Plasma membrane oxidoreductases: Effects on erythrocyte metabolism and redox homeostasis

Antioxidants and Redox Signaling

Volumn 8, Issue 7-8, 2006, Pages 1241-1247

  Kennett, Eleanor C ^a   Kuchel, Philip W ^a  

^a UNIVERSITY OF SYDNEY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; ASCORBATE FREE RADICAL REDUCTASE; ASCORBIC ACID; CYTOCHROME B5 REDUCTASE; GLUCOSE TRANSPORTER 1; GLUTATHIONE; GLUTATHIONE DISULFIDE; OXIDIZING AGENT; OXIDOREDUCTASE; PLASMA MEMBRANE OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG; WATER SOLUBLE TETRAZOLIUM 1 REDUCTASE;

BIOSENSOR; CELL FUNCTION; CELL GROWTH; CELL MEMBRANE; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME LOCALIZATION; ERYTHROCYTE METABOLISM; GLYCOLYSIS; HOMEOSTASIS; HUMAN; OXIDATION REDUCTION REACTION; OXIDATION REDUCTION STATE; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN FUNCTION; REACTION ANALYSIS; REVIEW;

ANIMALS; ERYTHROCYTE MEMBRANE; ERYTHROCYTES; HOMEOSTASIS; HUMANS; MODELS, BIOLOGICAL; OXIDATION-REDUCTION; OXIDOREDUCTASES;

EID: 33746841803     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2006.8.1241     Document Type: Review

References (49)

1. Baker MA and Lawen A. The function of the plasma membrane NADH-oxidoreductase system: a critical review of the structural and functional data. Antioxid Redox Signal 2: 197-212, 2000.
2. Berridge MV and Tan AS. Trans-plasma membrane electron transport: a cellular assay for NADH- and NADPH-oxidase based on extracellular, superoxide-mediated reduction of the sulfonated tetrazolium salt WST-1. Protoplasma 205: 74-82, 1998.
3. Berridge MV and Tan AS. Cell surface NAD(P)H-oxidase: relationship to transplasma membrane NADH-oxidoreductase and a potential source of circulating NADH-oxidase. Antioxid Redox Signal 2: 277-288, 2000.
4. Berridge MV and Tan AS. High capacity redox control at the plasma membrane of mammalian cells: trans membrane, cell-surface and serum NADH-oxidases. Antioxid Redox Signal 2: 231-242, 2000.
5. Berridge MV, Tan AS, McCoy KD, and Wang R. The biochemical and cellular basis of cell proliferation assays that use tetrazolium salts. Biochemica 4: 15-20, 1996.
6. Campanella ME, Chu H, and Low PS. Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane. Proc Natl Acad Sci USA 102: 2402-2407, 2005.
7. Ciriolo AR, Paci M, Sette M, de Martino A, Bozzi A, and Rotilio G. Transduction of reducing power across the plasma membrane by reduced glutathione. Eur J Biochem 215: 711-718, 1993.
8. Ciriolo MR, Sette M, Paci M, and Rotilio G. A study of the intracellular effects of glutathione by H-1-spin echo NMR of intact human erymrocytes. Biochem Int 20: 397-403, 1990.
9. Clemens MR and Waller HD. Lipid peroxidation in erythrocytes. Chem Phys Lipids 45: 251-268, 1987.
10. Cotgreave IA and Gerdes RG. Recent trends in glutathione biochemistry-glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation? Biochem Biophys Res Commun 242: 1-9, 1998.
11. Dormandy TL and Zarday Z. The mechanism of insulin action: the immediate electrochemical effects of insulin on red-cell systems. J Physiol (Lond) 180: 684-707, 1965.
12. Guarnieri C, Fraticelli A, Ventura C, Vaona I, and Budini R. External GSSG enhances intracellular glutathione in isolated cardiac myocytes. Biochem Biophys Res Commun 147: 658-665, 1987.
13. 13C NMR studies of vitamin C transport and its redox cycling in human erythrocytes. Biochemistry 37: 7578-7588, 1998.
14. 13C-NMR studies of transmembrane electron transfer to extracellular ferricyanide in human erythrocytes. Eur J Biochem 246: 638-645, 1997.
15. Kennett EC. Transmembrane electron transport systems in erythrocyte plasma membranes. PhD thesis, School of Molecular and Microbial Biosciences, University of Sydney, 2004, pp 218.
16. Kennett EC, Bubb WA, Bansal P, Alewood P, and Kuchel PW. NMR studies of exchange between intra- and extracellular glutathione in human erythrocytes. Redox Rep 10: 83-90, 2005.
17. Kennett EC and Kuchel PW. Redox reactions and electron transfer across the red cell membrane. IUBMB Life 55: 375-385, 2003.
18. Kennett EC, Ogawa E, Agar NS, Godwin IR, Bubb WA, and Kuchel PW. Investigation of methaemoglobin reduction by extracellular NADH in mammalian erythrocytes. Int J Biochem Cell Biol 37: 1438-1445, 2005.
19. Maneva A, Taleva B, and Maneva L. Lactoferrin-protector against oxidative stress and regulator of glycolysis in human erythrocytes. Z Naturforsch [C] 58: 256-262, 2003.
20. + transport damage induced by oxygen free radicals in human red cell membranes. J Biol Chem 258: 3107-3113, 1983.
21. Marques F, Crespo ME, and Bicho M. Control of NADH ferricyanide reductase activity in the human erythrocyte by somatotrophin and insulin. Redox Rep 1: 113-117, 1995.
22. May JM. Is ascorbic acid an antioxidant for the plasma membrane? FASEB J 13: 995-1006, 1999.
23. May JM and Qu ZC. Ascorbate-dependent electron transfer across the human erythrocyte membrane. Biochim Biophys Acta 1421: 19-31, 1999.
24. May JM, Qu ZC, and Cobb CE. Extracellular reduction of the ascorbate free radical by human erythrocytes. Biochem Biophys Res Commun 267: 118-123, 2000.
25. May JM, Qu ZC, and Cobb CE. Recycling of the ascorbate free radical by human erythrocyte membranes. Free Radic Biol Med 31: 117-124, 2001.
26. May JM, Qu ZC, and Cobb CE. Human erythrocyte recycling of ascorbic acid: relative contributions from the ascorbate free radical and dehydroascorbic acid. J Biol Chem 279: 14975-14982, 2004.
27. May JM, Qu ZC, and Morrow JD. Mechanisms of ascorbic acid recycling in human erythrocytes. Biochim Biophys Acta 1528: 159-166, 2001.
28. May JM, Qu ZC, Morrow JD, and Cobb CE. Ascorbate-dependent protection of human erythrocytes against oxidant stress generated by extracellular diazobenzene sulfonate. Biochem Pharmacol 60: 47-53, 2000.
29. May JM, Qu ZC, and Whitesell RR. Ascorbate is the major electron donor for a transmembrane oxidoreductase of human erythrocytes. Biochim Biophys Acta 1238: 127-136, 1995.
30. May JM, Qu ZC, Whitesell RR, and Cobb CE. Ascorbate recycling in human erythrocytes: role of GSH in reducing dehydroascorbate. Free Radic Biol Med 20: 543-551, 1996.
31. Meister A and Anderson ME. Glutathione. Annu Rev Biochem 52: 711-760, 1983.
32. Messana JM, Cieslinski DA, O'Connor RP, and Humes HD. Glutathione protects against exogenous oxidant injury to rabbit renal proximal tubules. Am J Physiol 255: F874-F884, 1988.
33. Mishra RK and Passow H. Induction of intracellular ATP synthesis by extracellular ferricyanide in human red blood cells. J Membr Biol 1: 214-224, 1969.
34. + on human erythrocyte metabolism: new estimation of the turnover through the phosphoglycerate shunt. Arch Biochem Biophys 210: 160-166, 1981.
35. Pendergrass JA, Srinivasan V, Clark EP, and Kumar KS. Glutathione redox status in the human cell line, A549, following intracellular glutathione depletion and extracellular glutathione addition. Tox Subst Mech 18: 11-20, 1999.
36. 2 production and DNA damage. Int J Cancer 87: 343-348, 2000.
37. 1H NMR and a computer model. Eur J Biochem 193: 83-90, 1990.
38. Russell J, Spickett C, Reglinski J, Smith W, McMurray J, and Abdullah I. Alteration of the erythrocyte glutathione redox balance by N-acetylcysteine, captopril and exogenous glutathione. FEBS Lett 347: 215-220, 1994.
39. Schipfer W, Neophytou B, Trobisch R, Groiss O and Goldenberg H. Reduction of extracellular potassium ferricyanide by transmembrane NADH: (acceptor) oxidoreductase of human erythrocytes. Int J Biochem 17: 819-823, 1985.
40. Tan AS and Berridge MV. Superoxide produced by activated neutrophils efficiently reduces the tetrazolium salt WST-1 to produce a soluble formazan: a simple colorimetric assay for measuring respiratory burst activation and for screening anti-inflammatory agents. J Immunol Methods 238: 59-68, 2000.
41. Thorburn DR and Kuchel PW. Regulation of the human-erythrocyte hexose-monophosphate shunt under conditions of oxidative stress: a study using NMR spectroscopy, a kinetic isotope effect, a reconstituted system and computer simulation. Eur J Biochem 150: 371-386, 1985.
42. Tietze F. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal Biochem 27: 502-522, 1969.
43. Tilton WM, Seaman C, Carriero D, and Piomelli S. Regulation of glycolysis in the erythrocyte: role of the lactate/pyruvate and NAD/NADH ratios. J Lab Clin Med 118: 146-152, 1991.
44. Van Duijn MM, Tijssen K, VanSteveninck J, Van der Broek P, and Van der Zee J. Erythrocytes reduce extracellular ascorbate free radicals using intracellular ascorbate as an electron donor. J Biol Chem 275: 27720-27725, 2000.
45. Van Duijn MM, Van der Zee J, and Van den Broek PJ. The ascorbate-driven reduction of extracellular ascorbate free radical by the erythrocyte is an electrogenic process. FEBS Lett 491: 67-70, 2001.
46. Van Duijn MM, Vanderzee J, Vansteveninck J, and Vandenbroek PJA. Ascorbate stimulates ferricyanide reduction in HL-60 cells through a mechanism distinct from the NADH-dependent plasma membrane reductase. J Biol Chem 271: 13415-13420, 1998.
47. Villalba JM, Navarro F, Cordoba F, Serrano A, Arroyo A, Crane FL, and Navas P. Coenzyme Q reductase from liver plasma membrane: purification and role in trans-plasma-membrane electron transport. Proc Natl Acad Sci U S A 92: 4887-4891, 1995.
48. Zamudio I and Canessa M. Nicotinamide-adenine dinucleotide dehydrogenase activity of human erythrocyte membranes. Biochim Biophys Acta 120: 165-169, 1966.
49. Zerez CR, Lachant NA, and Tanaka KR. Impaired erythrocyte methemoglobin reduction in sickle cell disease: dependence of methemoglobin reduction on reduced nicotinamide adenine dinucleotide content. Blood 76: 1008-1014, 1990.