Down regulation of DJ-1 enhances cell death by oxidative stress, ER stress, and proteasome inhibition

Biochemical and Biophysical Research Communications

Volumn 312, Issue 4, 2003, Pages 1342-1348

  Yokota, Takanori ^a   Sugawara, Kanako ^a   Ito, Kaoru ^a   Takahashi, Ryosuke ^b   Ariga, Hiroyoshi ^c,d   Mizusawa, Hidehiro ^a  

^a TOKYO MEDICAL AND DENTAL UNIVERSITY   (Japan)

^b RIKEN BRAIN SCIENCE INSTITUTE   (Japan)

^c HOKKAIDO UNIVERSITY   (Japan)

^d JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

Autosomal recessive early onset parkinsonism; DJ 1; ER stress; Hydrogen peroxide; Oxidative stress; Park 7; Parkinson's disease; Proteasome inhibition

Indexed keywords

GENE PRODUCT; HYDROGEN PEROXIDE; PAEL RECEPTOR; PARKIN; PROTEASOME; RECEPTOR; RNA; UNCLASSIFIED DRUG;

ANIMAL CELL; APOPTOSIS; ARTICLE; CELL DEATH; CELL LINE; CELL STIMULATION; CONTROLLED STUDY; DJ1 GENE; DOWN REGULATION; ENDOPLASMIC RETICULUM; ENZYME INHIBITION; GENE; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; INHIBITION KINETICS; MOUSE; NERVE CELL; NONHUMAN; OXIDATIVE STRESS; PARKINSONISM; PRIORITY JOURNAL; WILD TYPE;

EID: 0345357664     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.11.056     Document Type: Article

References (21)

1. Kitada T., Asakaw S., Hattori N., Matsumin H., Yamamura Y., Minoshima S., Yokochi M., Mizuno Y., Shimizu N. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature. 392:1998;605-608.
2. Bonifati V., Rizzu P., van Baren M.J., Schaap O., Breedveld G.J., Krieger E., Dekker M.C., Squitieri F., Ibanez P., Joosse M., van Dongen J.W., Vanacore N., van Swieten J.C., Brice A., Meco G., van Duijn C.M., Oostra B.A., Heutink P. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science. 299:2003;256-259.
3. Nagakubo D., Taira T., Kitaura H., Ikeda M., Tamai K., Iguchi-Ariga S.M., Ariga H. DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras. Biochem. Biophys. Res. Commun. 231:1997;509-513.
4. Mitsumoto A., Nakagawa Y. DJ-1 is an indicator for endogenous reactive oxygen species elicited by endotoxin. Free Radic. Res. 35:2001;885-893.
5. Takahashi K., Taira T., Niki T., Seino C., Iguchi-Ariga S.M.M., Ariga H. DJ-1 positively regulates the androgen receptor by impairing the binding of PIASxa to the receptor. J. Biol. Chem. 276:2001;37556-37563.
6. Yokota T., Sakamoto N., Enomto N., Tanabe Y., Miyagishi M., Maekawa S., Li Y., Kurosaki M., Taira K., Watanabe M., Mizusawa H. Inhibition of intracellular hepatitis C virus replication by synthetic and vector-derived small interfering RNAs. EMBO Rep. 2003;602-608.
7. Okada M., Matsumoto K., Niki T., Taira T., Iguchi-Ariga S.M.M., Ariga H. DJ-1, a target protein for an endocrine disrupter, participates in the fertilization in mice. Biol. Pharm. Bull. 25:2002;853-856.
8. Hague S., Rogaeva E., Hernande D., Gulick C., Singleton A., Hanson M., Johnson J., Weiser R., Gallardo M., Ravina B., Gwinn-Hardy K., Crawley A., St George-Hyslop P.H., Lang A.E., Heutink P., Bonifati V., Hardy J., Singleton A. Early-onset Parkinson's disease caused by a compound heterozygous DJ-1 mutation. Ann. Neurol. 54:2003;271-274.
9. Abou-Sleiman P.M., Healy D.G., Quinn N., Lees A.J., Wood N.W. The role of pathogenic DJ-1 mutations in Parkinson's disease. Ann. Neurol. 54:2003;283-286.
10. Miller D.W., Ahmad R., Hague S., Baptist M.J., Canet-Avile R., McLendon C., Carte C.M., Zhu P.P., Stadler J., Chandran J., Klinefelter G.R., Blackstone C., Cookson M.R. Related L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome system. J. Biol. Chem. 278:2003;36588-36595.
11. Macedo M.G., Anar B., Bronner I.F., Cannella M., Squitieri F., Bonifati V., Hoogeveen A., Heutink P., Rizzu P. The DJ-1L166P mutant protein associated with early onset Parkinson's disease is unstable and forms higher protein complexes. Hum. Mol. Genet. 12:2003;2807-2816.
12. Jenner P. Oxidative stress in Parkinson's disease. Ann. Neurol. 53(Suppl. 3):2003;S26-S36.
13. Griffiths P.D., Dobson B.R., Jones G.R., Clarke D.T. Iron in the basal ganglia in Parkinson's disease. An in vitro study using extended X-ray absorption fine structure and cryo-electron microscopy. Brain. 122:1999;667-673.
14. Andersen J.K. Do alterations in glutathione and iron levels contribute to pathology associated with Parkinson's disease? Ageing Vulnerability: Causes and Interventions, Novartis Foundation Symposium. vol. 235:2001;11-25 Wiley, New York.
15. Gutteridge J.M.C. Iron and oxygen radicals in brain. Ann. Neurol. 32:1992;S16-S21.
16. Imai Y., Soda M., Inoue H., Hattori N., Mizuno Y., Takahashi R. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell. 105:2001;891-902.
17. Imai Y., Soda M., Takahashi R. Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J. Biol. Chem. 275:2000;35661-35664.
18. Stefanis L., Larsen K.E., Rideout H.J., Sulzer D., Greene L.A. Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. J. Neurosci. 21:2001;9549-9560.
19. Tanaka Y., Engelender S., Igarashi S., Rao R.K., Wanner T., Tanzi R.E., Sawa A.L., Dawson V., Dawson T.M., Ross C.A. Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis. Hum. Mol. Genet. 10:2001;919-926.
20. Petrucelli L., O'Farrell C., Lockhart P.J., Baptist M., Kehoe K., Vink L., Choi P., Wolozin B., Farrer M., Hardy J., Cookson M.R. Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons. Neuron. 36:2002;1007-1019.
21. Harding H.P., Zhang Y., Zeng H., Novoa I., Lu P.D., Calfon M., Sadri N., Yun C., Popko B., Paules R., Stojdl D.F., Bell J.C., Hettmann T., Leiden J.M., Ron D. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol. Cell. 11:2003;619-633.