The covalent modification of spectrin in red cell membranes by the lipid peroxidation product 4-hydroxy-2-nonenal

Biochemical and Biophysical Research Communications

Volumn 391, Issue 3, 2010, Pages 1543-1547

  Arashiki, Nobuto ^a   Otsuka, Yayoi ^a   Ito, Daisuke ^a   Yang, Mira ^a   Komatsu, Tomohiko ^a   Sato, Kota ^a   Inaba, Mutsumi ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

Author keywords

4 Hydroxy 2 nonenal; Lipid peroxidation; Membrane; Red cell; Spectrin

Indexed keywords

4 HYDROXYNONENAL; ADENOSINE TRIPHOSPHATASE (MAGNESIUM); FODRIN; MEMBRANE LIPID; MEMBRANE PROTEIN; SPECTRIN; SPECTRIN BETA SUBUNIT; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CROSS LINKING; ERYTHROCYTE; ERYTHROCYTE MEMBRANE; HUMAN; HUMAN CELL; IMMUNOBLOTTING; LIPID BILAYER; LIPID PEROXIDATION; MASS SPECTROMETRY; PHYSIOLOGY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN MODIFICATION;

ALDEHYDES; AMINO ACID SEQUENCE; ERYTHROCYTE MEMBRANE; HUMANS; IMMUNOBLOTTING; LIPID PEROXIDATION; MOLECULAR SEQUENCE DATA; SPECTRIN; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 73949083731     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.12.121     Document Type: Article

References (25)

1. Bennett V., and Healy J. Organizing the fluid membrane bilayer: diseases linked to spectrin and ankyrin. Trends Mol. Med. 14 (2008) 28-36
2. Cohen A.M., Liu S.-C., Derick L.H., et al. Ultrastructural studies of the interaction of spectrin with phosphatidylserine liposomes. Blood 68 (1986) 920-926
3. Manno S., Takakuwa Y., and Mohandas N. Identification of a functional role for lipid asymmetry in biological membranes: phosphatidylserine-skeletal protein interactions modulate membrane stability. Proc. Natl. Acad. Sci. USA 99 (2002) 1943-1948
4. Mohandas N., and Gallagher P.G. Red cell membrane: past, present, and future. Blood 112 (2008) 3939-3948
5. Low P.S., Willardson B.M., Mohandas N., et al. Contribution of the band 3-ankyrin interaction to erythrocyte membrane stability. Blood 77 (1991) 1581-1586
6. Inaba M., Yawata A., Koshino I., et al. Defective anion transport and marked spherocytosis with membrane instability caused by hereditary total deficiency of red cell band 3 in cattle due to a nonsense mutation. J. Clin. Invest. 97 (1996) 1804-1817
7. Perrotta S., Gallagher P.G., and Mohandas N. Hereditary spherocytosis. Lancet 372 (2008) 1411-1426
8. Snyder L.M., Fortier N.L., Trainer J., et al. Effect of hydrogen peroxide exposure on normal human erythrocyte deformability, morphology, surface characteristics, and spectrin-hemoglobin cross-linking. J. Clin. Invest. 76 (1998) 1971-1977
9. Wagner G.M., Chiu D.T.-Y., Qju J.H., et al. Spectrin oxidation correlates with membrane vesiculation in stored RBCs. Blood 69 (1987) 1777-1781
10. Esterbauer H., Schauer R.J., and Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malondialdehyde and related aldehydes. Free Radic. Biol. Med. 11 (1991) 81-128
11. Schneider C., Tallman K.A., Porter N.A., et al. Two distinct pathways of formation of 4-hydroxynonenal. Mechanisms of nonenzymatic transformation of the 9- and 13-hydroperoxides of linoleic acid to 4-hydroxyalkenals. J. Biol. Chem. 276 (2001) 20831-20838
12. Uchida K. Review. 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress. Prog. Lipid Res. 42 (2003) 318-343
13. Petersen D.R., and Doorn J.A. Reactions of 4-hydroxynonenal with proteins and cellular targets. Free Radic. Biol. Med. 37 (2004) 937-945
14. Montine T.J., Amarnath V., Martin M.E., et al. E-4-hydroxy-2-nonenal is cytotoxic and cross-links cytoskeletal proteins in P19 neuroglial cultures. Am. J. Pathol. 148 (1996) 89-93
15. Lauderback C.M., Hackett J.M., Huang F.F., et al. The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: the role of Aβ1-42. J. Neurosci. 78 (2001) 413-416
16. Murray I.V.J., Liu L., Komatsu H., et al. Membrane-mediated amyloidogenesis and the promotion of oxidative lipid damage by amyloid β proteins. J. Biol. Chem. 282 (2007) 9335-9345
17. Stewart B.J., Doorn J.A., and Petersen D.R. Residue-specific adduction of tubulin by 4-hydroxynonenal and 4-oxononenal causes cross-linking and inhibits polymerization. Chem. Res. Toxicol. 20 (2007) 1111-1119
18. Kokubo J., Nagatani N., Hiroki K., et al. Mechanism of destruction of microtubule structures by 4-hydroxy-2-nonenal. Cell Struct. Funct. 33 (2008) 51-59
19. Ando K., Beppu M., and Kitagawa K. Evidence for accumulation of lipid hydroperoxides during the aging of human red blood cells in the circulation. Biol. Pharmacol. Bull. 18 (1995) 659-663
20. Uchida K., Hasui Y., and Osawa T. Covalent attachment of 4-hydroxy-2-nonenal to erythrocyte proteins. J. Biochem. 122 (1997) 1246-1251
21. Tiffert T., Lew V.L., Ginsburg H., et al. The hydration state of human red blood cells and their susceptibility to invasion by Plasmodium falciparum. Blood 105 (2005) 4853-4860
22. Ito D., Koshino I., Arashiki N., et al. Ubiquitylation-independent ER-associated degradation of an AE1 mutant associated with dominant hereditary spherocytosis in cattle. J. Cell Sci. 119 (2006) 3602-3612
23. Fenaille F., Guy P.A., and Tabet J.C. Study of protein modified by 4-hysroxy-2-nonenal and other short chain aldehydes analyzed by electrospray ionization tandem mass spectrometry. J. Am. Soc. Mass Spectrom. 14 (2003) 215-226
24. An X., Guo X., Sum H., et al. Phosphatidylserine binding sites in erythroid spectrin: location and implications for membrane stability. Biochemistry 43 (2004) 310-315
25. Liu L., Komatsu H., Murray I.V.J., et al. Promotion of amyloid β protein misfolding and fibrillogenesis by a lipid oxidation product. J. Mol. Biol. 377 (2008) 1236-1250