The Drosophila carbonyl reductase sniffer is an efficient 4-oxonon-2-enal (4ONE) reductase

Chemico-Biological Interactions

Volumn 191, Issue 1-3, 2011, Pages 48-54

  Martin, Hans Jörg ^a   Ziemba, Marta ^a   Kisiela, Michael ^a   Botella, José A ^b   Schneuwly, Stephan ^b   Maser, Edmund ^a  

^a UNIVERSITY HOSPITAL SCHLESWIG HOLSTEIN   (Germany)

^b UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

4HNE; 4ONE; Carbonyl reductase; Lipid peroxidation; Sniffer; Toxic aldehydes

Indexed keywords

4 HYDROXY 2 ENAL REDUCTASE; 4 OXONON 2 ENAL REDUCTASE; CARBONYL REDUCTASE; OXIDOREDUCTASE; SNIFFER; UNCLASSIFIED DRUG;

CATALYSIS; CONFERENCE PAPER; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME PURIFICATION; EXPRESSION VECTOR; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; LIPID METABOLISM; LIPID PEROXIDATION; MASS FRAGMENTOGRAPHY; MOLECULAR DYNAMICS; NONHUMAN; NUCLEOTIDE SEQUENCE;

ALCOHOL OXIDOREDUCTASES; ALDEHYDES; ANIMALS; CLONING, MOLECULAR; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; LIPID METABOLISM; NEURODEGENERATIVE DISEASES; OXIDATION-REDUCTION; OXIDATIVE STRESS; RECOMBINANT PROTEINS;

BACTERIA (MICROORGANISMS); DROSOPHILA MELANOGASTER;

EID: 79957557526     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2010.12.006     Document Type: Conference Paper

References (32)

1. A.A. Fatokun, T.W. Stone, R.A. Smith, Oxidative stress in neurodegeneration and available means of protection, Front. Biosci. 13 (2008) 3288-3311.
2. B. Halliwell, Oxidative stress and neurodegeneration: where are we now? J. Neurochem. 97 (2006) 1634-1658. (Pubitemid 43873658)
3. J.A. Navarro, E. Ohmann, D. Sanchez, J.A. Botella, G. Liebisch, M.D. Molto, M.D. Ganfornina, G. Schmitz, S. Schneuwly, Altered lipid metabolism in a Drosophila model of Friedreich's ataxia, Hum. Mol. Genet. 19 (2010) 2828-2840.
4. S.H. Lee, I.A. Blair, Characterization of 4-oxo-2-nonenal as a novel product of lipid peroxidation, Chem. Res. Toxicol. 13 (2000) 698-702. (Pubitemid 30663446)
5. A.W. Girotti, Lipid hydroperoxide generation, turnover, and effector action in biological systems, J. Lipid Res. 39 (1998) 1529-1542. (Pubitemid 28377917)
6. H. Esterbauer, K.H. Cheeseman, Determination of aldehydic lipid peroxidation products: malonaldehyde and 4-hydroxynonenal, Methods Enzymol. 186 (1990) 407-421. (Pubitemid 20279982)
7. H. Esterbauer, R.J. Schaur, H. Zollner, Chemistry and biochemistry of 4- hydroxynonenal, malonaldehyde and related aldehydes, Free Radic. Biol. Med. 11 (1991) 81-128.
8. J.A Doorn, D.R. Petersen, Covalent adduction of nucleophilic amino acids by 4-hydroxynonenal and 4-oxononenal, Chem. Biol. Interact. 143-144 (2003) 93-100. (Pubitemid 36246435)
9. J.A. Doorn, D.R. Petersen, 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. (Pubitemid 35364906)
10. D.R. Petersen, J.A. Doorn, Reactions of 4-hydroxynonenal with proteins and cellular targets, Free Radic. Biol. Med. 37 (2004) 937-945. (Pubitemid 39164576)
11. D. Rindgen, M. Nakajima, S. Wehrli, K. Xu, I.A. Blair, Covalent modifications to 2′-deoxyguanosine by 4-oxo-2-nonenal, a novel product of lipid peroxidation, Chem. Res. Toxicol. 12 (1999) 1195-1204.
12. T Oe, S.H. Lee, M.V. Silva Elipe, B.H. Arison, I.A. Blair, A novel lipid hydroperoxide-derived modification to arginine, Chem. Res. Toxicol. 16 (2003) 1598-1605. (Pubitemid 38049379)
13. W.H. Zhang, J. Liu, G. Xu, Q. Yuan, L.M. Sayre, Model studies on protein side chain modification by 4-oxo-2-nonenal, Chem. Res. Toxicol. 16 (2003) 512-523. (Pubitemid 36514509)
14. T. Matsunaga, S. Shintani, A. Hara, Multiplicity of mammalian reductases for xenobiotic carbonyl compounds, Drug Metab. Pharmacokinet. 21 (2006) 1-18.
15. F. Hoffmann, E. Maser, Carbonyl reductases and pluripotent hydroxysteroid dehydrogenases of the short-chain dehydrogenase/reductase superfamily, Drug Metab. Rev. 39 (2007) 87-144.
16. T.M. Penning, J.E. Drury, Human aldo-keto reductases: function, gene regulation, and single nucleotide polymorphisms, Arch. Biochem. Biophys. 464 (2007) 241-250.
17. D Hyndman, D.R. Bauman, V.V. Heredia, T.M. Penning, The aldo-keto reductase superfamily homepage, Chem. Biol. Interact. 143-144 (2003) 621-631. (Pubitemid 36246464)
18. K.L. Kavanagh, H. Jornvall, B. Persson, U. Oppermann, Medium- and short-chain dehydrogenase/reductase gene and protein families: the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes, Cell. Mol. Life Sci. 65 (2008) 3895-3906.
19. T. Sgraja, J. Ulschmid, K. Becker, S. Schneuwly, G. Klebe, K. Reuter, A. Heine, Structural insights into the neuroprotective-acting carbonyl reductase Sniffer of Drosophila melanogaster, J. Mol. Biol. 342 (2004) 1613-1624.
20. J.A. Botella, J.K. Ulschmid, C. Gruenewald, C. Moehle, D. Kretzschmar, K. Becker, S. Schneuwly, The Drosophila carbonyl reductase sniffer prevents oxidative stress-induced neurodegeneration, Curr. Biol. 14 (2004) 782-786.
21. J.A. Doorn, E. Maser, A. Blum, D.J. Claffey, D.R. Petersen, Human carbonyl reductase catalyzes reduction of 4-oxonon-2-enal, Biochemistry 43 (2004) 13106-13114. (Pubitemid 39366059)
22. M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein - dye binding, Anal. Biochem. 72 (1976) 248-254.
23. H.J. Martin, E. Maser, Role of human aldo-keto-reductase AKR1B10 in the protection against toxic aldehydes, Chem. Biol. Interact. 178 (2009) 145-150.
24. D. Lin, H.G. Lee, Q. Liu, G. Perry, M.A. Smith, L.M. Sayre, 4-Oxo-2-nonenal is both more neurotoxic and more protein reactive than 4-hydroxy-2-nonenal, Chem. Res. Toxicol. 18 (2005) 1219-1231. (Pubitemid 41170246)
25. P. Rice, I. Longden, A. Bleasby, EMBOSS: the European Molecular Biology Open Software Suite, Trends Genet. 16 (2000) 276-277.
26. E. Maser, Neuroprotective role for carbonyl reductase? Biochem. Biophys. Res. Commun. 340 (2006) 1019-1022.
27. R.L. Bateman, D. Rauh, B. Tavshanjian, K.M. Shokat, Human carbonyl reductase 1 is an S-nitrosoglutathione reductase, J. Biol. Chem. 283 (2008) 35756-35762.
28. K. Uchida, E.R. Stadtman, Selective cleavage of thioether linkage in proteins modified with 4-hydroxynonenal, Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 5611-5615.
29. H. Bauer, S.M. Kanzok, R.H. Schirmer, Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin peroxidase-1 from Drosophila melanogaster: isolation and characterization of a second thioredoxin in D. melanogaster and evidence for distinct biological functions of Trx-1 and Trx-2, J. Biol. Chem. 277 (2002) 17457-17463.
30. J. Ma, R. Yan, X. Zu, J.M. Cheng, K. Rao, D.F. Liao, D. Cao, Aldo-keto reductase family 1 B10 affects fatty acid synthesis by regulating the stability of acetyl-CoA carboxylase-alpha in breast cancer cells, J. Biol. Chem. 283 (2007) 3418-3423.
31. D.L. Vander Jagt, N.S. Kolb, T.J. Vander Jagt, J. Chino, F.J. Martinez, L.A. Hunsaker, R.E. Royer, Substrate specificity of human aldose reductase: identification of 4-hydroxynonenal as an endogenous substrate, Biochim. Biophys. Acta 1249 (1995) 117-126.
32. B. Lu, Recent advances in using Drosophila to model neurodegenerative diseases, Apoptosis 14 (2009) 1008-1020.