Differential distribution of 4-hydroxynonenal adducts to sulfur and nitrogen residues in blood proteins as revealed using Raney nickel and gas chromatography-mass spectrometry

Free Radical Biology and Medicine

Volumn 47, Issue 10, 2009, Pages 1375-1385

  Lesgards, Jean François ^a,b   Frayne, Isabelle Robillard ^a,b   Comte, Blandine ^a   Busseuil, David ^a,b   Rhéaume, Éric ^a,b   Tardif, Jean Claude ^a,b   Rosiers, Christine Des ^a,b  

^a UNIVERSITÉ DE MONTRÉAL   (Canada)

^b MONTREAL HEART INSTITUTE   (Canada)

Author keywords

Aldehydes; Free radicals; Lipoperoxidation; Oxidative stress; Plasma; Protein modification, Hypercholesterolemia

Indexed keywords

4 HYDROXYNONENAL; ALBUMIN; CYSTEINE; HISTIDINE; LYSINE; NICKEL; NITROGEN; PHENYLHYDRAZINE DERIVATIVE; POLYAMINOACID; SULFUR;

ARTICLE; CONTROLLED STUDY; GAS CHROMATOGRAPHY; HYPERCHOLESTEROLEMIA; IN VITRO STUDY; LIPID PEROXIDATION; MALE; MASS SPECTROMETRY; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN BLOOD LEVEL; PROTEIN CLEAVAGE; PROTEIN MODIFICATION; QUANTITATIVE ANALYSIS; RABBIT;

ALDEHYDES; ANIMALS; BLOOD PROTEINS; GAS CHROMATOGRAPHY-MASS SPECTROMETRY; HISTIDINE; LYSINE; MALE; NICKEL; RABBITS;

ORYCTOLAGUS CUNICULUS; RATTUS;

EID: 70350015366     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2009.08.002     Document Type: Article

References (45)

1. Poli G., Schaur R.J., Siems W.G., and Leonarduzzi G. 4-Hydroxynonenal: a membrane lipid oxidation product of medicinal interest. Med. Res. Rev. 28 (2008) 569-631
2. Benedetti A., Comporti M., and Esterbauer H. Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids. Biochim. Biophys. Acta 620 (1980) 281-296
3. Mlakar A., and Spiteller G. Previously unknown aldehydic lipid peroxidation compounds of arachidonic acid. Chem. Phys. Lipids 79 (1996) 47-53
4. Doorn J.A., and Petersen D.R. Covalent modification of amino acid nucleophiles by the lipid peroxidation products 4-hydroxy-2-nonenal and 4-oxo-2-nonenal. Chem. Res. Toxicol. 15 (2002) 1445-1450
5. Carini M., Aldini G., and Facino R.M. Mass spectrometry for detection of 4-hydroxy-trans-2-nonenal (HNE) adducts with peptides and proteins. Mass Spectrom. Rev. 23 (2004) 281-305
6. Uchida K. Role of reactive aldehyde in cardiovascular diseases. Free Radic. Biol. Med. 28 (2000) 1685-1696
7. +-isocitrate dehydrogenase is inactivated through 4-hydroxynonenal adduct formation: an event that precedes hypertrophy development. J. Biol. Chem. 278 (2003) 45154-45159
8. Grimsrud P.A., Picklo Sr. M.J., Griffin T.J., and Bernlohr D.A. Carbonylation of adipose proteins in obesity and insulin resistance: identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal. Mol. Cell. Proteomics 6 (2007) 624-637
9. Uchida K. 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress. Prog. Lipid Res. 42 (2003) 318-343
10. Uchida K., Itakura K., Kawakishi S., Hiai H., Toyokuni S., and Stadtman E.R. Characterization of epitopes recognized by 4-hydroxy-2-nonenal specific antibodies. Arch. Biochem. Biophys. 324 (1995) 241-248
11. Yoritaka A., Hattori N., Uchida K., Tanaka M., Stadtman E.R., and Mizuno Y. Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease. Proc. Natl. Acad. Sci. USA 93 (1996) 2696-2701
12. Traverso N., Menini S., Cosso L., Odetti P., Albano E., Pronzato M.A., and Marinari U.M. Immunological evidence for increased oxidative stress in diabetic rats. Diabetologia 41 (1998) 265-270
13. Moreau R., Nguyen B.T., Doneanu C.E., and Hagen T.M. Reversal by aminoguanidine of the age-related increase in glycoxidation and lipoxidation in the cardiovascular system of Fischer 344 rats. Biochem. Pharmacol. 69 (2005) 29-40
14. Toyokuni S., Yamada S., Kashima M., Ihara Y., Yamada Y., Tanaka T., Hiai H., Seino Y., and Uchida K. Serum 4-hydroxy-2-nonenal-modified albumin is elevated in patients with type 2 diabetes mellitus. Antioxid. Redox Signal. 2 (2000) 681-685
15. Kimura H., Liu S., Yamada S., Uchida K., Matsumoto K., Mukaida M., and Yoshida K. Rapid increase in serum lipid peroxide 4-hydroxynonenal (HNE) through monocyte NADPH oxidase in early endo-toxemia. Free Radic. Res. 39 (2005) 845-851
16. Alderton A.L., Faustman C., Liebler D.C., and Hill D.W. Induction of redox instability of bovine myoglobin by adduction with 4-hydroxy-2-nonenal. Biochemistry 42 (2003) 4398-4405
17. Orioli M., Aldini G., Beretta G., Facino R.M., and Carini M. LC-ESI-MS/MS determination of 4-hydroxy-trans-2-nonenal Michael adducts with cysteine and histidine-containing peptides as early markers of oxidative stress in excitable tissues. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 827 (2005) 109-118
18. Han B., Stevens J.F., and Maier C.S. Design, synthesis, and application of a hydrazide-functionalized isotope-coded affinity tag for the quantification of oxylipid-protein conjugates. Anal. Chem. 79 (2007) 3342-3354
19. Grimsrud P.A., Xie H., Griffin T.J., and Bernlohr D.A. Oxidative stress and covalent modification of protein with bioactive aldehydes. J. Biol. Chem 283 (2008) 21837-21841
20. Selley M.L. Determination of the lipid peroxidation product (E)-4-hydroxy-2-nonenal in clinical samples by gas chromatography-negative-ion chemical ionisation mass spectrometry of the O-pentafluorobenzyl oxime. J. Chromatogr. B Biomed. Sci. Appl. 691 (1997) 263-268
21. Spies-Martin D., Sommerburg O., Langhans C.D., and Leichsenring M. Measurement of 4-hydroxynonenal in small volume blood plasma samples: modification of a gas chromatographic-mass spectrometric method for clinical settings. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 774 (2002) 231-239
22. Requena J.R., Fu M.X., Ahmed M.U., Jenkins A.J., Lyons T.J., Baynes J.W., and Thorpe S.R. Quantification of malondialdehyde and 4-hydroxynonenal adducts to lysine residues in native and oxidized human low-density lipoprotein. Biochem. J. 322 Pt. 1 (1997) 317-325
23. Asselin C., Bouchard B., Tardif J.C., and Des Rosiers C. Circulating 4-hydroxynonenal-protein thioether adducts assessed by gas chromatography-mass spectrometry are increased with disease progression and aging in spontaneously hypertensive rats. Free Radic. Biol. Med. 41 (2006) 97-105
24. Veronneau M., Comte B., and Des Rosiers C. Quantitative gas chromatographic-mass spectrometric assay of 4-hydroxynonenal bound to thiol proteins in ischemic/reperfused rat hearts. Free Radic. Biol. Med. 33 (2002) 1380-1388
25. Rilling H.C., Bruenger E., Epstein W.W., and Kandutsch A.A. Prenylated proteins: demonstration of a thioether linkage to cysteine of proteins. Biochem. Biophys. Res. Commun. 163 (1989) 143-148
26. Uchida K., and Stadtman E.R. Selective cleavage of thioether linkage in proteins modified with 4-hydroxynonenal. Proc. Natl. Acad. Sci. USA 89 (1992) 5611-5615
27. Keefer L.K., and Lunn G. Nickel-aluminum alloy as a reducing agent. Chem. Rev. 89 (1989) 459-502
28. Uchida K., Kanematsu M., Sakai K., Matsuda T., Hattori N., Mizuno Y., Suzuki D., Miyata T., Noguchi N., Niki E., and Osawa T. Protein-bound acrolein: potential markers for oxidative stress. Proc. Natl. Acad. Sci. USA 95 (1998) 4882-4887
29. Busseuil D., Shi Y., Mecteau M., Brand G., Kernaleguen A.E., Thorin E., Latour J.G., Rheaume E., and Tardif J.C. Regression of aortic valve stenosis by ApoA-I mimetic peptide infusions in rabbits. Br. J. Pharmacol. 154 (2008) 765-773
30. Des Rosiers C., Rivest M.J., Boily M.J., Jette M., Carrobe-Cohen A., and Kumar A. Gas chromatographic-mass spectrometric assay of tissue malondialdehyde, 4-hydroxynonenal, and other aldehydes after their reduction to stable alcohols. Anal. Biochem. 208 (1993) 161-170
31. Aldini G., Gamberoni L., Orioli M., Beretta G., Regazzoni L., Maffei F.R., and Carini M. Mass spectrometric characterization of covalent modification of human serum albumin by 4-hydroxy-trans-2-nonenal. J. Mass Spectrom. 41 (2006) 1149-1161
32. Szapacs M.E., Riggins J.N., Zimmerman L.J., and Liebler D.C. Covalent adduction of human serum albumin by 4-hydroxy-2-nonenal: kinetic analysis of competing alkylation reactions. Biochemistry 45 (2006) 10521-10528
33. Oppermann U. Carbonyl reductases: the complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology. Annu. Rev. Pharmacol. Toxicol. 47 (2007) 293-322
34. Ong W.Y., Jenner A.M., Pan N., Ong C.N., and Halliwell B. Elevated oxidative stress, iron accumulation around microvessels and increased 4-hydroxynonenal immunostaining in zone 1 of the liver acinus in hypercholesterolemic rabbits. Free Radic. Res. 43 (2009) 241-249
35. Petersen D.R., and Doorn J.A. Reactions of 4-hydroxynonenal with proteins and cellular targets. Free Radic. Biol. Med. 37 (2004) 937-945
36. Nadkarni D.V., and Sayre L.M. Structural definition of early lysine and histidine adduction chemistry of 4-hydroxynonenal. Chem. Res. Toxicol. 8 (1995) 284-291
37. Sayre L.M., Lin D., Yuan Q., Zhu X., and Tang X. Protein adducts generated from products of lipid oxidation: focus on HNE and ONE. Drug Metab. Rev. 38 (2006) 651-675
38. Aldini G., Vistoli G., Regazzoni L., Gamberoni L., Facino R.M., Yamaguchi S., Uchida K., and Carini M. Albumin is the main nucleophilic target of human plasma: a protective role against pro-atherogenic electrophilic reactive carbonyl species?. Chem. Res. Toxicol. 21 (2008) 824-835
39. Angyal S.J., Stevens J.D., and Odier L. Selective deuteration over Raney nickel in deuterium oxide:1,6-anhydrohexoses. Carbohydr. Res. 169 (1987) 151-157
40. Djedaini F., Desalos J., and Perly B. Regio- and stereo-selective deuterium labelling of β-cyclodextrin. J. Labelled Compd. Radiopharm. 28 (1990) 785-791
41. Roe M.R., Xie H., Bandhakavi S., and Griffin T.J. Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry. Anal. Chem. 79 (2007) 3747-3756
42. Ohara H., Miyabe Y., Deyashiki Y., Matsuura K., and Hara A. Reduction of drug ketones by dihydrodiol dehydrogenases, carbonyl reductase and aldehyde reductase of human liver. Biochem. Pharmacol. 50 (1995) 221-227
43. O'Connor T., Ireland L.S., Harrison D.J., and Hayes J.D. Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members. Biochem. J. 343 Pt. 2 (1999) 487-504
44. Luckey S.W., and Petersen D.R. Metabolism of 4-hydroxynonenal by rat Kupffer cells. Arch. Biochem. Biophys. 389 (2001) 77-83
45. Srivastava S., Dixit B.L., Cai J., Sharma S., Hurst H.E., Bhatnagar A., and Srivastava S.K. Metabolism of lipid peroxidation product, 4-hydroxynonenal (HNE) in rat erythrocytes: role of aldose reductase. Free Radic. Biol. Med. 29 (2000) 642-651