A novel giant peroxisomal superoxide dismutase motif-containing protein

Free Radical Biology and Medicine

Volumn 48, Issue 6, 2010, Pages 811-820

  Toutzaris, Diamandis ^a   Lewerenz, Jan ^b   Albrecht, Philipp ^a   Jensen, Laran T ^c   Letz, Julia ^b   Geerts, Andreas ^d   Golz, Stefan ^d   Methner, Axel ^a  

^a UNIVERSITY HOSPITAL DÜSSELDORF   (Germany)

^b UNIVERSITY MEDICAL CENTER HAMBURG EPPENDORF   (Germany)

^c JOHNS HOPKINS UNIVERSITY   (United States)

^d BAYER PHARMA AG   (Germany)

Author keywords

Free radicals; Glutamate toxicity; HT22 cells; Oxidative stress; Peroxisome; SOD

Indexed keywords

CATALASE; GLUTAMIC ACID; HISTIDINE; MUTANT PROTEIN; MYOCILIN; SUPEROXIDE DISMUTASE;

AMINO ACID COMPOSITION; ANIMAL CELL; ARTICLE; CELLULAR DISTRIBUTION; CELLULAR STRESS RESPONSE; CONTROLLED STUDY; CYTOTOXICITY; GENE FUNCTION; GENE LOCATION; GENE OVEREXPRESSION; GENE STRUCTURE; HIPPOCAMPUS; MAMMAL CELL; MOUSE; NERVOUS SYSTEM; NONHUMAN; OXIDATIVE STRESS; PEROXISOME; PRIORITY JOURNAL; PROTEIN CONTENT; PROTEIN MOTIF; PYRAMIDAL NERVE CELL; UPREGULATION;

ANIMALS; CELLS, CULTURED; CLONING, MOLECULAR; CYTOSKELETAL PROTEINS; EYE PROTEINS; GLUTAMIC ACID; GLYCOPROTEINS; MICE; OXIDATIVE STRESS; PEROXISOMES; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, MESSENGER; SUPEROXIDE DISMUTASE;

MAMMALIA;

EID: 76049127092     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2009.12.023     Document Type: Article

References (41)

1. Choi D.W. Glutamate neurotoxicity and diseases of the nervous system. Neuron 1 (1988) 623-634
2. Murphy T.H., Miyamoto M., Sastre A., Schnaar R.L., and Coyle J.T. Glutamate toxicity in a neuronal cell line involves inhibition of cystine transport leading to oxidative stress. Neuron 2 (1989) 1547-1558
3. Murphy T.H., Schnaar R.L., and Coyle J.T. Immature cortical neurons are uniquely sensitive to glutamate toxicity by inhibition of cystine uptake. FASEB J. 4 (1990) 1624-1633
4. Schulz J.B., Lindenau J., Seyfried J., and Dichgans J. Glutathione, oxidative stress and neurodegeneration. Eur. J. Biochem. 267 (2000) 4904-4911
5. Dringen R., Gutterer J.M., and Hirrlinger J. Glutathione metabolism in brain metabolic interaction between astrocytes and neurons in the defense against reactive oxygen species. Eur. J. Biochem. 267 (2000) 4912-4916
6. Beal M.F. Mitochondria, free radicals, and neurodegeneration. Curr. Opin. Neurobiol. 6 (1996) 661-666
7. Coyle J.T., and Puttfarcken P. Oxidative stress, glutamate, and neurodegenerative disorders. Science 262 (1993) 689-695
8. Pratico D. Alzheimer's disease and oxygen radicals: new insights. Biochem. Pharmacol. 63 (2002) 563-567
9. Halliwell B. Reactive oxygen species and the central nervous system. J. Neurochem. 59 (1992) 1609-1623
10. Schubert D., and Piasecki D. Oxidative glutamate toxicity can be a component of the excitotoxicity cascade. J. Neurosci. 21 (2001) 7455-7462
11. Miyamoto M., Murphy T.H., Schnaar R.L., and Coyle J.T. Antioxidants protect against glutamate-induced cytotoxicity in a neuronal cell line. J. Pharmacol. Exp. Ther. 250 (1989) 1132-1140
12. Davis J.B., and Maher P. Protein kinase C activation inhibits glutamate-induced cytotoxicity in a neuronal cell line. Brain Res. 652 (1994) 169-173
13. Maher P., and Davis J.B. The role of monoamine metabolism in oxidative glutamate toxicity. J. Neurosci. 16 (1996) 6394-6401
14. Froissard P., Monrocq H., and Duval D. Role of glutathione metabolism in the glutamate-induced programmed cell death of neuronal-like PC12 cells. Eur. J. Pharmacol. 326 (1997) 93-99
15. Ratan R.R., Murphy T.H., and Baraban J.M. Oxidative stress induces apoptosis in embryonic cortical neurons. J. Neurochem. 62 (1994) 376-379
16. Oka A., Belliveau M.J., Rosenberg P.A., and Volpe J.J. Vulnerability of oligodendroglia to glutamate: pharmacology, mechanisms, and prevention. J. Neurosci. 13 (1993) 1441-1453
17. Chen C.J., Liao S.L., and Kuo J.S. Gliotoxic action of glutamate on cultured astrocytes. J. Neurochem. 75 (2000) 1557-1565
18. Tan S., Wood M., and Maher P. Oxidative stress induces a form of programmed cell death with characteristics of both apoptosis and necrosis in neuronal cells. J. Neurochem. 71 (1998) 95-105
19. Li Y., Maher P., and Schubert D. A role for 12-lipoxygenase in nerve cell death caused by glutathione depletion. Neuron 19 (1997) 453-463
20. Tan S., Sagara Y., Liu Y., Maher P., and Schubert D. The regulation of reactive oxygen species production during programmed cell death. J. Cell Biol. 141 (1998) 1423-1432
21. Li Y., Maher P., and Schubert D. Requirement for cGMP in nerve cell death caused by glutathione depletion. J. Cell Biol. 139 (1997) 1317-1324
22. Lewerenz J., Klein M., and Methner A. Cooperative action of glutamate transporters and cystine/glutamate antiporter system Xc- protects from oxidative glutamate toxicity. J. Neurochem. 98 (2006) 916-925
23. Dittmer S., Sahin M., Pantlen A., Saxena A., Toutzaris D., Pina A.L., Geerts A., Golz S., and Methner A. The constitutively active orphan G-protein-coupled receptor GPR39 protects from cell death by increasing secretion of pigment epithelium-derived growth factor. J. Biol. Chem. 283 (2008) 7074-7081
24. Sahin M., Joost P., Saxena A., Lewerenz J., and Methner A. Induction of Bcl-2 by functional regulation of G-protein coupled receptors protects from oxidative glutamate toxicity by increasing glutathione. Free Radic. Res. 40 (2006) 1113-1123
25. Sturtz L.A., Diekert K., Jensen L.T., Lill R., and Culotta V.C.A. fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. J. Biol. Chem. 276 (2001) 38084-38089
26. Liu X.F., Elashvili I., Gralla E.B., Valentine J.S., Lapinskas P., and Culotta V.C. Yeast lacking superoxide dismutase: isolation of genetic suppressors. J. Biol. Chem. 267 (1992) 18298-18302
27. Slekar K.H., Kosman D., and Culotta V.C. The yeast copper/zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection. J. Biol. Chem. 271 (1996) 28831-28836
28. Gietz R.D., and Schiestl R.H. Applications of high efficiency lithium acetate transformation of intact yeast cells using single-stranded nucleic acids as carrier. Yeast 7 (1991) 253-263
29. Gralla E.B., and Kosman D.J. Molecular genetics of superoxide dismutases in yeasts and related fungi. Adv. Genet. 30 (1992) 251-319
30. Townsend A.J., Leone-Kabler S., Haynes R.L., Wu Y., Szweda L., and Bunting K.D. Selective protection by stably transfected human ALDH3A1 (but not human ALDH1A1) against toxicity of aliphatic aldehydes in V79 cells. Chem. Biol. Interact. 130-132 (2001) 261-273
31. Neuberger G., Maurer-Stroh S., Eisenhaber B., Hartig A., and Eisenhaber F. Prediction of peroxisomal targeting signal 1 containing proteins from amino acid sequence. J. Mol. Biol. 328 (2003) 581-592
32. Bannister J.V., Bannister W.H., and Rotilio G. Aspects of the structure, function, and applications of superoxide dismutase. CRC Crit. Rev. Biochem. 22 (1987) 111-180
33. Culotta V.C., Klomp L., Strain J., Casareno R., Krems B., and Gitlin J.D. The copper chaperone for superoxide dismutase. J. Biol. Chem. 272 (1997) 23469-23472
34. Sagara Y., Dargusch R., Chambers D., Davis J., Schubert D., and Maher P. Cellular mechanisms of resistance to chronic oxidative stress. Free Radic. Biol. Med. 24 (1998) 1375-1389
35. Sagara Y., Ishige K., Tsai C., and Maher P. Tyrphostins protect neuronal cells from oxidative stress. J. Biol. Chem. 277 (2002) 36204-36215
36. Tan S., Somia N., Maher P., and Schubert D. Regulation of antioxidant metabolism by translation initiation factor 2alpha. J. Cell Biol. 152 (2001) 997-1006
37. Lindahl R. Aldehyde dehydrogenases and their role in carcinogenesis. Crit. Rev. Biochem. Mol. Biol. 27 (1992) 283-335
38. Nebert D.W. Drug-metabolizing enzymes, polymorphisms and interindividual response to environmental toxicants. Clin. Chem. Lab. Med. 38 (2000) 857-861
39. Zimatkin S.M. Histochemical study of aldehyde dehydrogenase in the rat CNS. J. Neurochem. 56 (1991) 1-11
40. Iourgenko V., Zhang W., Mickanin C., Daly I., Jiang C., Hexham J.M., Orth A.P., Miraglia L., Meltzer J., Garza D., Chirn G.W., McWhinnie E., Cohen D., Skelton J., Terry R., Yu Y., Bodian D., Buxton F.P., Zhu J., Song C., and Labow M.A. Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells. Proc. Natl. Acad. Sci. USA 100 (2003) 12147-12152
41. Santos M.J., Quintanilla R.A., Toro A., Grandy R., Dinamarca M.C., Godoy J.A., and Inestrosa N.C. Peroxisomal proliferation protects from beta-amyloid neurodegeneration. J. Biol. Chem. 280 (2005) 41057-41068