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Volumn 101, Issue 2-3, 2010, Pages 214-218

Oxidative stress in Niemann-Pick disease, type C

Author keywords

Coenzyme Q10; Lysosomal storage disease; Neurodegenerative disease; Oxidative stress; Trolox equivalent antioxidant capacity

Indexed keywords

ANTIOXIDANT; UBIDECARENONE;

EID: 77957226432     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2010.06.018     Document Type: Article
Times cited : (109)

References (45)
  • 1
    • 0141886877 scopus 로고    scopus 로고
    • Niemann-Pick disease type C
    • Vanier M.T., Millat G. Niemann-Pick disease type C. Clin. Genet. 2003, 64(4):269-281.
    • (2003) Clin. Genet. , vol.64 , Issue.4 , pp. 269-281
    • Vanier, M.T.1    Millat, G.2
  • 2
    • 0030863352 scopus 로고    scopus 로고
    • Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis
    • Carstea E.D., et al. Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis. Science 1997, 277(5323):228-231.
    • (1997) Science , vol.277 , Issue.5323 , pp. 228-231
    • Carstea, E.D.1
  • 3
    • 0034704245 scopus 로고    scopus 로고
    • Identification of HE1 as the second gene of Niemann-Pick C disease
    • Naureckiene S., et al. Identification of HE1 as the second gene of Niemann-Pick C disease. Science 2000, 290(5500):2298-2301.
    • (2000) Science , vol.290 , Issue.5500 , pp. 2298-2301
    • Naureckiene, S.1
  • 4
    • 0034637440 scopus 로고    scopus 로고
    • Topological analysis of Niemann-Pick C1 protein reveals that the membrane orientation of the putative sterol-sensing domain is identical to those of 3-hydroxy-3-methylglutaryl-CoA reductase and sterol regulatory element binding protein cleavage-activating protein
    • Davies J.P., Ioannou Y.A. Topological analysis of Niemann-Pick C1 protein reveals that the membrane orientation of the putative sterol-sensing domain is identical to those of 3-hydroxy-3-methylglutaryl-CoA reductase and sterol regulatory element binding protein cleavage-activating protein. J. Biol. Chem. 2000, 275(32):24367-24374.
    • (2000) J. Biol. Chem. , vol.275 , Issue.32 , pp. 24367-24374
    • Davies, J.P.1    Ioannou, Y.A.2
  • 5
    • 0037418188 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease
    • Friedland N., et al. Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease. Proc. Natl. Acad. Sci. U. S. A. 2003, 100(5):2512-2517.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , Issue.5 , pp. 2512-2517
    • Friedland, N.1
  • 6
    • 67549105629 scopus 로고    scopus 로고
    • Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol
    • Kwon H.J., et al. Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol. Cell 2009, 137(7):1213-1224.
    • (2009) Cell , vol.137 , Issue.7 , pp. 1213-1224
    • Kwon, H.J.1
  • 7
    • 0027976761 scopus 로고
    • The Niemann-Pick C lesion and its relationship to the intracellular distribution and utilization of LDL cholesterol
    • Pentchev P.G., et al. The Niemann-Pick C lesion and its relationship to the intracellular distribution and utilization of LDL cholesterol. Biochim. Biophys. Acta 1994, 1225(3):235-243.
    • (1994) Biochim. Biophys. Acta , vol.1225 , Issue.3 , pp. 235-243
    • Pentchev, P.G.1
  • 8
    • 0035928841 scopus 로고    scopus 로고
    • Critical role for glycosphingolipids in Niemann-Pick disease type C
    • Zervas M., et al. Critical role for glycosphingolipids in Niemann-Pick disease type C. Curr. Biol. 2001, 11(16):1283-1287.
    • (2001) Curr. Biol. , vol.11 , Issue.16 , pp. 1283-1287
    • Zervas, M.1
  • 9
    • 0037815282 scopus 로고    scopus 로고
    • NPC1 and NPC2 regulate cellular cholesterol homeostasis through generation of low density lipoprotein cholesterol-derived oxysterols
    • Frolov A., et al. NPC1 and NPC2 regulate cellular cholesterol homeostasis through generation of low density lipoprotein cholesterol-derived oxysterols. J. Biol. Chem. 2003, 278(28):25517-25525.
    • (2003) J. Biol. Chem. , vol.278 , Issue.28 , pp. 25517-25525
    • Frolov, A.1
  • 10
    • 0030937904 scopus 로고    scopus 로고
    • Peroxisomal impairment in Niemann-Pick type C disease
    • Schedin S., et al. Peroxisomal impairment in Niemann-Pick type C disease. J. Biol. Chem. 1997, 272(10):6245-6251.
    • (1997) J. Biol. Chem. , vol.272 , Issue.10 , pp. 6245-6251
    • Schedin, S.1
  • 11
    • 55549134611 scopus 로고    scopus 로고
    • Niemann-Pick disease type C1 is a sphingosine storage disease that causes deregulation of lysosomal calcium
    • Lloyd-Evans E., et al. Niemann-Pick disease type C1 is a sphingosine storage disease that causes deregulation of lysosomal calcium. Nat. Med. 2008, 14(11):1247-1255.
    • (2008) Nat. Med. , vol.14 , Issue.11 , pp. 1247-1255
    • Lloyd-Evans, E.1
  • 12
    • 0842320913 scopus 로고    scopus 로고
    • Postnatal development of inflammation in a murine model of Niemann-Pick type C disease: immunohistochemical observations of microglia and astroglia
    • Baudry M., et al. Postnatal development of inflammation in a murine model of Niemann-Pick type C disease: immunohistochemical observations of microglia and astroglia. Exp. Neurol. 2003, 184(2):887-903.
    • (2003) Exp. Neurol. , vol.184 , Issue.2 , pp. 887-903
    • Baudry, M.1
  • 13
    • 11444254013 scopus 로고    scopus 로고
    • Apoptosis accompanied by up-regulation of TNF-alpha death pathway genes in the brain of Niemann-Pick type C disease
    • Wu Y.P., et al. Apoptosis accompanied by up-regulation of TNF-alpha death pathway genes in the brain of Niemann-Pick type C disease. Mol. Genet. Metab. 2005, 84(1):9-17.
    • (2005) Mol. Genet. Metab. , vol.84 , Issue.1 , pp. 9-17
    • Wu, Y.P.1
  • 14
    • 3142774112 scopus 로고    scopus 로고
    • Niemann-Pick type C disease involves disrupted neurosteroidogenesis and responds to allopregnanolone
    • Griffin L.D., et al. Niemann-Pick type C disease involves disrupted neurosteroidogenesis and responds to allopregnanolone. Nat. Med. 2004, 10(7):704-711.
    • (2004) Nat. Med. , vol.10 , Issue.7 , pp. 704-711
    • Griffin, L.D.1
  • 15
    • 0028806088 scopus 로고
    • Muscarinic toxins from the black mamba Dendroaspis polylepis
    • Jolkkonen M., et al. Muscarinic toxins from the black mamba Dendroaspis polylepis. Eur. J. Biochem. 1995, 234(2):579-585.
    • (1995) Eur. J. Biochem. , vol.234 , Issue.2 , pp. 579-585
    • Jolkkonen, M.1
  • 16
    • 70349784564 scopus 로고    scopus 로고
    • Oxidative stress in NPC1 deficient cells: protective effect of allopregnanolone
    • Zampieri S., et al. Oxidative stress in NPC1 deficient cells: protective effect of allopregnanolone. J. Cell Mol. Med. 2008.
    • (2008) J. Cell Mol. Med.
    • Zampieri, S.1
  • 17
    • 67349166918 scopus 로고    scopus 로고
    • Cholesterol synthesis inhibitor U18666A and the role of sterol metabolism and trafficking in numerous pathophysiological processes
    • Cenedella R.J. Cholesterol synthesis inhibitor U18666A and the role of sterol metabolism and trafficking in numerous pathophysiological processes. Lipids 2009, 44(6):477-487.
    • (2009) Lipids , vol.44 , Issue.6 , pp. 477-487
    • Cenedella, R.J.1
  • 18
    • 66249083144 scopus 로고    scopus 로고
    • Mitochondrial cholesterol loading exacerbates amyloid beta peptide-induced inflammation and neurotoxicity
    • Fernandez A., et al. Mitochondrial cholesterol loading exacerbates amyloid beta peptide-induced inflammation and neurotoxicity. J. Neurosci. 2009, 29(20):6394-6405.
    • (2009) J. Neurosci. , vol.29 , Issue.20 , pp. 6394-6405
    • Fernandez, A.1
  • 19
    • 33747626511 scopus 로고    scopus 로고
    • Mitochondrial free cholesterol loading sensitizes to TNF- and Fas-mediated steatohepatitis
    • Mari M., et al. Mitochondrial free cholesterol loading sensitizes to TNF- and Fas-mediated steatohepatitis. Cell Metab. 2006, 4(3):185-198.
    • (2006) Cell Metab. , vol.4 , Issue.3 , pp. 185-198
    • Mari, M.1
  • 20
    • 15744378799 scopus 로고    scopus 로고
    • Altered cholesterol metabolism in Niemann-Pick type C1 mouse brains affects mitochondrial function
    • Yu W., et al. Altered cholesterol metabolism in Niemann-Pick type C1 mouse brains affects mitochondrial function. J. Biol. Chem. 2005, 280(12):11731-11739.
    • (2005) J. Biol. Chem. , vol.280 , Issue.12 , pp. 11731-11739
    • Yu, W.1
  • 21
    • 45749136703 scopus 로고    scopus 로고
    • Niemann-Pick C1 protects against atherosclerosis in mice via regulation of macrophage intracellular cholesterol trafficking
    • Zhang J.R., et al. Niemann-Pick C1 protects against atherosclerosis in mice via regulation of macrophage intracellular cholesterol trafficking. J. Clin. Invest. 2008, 118(6):2281-2290.
    • (2008) J. Clin. Invest. , vol.118 , Issue.6 , pp. 2281-2290
    • Zhang, J.R.1
  • 22
    • 0343714594 scopus 로고    scopus 로고
    • Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase
    • Kadenbach B., et al. Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase. Free Radic. Biol. Med. 2000, 29(3-4):211-221.
    • (2000) Free Radic. Biol. Med. , vol.29 , Issue.3-4 , pp. 211-221
    • Kadenbach, B.1
  • 23
    • 0030770030 scopus 로고    scopus 로고
    • Plasma ratio of ubiquinol and ubiquinone as a marker of oxidative stress
    • Yamamoto Y., Yamashita S. Plasma ratio of ubiquinol and ubiquinone as a marker of oxidative stress. Mol. Aspects Med. 1997, 18 Suppl:S79-S84.
    • (1997) Mol. Aspects Med. , vol.18 Suppl
    • Yamamoto, Y.1    Yamashita, S.2
  • 24
    • 0027397359 scopus 로고
    • Autoxidation of lipids and antioxidation by alpha-tocopherol and ubiquinol in homogeneous solution and in aqueous dispersions of lipids: unrecognized consequences of lipid particle size as exemplified by oxidation of human low density lipoprotein
    • Ingold K.U., et al. Autoxidation of lipids and antioxidation by alpha-tocopherol and ubiquinol in homogeneous solution and in aqueous dispersions of lipids: unrecognized consequences of lipid particle size as exemplified by oxidation of human low density lipoprotein. Proc. Natl. Acad. Sci. U. S. A. 1993, 90(1):45-49.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , Issue.1 , pp. 45-49
    • Ingold, K.U.1
  • 25
    • 33746360550 scopus 로고    scopus 로고
    • Free radical scavenger and antioxidant capacity correlation of alpha-tocopherol and Trolox measured by three in vitro methodologies
    • Castro I.A., et al. Free radical scavenger and antioxidant capacity correlation of alpha-tocopherol and Trolox measured by three in vitro methodologies. Int. J. Food Sci. Nutr. 2006, 57(1-2):75-82.
    • (2006) Int. J. Food Sci. Nutr. , vol.57 , Issue.1-2 , pp. 75-82
    • Castro, I.A.1
  • 26
    • 73949159934 scopus 로고    scopus 로고
    • Linear clinical progression, independent of age of onset, in Niemann-Pick disease, type C. Am J Med Genet B Neuropsychiatr Genet. 153B
    • Yanjanin, N.M., et al., Linear clinical progression, independent of age of onset, in Niemann-Pick disease, type C. Am J Med Genet B Neuropsychiatr Genet. 153B(1): p. 132-40.
    • , Issue.1 , pp. 132-40
    • Yanjanin, N.M.1
  • 27
    • 77949441746 scopus 로고    scopus 로고
    • Long-term miglustat therapy in children with Niemann-Pick disease type C
    • Patterson M.C., et al. Long-term miglustat therapy in children with Niemann-Pick disease type C. J. Child Neurol. 2009.
    • (2009) J. Child Neurol.
    • Patterson, M.C.1
  • 28
    • 3042841602 scopus 로고    scopus 로고
    • A novel role of lactosylceramide in the regulation of lipopolysaccharide/interferon-gamma-mediated inducible nitric oxide synthase gene expression: implications for neuroinflammatory diseases
    • Pannu R., et al. A novel role of lactosylceramide in the regulation of lipopolysaccharide/interferon-gamma-mediated inducible nitric oxide synthase gene expression: implications for neuroinflammatory diseases. J. Neurosci. 2004, 24(26):5942-5954.
    • (2004) J. Neurosci. , vol.24 , Issue.26 , pp. 5942-5954
    • Pannu, R.1
  • 29
    • 62649107795 scopus 로고    scopus 로고
    • Inherited disorders affecting mitochondrial function are associated with glutathione deficiency and hypocitrullinemia
    • Atkuri K.R., et al. Inherited disorders affecting mitochondrial function are associated with glutathione deficiency and hypocitrullinemia. Proc. Natl Acad. Sci. USA 2009, 106(10):3941-3945.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , Issue.10 , pp. 3941-3945
    • Atkuri, K.R.1
  • 30
    • 52649137489 scopus 로고    scopus 로고
    • Coenzyme Q(10) and alpha-lipoic acid supplementation in diabetic rats: conduction velocity distributions
    • Ayaz M., et al. Coenzyme Q(10) and alpha-lipoic acid supplementation in diabetic rats: conduction velocity distributions. Methods Find. Exp. Clin. Pharmacol. 2008, 30(5):367-374.
    • (2008) Methods Find. Exp. Clin. Pharmacol. , vol.30 , Issue.5 , pp. 367-374
    • Ayaz, M.1
  • 31
    • 58149385696 scopus 로고    scopus 로고
    • Coenzyme Q10 and oxidative imbalance in Down syndrome: biochemical and clinical aspects
    • Tiano L., et al. Coenzyme Q10 and oxidative imbalance in Down syndrome: biochemical and clinical aspects. Biofactors 2008, 32(1-4):161-167.
    • (2008) Biofactors , vol.32 , Issue.1-4 , pp. 161-167
    • Tiano, L.1
  • 32
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction
    • Devi L., et al. Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction. J. Neurosci. 2006, 26(35):9057-9068.
    • (2006) J. Neurosci. , vol.26 , Issue.35 , pp. 9057-9068
    • Devi, L.1
  • 33
    • 55849122639 scopus 로고    scopus 로고
    • Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis
    • Henchcliffe C., Beal M.F. Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis. Nat. Clin. Pract. Neurol. 2008, 4(11):600-609.
    • (2008) Nat. Clin. Pract. Neurol. , vol.4 , Issue.11 , pp. 600-609
    • Henchcliffe, C.1    Beal, M.F.2
  • 34
    • 10644241578 scopus 로고    scopus 로고
    • An increase of oxidized coenzyme Q-10 occurs in the plasma of sporadic ALS patients
    • Sohmiya M., et al. An increase of oxidized coenzyme Q-10 occurs in the plasma of sporadic ALS patients. J. Neurol. Sci. 2005, 228(1):49-53.
    • (2005) J. Neurol. Sci. , vol.228 , Issue.1 , pp. 49-53
    • Sohmiya, M.1
  • 35
    • 4043181369 scopus 로고    scopus 로고
    • Clinical laboratory monitoring of coenzyme Q10 use in neurologic and muscular diseases
    • Steele P.E., et al. Clinical laboratory monitoring of coenzyme Q10 use in neurologic and muscular diseases. Am. J. Clin. Pathol. 2004, 121 Suppl:S113-S120.
    • (2004) Am. J. Clin. Pathol. , vol.121 Suppl
    • Steele, P.E.1
  • 36
    • 0036523110 scopus 로고    scopus 로고
    • Therapeutic effects of coenzyme Q10 and remacemide in transgenic mouse models of Huntington's disease
    • Ferrante R.J., et al. Therapeutic effects of coenzyme Q10 and remacemide in transgenic mouse models of Huntington's disease. J. Neurosci. 2002, 22(5):1592-1599.
    • (2002) J. Neurosci. , vol.22 , Issue.5 , pp. 1592-1599
    • Ferrante, R.J.1
  • 37
    • 56049088295 scopus 로고    scopus 로고
    • Coenzyme Q10 and vitamin E deficiency in Friedreich's ataxia: predictor of efficacy of vitamin E and coenzyme Q10 therapy
    • Cooper J.M., et al. Coenzyme Q10 and vitamin E deficiency in Friedreich's ataxia: predictor of efficacy of vitamin E and coenzyme Q10 therapy. Eur. J. Neurol. 2008, 15(12):1371-1379.
    • (2008) Eur. J. Neurol. , vol.15 , Issue.12 , pp. 1371-1379
    • Cooper, J.M.1
  • 38
    • 1242352531 scopus 로고    scopus 로고
    • A comparison of family history of psychiatric disorders among patients with early- and late-onset Alzheimer's disease
    • Devi G., et al. A comparison of family history of psychiatric disorders among patients with early- and late-onset Alzheimer's disease. J. Neuropsychiatry Clin. Neurosci. 2004, 16(1):57-62.
    • (2004) J. Neuropsychiatry Clin. Neurosci. , vol.16 , Issue.1 , pp. 57-62
    • Devi, G.1
  • 39
    • 9244256748 scopus 로고    scopus 로고
    • The role of DT-diaphorase in the maintenance of the reduced antioxidant form of coenzyme Q in membrane systems
    • Beyer R.E., et al. The role of DT-diaphorase in the maintenance of the reduced antioxidant form of coenzyme Q in membrane systems. Proc. Natl. Acad. Sci. U. S. A. 1996, 93(6):2528-2532.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , Issue.6 , pp. 2528-2532
    • Beyer, R.E.1
  • 40
    • 0028915679 scopus 로고
    • Prevention of tocopherol-mediated peroxidation in ubiquinol-10-free human low density lipoprotein
    • Bowry V.W., et al. Prevention of tocopherol-mediated peroxidation in ubiquinol-10-free human low density lipoprotein. J. Biol. Chem. 1995, 270(11):5756-5763.
    • (1995) J. Biol. Chem. , vol.270 , Issue.11 , pp. 5756-5763
    • Bowry, V.W.1
  • 41
    • 36148991943 scopus 로고    scopus 로고
    • Cell-autonomous death of cerebellar purkinje neurons with autophagy in Niemann-Pick type C disease
    • Ko D.C., et al. Cell-autonomous death of cerebellar purkinje neurons with autophagy in Niemann-Pick type C disease. PLoS Genet. 2005, 1(1):81-95.
    • (2005) PLoS Genet. , vol.1 , Issue.1 , pp. 81-95
    • Ko, D.C.1
  • 42
    • 43749115379 scopus 로고    scopus 로고
    • Niemann-Pick type C1 I1061T mutant encodes a functional protein that is selected for endoplasmic reticulum-associated degradation due to protein misfolding
    • Gelsthorpe M.E., et al. Niemann-Pick type C1 I1061T mutant encodes a functional protein that is selected for endoplasmic reticulum-associated degradation due to protein misfolding. J. Biol. Chem. 2008, 283(13):8229-8236.
    • (2008) J. Biol. Chem. , vol.283 , Issue.13 , pp. 8229-8236
    • Gelsthorpe, M.E.1
  • 43
    • 34648822560 scopus 로고    scopus 로고
    • Influence of food intake on the pharmacokinetics of miglustat, an inhibitor of glucosylceramide synthase
    • van Giersbergen P.L., Dingemanse J. Influence of food intake on the pharmacokinetics of miglustat, an inhibitor of glucosylceramide synthase. J. Clin. Pharmacol. 2007, 47(10):1277-1282.
    • (2007) J. Clin. Pharmacol. , vol.47 , Issue.10 , pp. 1277-1282
    • van Giersbergen, P.L.1    Dingemanse, J.2
  • 44
    • 0041700117 scopus 로고    scopus 로고
    • Cholesterol accumulation in NPC1-deficient neurons is ganglioside dependent
    • Gondre-Lewis M.C., McGlynn R., Walkley S.U. Cholesterol accumulation in NPC1-deficient neurons is ganglioside dependent. Curr. Biol. 2003, 13(15):1324-1329.
    • (2003) Curr. Biol. , vol.13 , Issue.15 , pp. 1324-1329
    • Gondre-Lewis, M.C.1    McGlynn, R.2    Walkley, S.U.3
  • 45
    • 34547753513 scopus 로고    scopus 로고
    • Miglustat for treatment of Niemann-Pick C disease: a randomised controlled study
    • Patterson M.C., et al. Miglustat for treatment of Niemann-Pick C disease: a randomised controlled study. Lancet Neurol. 2007, 6(9):765-772.
    • (2007) Lancet Neurol. , vol.6 , Issue.9 , pp. 765-772
    • Patterson, M.C.1


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