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Volumn 57, Issue 2, 2010, Pages 102-110

Deficiency of ubiquitin carboxy-terminal hydrolase-L1 (UCH-L1) leads to vulnerability to lipid peroxidation

Author keywords

Tocopherol (vitamin E); Dorsal root ganglion; Gracile axonal dystrophy (gad); Lipid peroxidation; Phosphatidic acid; UCH L1

Indexed keywords

4 HYDROXYNONENAL; ALPHA TOCOPHEROL; UBIQUITIN THIOLESTERASE; UBIQUITIN THIOLESTERASE 1; UNCLASSIFIED DRUG; PHOSPHATIDIC ACID;

EID: 77953912384     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2010.04.015     Document Type: Article
Times cited : (19)

References (56)
  • 1
    • 24944511195 scopus 로고    scopus 로고
    • Immunocytochemical localization of a neuron-specific diacylglycerol kinase beta and gamma in the developing rat brain
    • Adachi N., Oyasu M., Taniguchi T., Yamaguchi Y., Takenaka R., Shirai Y., Saito N. Immunocytochemical localization of a neuron-specific diacylglycerol kinase beta and gamma in the developing rat brain. Brain Res. Mol. Brain Res. 2005, 139:288-299.
    • (2005) Brain Res. Mol. Brain Res. , vol.139 , pp. 288-299
    • Adachi, N.1    Oyasu, M.2    Taniguchi, T.3    Yamaguchi, Y.4    Takenaka, R.5    Shirai, Y.6    Saito, N.7
  • 2
    • 0036700750 scopus 로고    scopus 로고
    • Protective role of vitamin E on mefenamic acid-induced alterations in erythrocytes
    • Ahmad I., Suhail M. Protective role of vitamin E on mefenamic acid-induced alterations in erythrocytes. Biochemistry (Mosc.) 2002, 67:945-948.
    • (2002) Biochemistry (Mosc.) , vol.67 , pp. 945-948
    • Ahmad, I.1    Suhail, M.2
  • 4
    • 0029888864 scopus 로고    scopus 로고
    • Phosphatidate phosphohydrolase and signal transduction
    • Brindley D.N., Waggoner D.W. Phosphatidate phosphohydrolase and signal transduction. Chem. Phys. Lipids 1996, 80:45-57.
    • (1996) Chem. Phys. Lipids , vol.80 , pp. 45-57
    • Brindley, D.N.1    Waggoner, D.W.2
  • 7
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
    • Choi J., Levey A.I., Weintraub S.T., Rees H.D., Gearing M., Chin L.S., Li L. Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. J. Biol. Chem. 2004, 279:13256-13264.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3    Rees, H.D.4    Gearing, M.5    Chin, L.S.6    Li, L.7
  • 8
    • 77953917609 scopus 로고    scopus 로고
    • CLEA Japan, Inc., CLEA Rodent Diet CE-2 (for breeding and reproduction).
    • CLEA Japan, Inc., 2007. CLEA Rodent Diet CE-2 (for breeding and reproduction). http://www.clea-japan.com/Feed/ce2.html.
    • (2007)
  • 10
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson W.S., Jonas A., Clayton D.F., George J.M. Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 1998, 273:9443-9449.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 11
    • 33947280424 scopus 로고    scopus 로고
    • Alpha-synuclein gene ablation increases docosahexaenoic acid incorporation and turnover in brain phospholipids
    • Golovko M.Y., Rosenberger T.A., Feddersen S., Faergeman N.J., Murphy E.J. Alpha-synuclein gene ablation increases docosahexaenoic acid incorporation and turnover in brain phospholipids. J. Neurochem. 2007, 101:201-211.
    • (2007) J. Neurochem. , vol.101 , pp. 201-211
    • Golovko, M.Y.1    Rosenberger, T.A.2    Feddersen, S.3    Faergeman, N.J.4    Murphy, E.J.5
  • 13
    • 0025880527 scopus 로고
    • The effect of n-3 fatty acids on osmotic fragility of rat erythrocytes
    • Hagve T.A., Johansen Y., Christophersen B. The effect of n-3 fatty acids on osmotic fragility of rat erythrocytes. Biochim. Biophys. Acta 1991, 1084:251-254.
    • (1991) Biochim. Biophys. Acta , vol.1084 , pp. 251-254
    • Hagve, T.A.1    Johansen, Y.2    Christophersen, B.3
  • 15
    • 0028033002 scopus 로고
    • Increased proportion of docosahexanoic acid and high lipid peroxidation capacity in erythrocytes of stroke patients
    • Imre S.G., Fekete I., Farkas T. Increased proportion of docosahexanoic acid and high lipid peroxidation capacity in erythrocytes of stroke patients. Stroke 1994, 25:2416-2420.
    • (1994) Stroke , vol.25 , pp. 2416-2420
    • Imre, S.G.1    Fekete, I.2    Farkas, T.3
  • 16
    • 53049101345 scopus 로고    scopus 로고
    • Aberrant interaction between Parkinson disease-associated mutant UCH-L1 and the lysosomal receptor for chaperone-mediated autophagy
    • Kabuta T., Furuta A., Aoki S., Furuta K., Wada K. Aberrant interaction between Parkinson disease-associated mutant UCH-L1 and the lysosomal receptor for chaperone-mediated autophagy. J. Biol. Chem. 2008, 283:23731-23738.
    • (2008) J. Biol. Chem. , vol.283 , pp. 23731-23738
    • Kabuta, T.1    Furuta, A.2    Aoki, S.3    Furuta, K.4    Wada, K.5
  • 17
    • 43049093757 scopus 로고    scopus 로고
    • Aberrant molecular properties shared by familial Parkinson's disease-associated mutant UCH-L1 and carbonyl-modified UCH-L1
    • Kabuta T., Setsuie R., Mitsui T., Kinugawa A., Sakurai M., Aoki S., Uchida K., Wada K. Aberrant molecular properties shared by familial Parkinson's disease-associated mutant UCH-L1 and carbonyl-modified UCH-L1. Hum. Mol. Genet. 2008, 17:1482-1496.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 1482-1496
    • Kabuta, T.1    Setsuie, R.2    Mitsui, T.3    Kinugawa, A.4    Sakurai, M.5    Aoki, S.6    Uchida, K.7    Wada, K.8
  • 19
    • 0032502276 scopus 로고    scopus 로고
    • Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases
    • Larsen C.N., Krantz B.A., Wilkinson K.D. Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases. Biochemistry 1998, 37:3358-3368.
    • (1998) Biochemistry , vol.37 , pp. 3358-3368
    • Larsen, C.N.1    Krantz, B.A.2    Wilkinson, K.D.3
  • 20
    • 0037131567 scopus 로고    scopus 로고
    • The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility
    • Liu Y., Fallon L., Lashuel H.A., Liu Z., Lansbury P.T. The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility. Cell 2002, 111:209-218.
    • (2002) Cell , vol.111 , pp. 209-218
    • Liu, Y.1    Fallon, L.2    Lashuel, H.A.3    Liu, Z.4    Lansbury, P.T.5
  • 21
    • 66449116737 scopus 로고    scopus 로고
    • Intracellular trafficking of presenilin 1 is regulated by beta-amyloid precursor protein and phospholipase D1
    • Liu Y., Zhang Y.W., Wang X., Zhang H., You X., Liao F.F., Xu H. Intracellular trafficking of presenilin 1 is regulated by beta-amyloid precursor protein and phospholipase D1. J. Biol. Chem. 2009, 284:12145-12152.
    • (2009) J. Biol. Chem. , vol.284 , pp. 12145-12152
    • Liu, Y.1    Zhang, Y.W.2    Wang, X.3    Zhang, H.4    You, X.5    Liao, F.F.6    Xu, H.7
  • 23
    • 0024810802 scopus 로고
    • Neuropathology of gracile axonal dystrophy (GAD) mouse. An animal model of central distal axonopathy in primary sensory neurons
    • Mukoyama M., Yamazaki K., Kikuchi T., Tomita T. Neuropathology of gracile axonal dystrophy (GAD) mouse. An animal model of central distal axonopathy in primary sensory neurons. Acta Neuropathol. 1989, 79:294-299.
    • (1989) Acta Neuropathol. , vol.79 , pp. 294-299
    • Mukoyama, M.1    Yamazaki, K.2    Kikuchi, T.3    Tomita, T.4
  • 27
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis
    • Perrin R.J., Woods W.S., Clayton D.F., George J.M. Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis. J. Biol. Chem. 2000, 275:34393-34398.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34393-34398
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 29
    • 0037359765 scopus 로고    scopus 로고
    • Apolipoprotein E and cholesterol metabolism in the pathogenesis and treatment of Alzheimer's disease
    • Poirier J. Apolipoprotein E and cholesterol metabolism in the pathogenesis and treatment of Alzheimer's disease. Trends Mol. Med. 2003, 9:94-101.
    • (2003) Trends Mol. Med. , vol.9 , pp. 94-101
    • Poirier, J.1
  • 30
    • 57649221161 scopus 로고    scopus 로고
    • Evidence of oxidative stress in Alzheimer's disease brain and antioxidant therapy: lights and shadows
    • Pratico D. Evidence of oxidative stress in Alzheimer's disease brain and antioxidant therapy: lights and shadows. Ann. NY Acad. Sci. 2008, 1147:70-78.
    • (2008) Ann. NY Acad. Sci. , vol.1147 , pp. 70-78
    • Pratico, D.1
  • 31
    • 0035857445 scopus 로고    scopus 로고
    • Elevated activity of phospholipid biosynthetic enzymes in substantia nigra of patients with Parkinson's disease
    • Ross B.M., Mamalias N., Moszczynska A., Rajput A.H., Kish S.J. Elevated activity of phospholipid biosynthetic enzymes in substantia nigra of patients with Parkinson's disease. Neuroscience 2001, 102:899-904.
    • (2001) Neuroscience , vol.102 , pp. 899-904
    • Ross, B.M.1    Mamalias, N.2    Moszczynska, A.3    Rajput, A.H.4    Kish, S.J.5
  • 32
    • 0031937355 scopus 로고    scopus 로고
    • Phospholipid-metabolizing enzymes in Alzheimer's disease: increased lysophospholipid acyltransferase activity and decreased phospholipase A2 activity
    • Ross B.M., Moszczynska A., Erlich J., Kish S.J. Phospholipid-metabolizing enzymes in Alzheimer's disease: increased lysophospholipid acyltransferase activity and decreased phospholipase A2 activity. J. Neurochem. 1998, 70:786-793.
    • (1998) J. Neurochem. , vol.70 , pp. 786-793
    • Ross, B.M.1    Moszczynska, A.2    Erlich, J.3    Kish, S.J.4
  • 33
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C.A., Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 2004, 10(Suppl.):S10-17.
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 34
    • 0037163887 scopus 로고    scopus 로고
    • Vitamin E sensitive genes in the developing rat fetal brain: a high-density oligonucleotide microarray analysis
    • Roy S., Lado B.H., Khanna S., Sen C.K. Vitamin E sensitive genes in the developing rat fetal brain: a high-density oligonucleotide microarray analysis. FEBS Lett. 2002, 530:17-23.
    • (2002) FEBS Lett. , vol.530 , pp. 17-23
    • Roy, S.1    Lado, B.H.2    Khanna, S.3    Sen, C.K.4
  • 35
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein D.C. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 2006, 443:780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 37
    • 0030989545 scopus 로고    scopus 로고
    • 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease
    • Sayre L.M., Zelasko D.A., Harris P.L., Perry G., Salomon R.G., Smith M.A. 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease. J. Neurochem. 1997, 68:2092-2097.
    • (1997) J. Neurochem. , vol.68 , pp. 2092-2097
    • Sayre, L.M.1    Zelasko, D.A.2    Harris, P.L.3    Perry, G.4    Salomon, R.G.5    Smith, M.A.6
  • 38
    • 2942699852 scopus 로고    scopus 로고
    • Yeast genetics targets lipids in Parkinson's disease
    • Scherzer C.R., Feany M.B. Yeast genetics targets lipids in Parkinson's disease. Trends Genet. 2004, 20:273-277.
    • (2004) Trends Genet. , vol.20 , pp. 273-277
    • Scherzer, C.R.1    Feany, M.B.2
  • 40
    • 39849101072 scopus 로고    scopus 로고
    • Neuroaxonal dystrophy caused by group VIA phospholipase A2 deficiency in mice: a model of human neurodegenerative disease
    • Shinzawa K., Sumi H., Ikawa M., Matsuoka Y., Okabe M., Sakoda S., Tsujimoto Y. Neuroaxonal dystrophy caused by group VIA phospholipase A2 deficiency in mice: a model of human neurodegenerative disease. J. Neurosci. 2008, 28:2212-2220.
    • (2008) J. Neurosci. , vol.28 , pp. 2212-2220
    • Shinzawa, K.1    Sumi, H.2    Ikawa, M.3    Matsuoka, Y.4    Okabe, M.5    Sakoda, S.6    Tsujimoto, Y.7
  • 41
    • 37549068169 scopus 로고    scopus 로고
    • Alpha-synuclein selectively binds to anionic phospholipids embedded in liquid-disordered domains
    • Stockl M., Fischer P., Wanker E., Herrmann A. Alpha-synuclein selectively binds to anionic phospholipids embedded in liquid-disordered domains. J. Mol. Biol. 2008, 375:1394-1404.
    • (2008) J. Mol. Biol. , vol.375 , pp. 1394-1404
    • Stockl, M.1    Fischer, P.2    Wanker, E.3    Herrmann, A.4
  • 42
    • 0015810617 scopus 로고
    • Phospholipids and acyl groups in subcellular fractions from human cerebral cortex
    • Sun G.Y. Phospholipids and acyl groups in subcellular fractions from human cerebral cortex. J. Lipid Res. 1973, 14:656-663.
    • (1973) J. Lipid Res. , vol.14 , pp. 656-663
    • Sun, G.Y.1
  • 43
    • 0018897698 scopus 로고
    • Axonal dystrophy in the gracile nucleus in congenital biliary atresia and cystic fibrosis (mucoviscidosis): beneficial effect of vitamin E therapy
    • Sung J.H., Park S.H., Mastri A.R., Warwick W.J. Axonal dystrophy in the gracile nucleus in congenital biliary atresia and cystic fibrosis (mucoviscidosis): beneficial effect of vitamin E therapy. J. Neuropathol. Exp. Neurol. 1980, 39:584-597.
    • (1980) J. Neuropathol. Exp. Neurol. , vol.39 , pp. 584-597
    • Sung, J.H.1    Park, S.H.2    Mastri, A.R.3    Warwick, W.J.4
  • 44
    • 54249158324 scopus 로고    scopus 로고
    • Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
    • Tai H.C., Schuman E.M. Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nat. Rev. Neurosci. 2008, 9:826-838.
    • (2008) Nat. Rev. Neurosci. , vol.9 , pp. 826-838
    • Tai, H.C.1    Schuman, E.M.2
  • 46
    • 0026748832 scopus 로고
    • Effect of docosahexaenoic acid on membrane fluidity and function in intact cultured Y-79 retinoblastoma cells
    • Treen M., Uauy R.D., Jameson D.M., Thomas V.L., Hoffman D.R. Effect of docosahexaenoic acid on membrane fluidity and function in intact cultured Y-79 retinoblastoma cells. Arch. Biochem. Biophys. 1992, 294:564-570.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 564-570
    • Treen, M.1    Uauy, R.D.2    Jameson, D.M.3    Thomas, V.L.4    Hoffman, D.R.5
  • 47
    • 0023711866 scopus 로고
    • Effect of high doses of dietary vitamin E on the concentrations of vitamin E in several brain regions, plasma, liver, and adipose tissue of rats
    • Vatassery G.T., Brin M.F., Fahn S., Kayden H.J., Traber M.G. Effect of high doses of dietary vitamin E on the concentrations of vitamin E in several brain regions, plasma, liver, and adipose tissue of rats. J. Neurochem. 1988, 51:621-623.
    • (1988) J. Neurochem. , vol.51 , pp. 621-623
    • Vatassery, G.T.1    Brin, M.F.2    Fahn, S.3    Kayden, H.J.4    Traber, M.G.5
  • 52
    • 58149465620 scopus 로고    scopus 로고
    • Reduced membrane lipids in the cortex of Alzheimer's disease transgenic mice
    • Yao J.K., Wengenack T.M., Curran G.L., Poduslo J.F. Reduced membrane lipids in the cortex of Alzheimer's disease transgenic mice. Neurochem. Res. 2009, 34:102-108.
    • (2009) Neurochem. Res. , vol.34 , pp. 102-108
    • Yao, J.K.1    Wengenack, T.M.2    Curran, G.L.3    Poduslo, J.F.4
  • 55
    • 34447568476 scopus 로고    scopus 로고
    • Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos
    • Zhao C., Du G., Skowronek K., Frohman M.A., Bar-Sagi D. Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos. Nat. Cell Biol. 2007, 9:706-712.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 706-712
    • Zhao, C.1    Du, G.2    Skowronek, K.3    Frohman, M.A.4    Bar-Sagi, D.5
  • 56
    • 57649155208 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease: a mechanism of pathogenic and therapeutic significance
    • Zhou C., Huang Y., Przedborski S. Oxidative stress in Parkinson's disease: a mechanism of pathogenic and therapeutic significance. Ann. NY Acad. Sci. 2008, 1147:93-104.
    • (2008) Ann. NY Acad. Sci. , vol.1147 , pp. 93-104
    • Zhou, C.1    Huang, Y.2    Przedborski, S.3


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