, 379-384.
32. Rodríguez-Aguilera, J. C., Navarro, F., Arroyo, A., Villalba, J. M., and Navas, P. (1993). J. Biol. Chem. 268, 26346-26349.
33. Rose, R. C., and Bode, A. M. (1993). FASEB J. 7, 1135-1142.
34. Schulze, H. U., and Staudinger, H.(1971). Hoppe-Seyler's Z. Physiol. Chem. 352, 1659-1674.
35. Shirabe, K., Landi, M. T., Takeshita, M., Uziel, G., Fedrizzi, E., and Borgese, N. (1995). Am. J. Hum. Genet. 57, 302-310.
36. Storrie, B., and Madden, E. A. (1990). Methods Enzymol. 182, 203-235.
37. Stoscheck, C. M. (1990). Methods Enzymol. 180, 50-68.
38. Sun, I. L., Sun, E. E., Crane, F. L., Morré, D. J., Lindgren, A., and Low, H. (1992). Proc. Natl. Acad. Sci. USA 89, 11126-11130.
39. Villalba, J. M., Canalejo, A., Rodriguez-Aguilera, J. C., Burón, M. I., Morré, D. J., and Navas, P. (1993). J. Bioenerg. Biomembr. 25, 411-417.
40. Villalba, J. M., Navarro, F., Córdoba, F., Serrano, A., Arroyo, A., Crane, F. L., and Navas, P. (1995). Proc. Natl. Acad. Sci. USA 92, 4887-4891.
41. Winkler, B. S. (1987). Biochim. Biophys. Acta 925, 258-264.