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Smith, M.A.1
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Increased oxidative damage is correlated to altered mitochondrial function in heterozygous manganese superoxide dismutase knockout mice
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Williams MD, Van Remmen H, Conrad CC, Huang TT, Epstein CJ, Richardon A: Increased oxidative damage is correlated to altered mitochondrial function in heterozygous manganese superoxide dismutase knockout mice. J Biol Chem 1998, 273:28510-28515. Manganese Superoxide dismutase (MnSOD) knockout mice, exhibiting a 50% drop in mitochondrial activity of MnSOD but not CuZnSOD or glutathione peroxidase, witness an increased oxidative damage to mitochondria as shown by increased mitochondrial protein carbonyls and 8-hydroxy-deoxyguanosine in mitochondrial DNA. No damage to cytosolic proteins or to nuclear DNA was observed.
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Mezzetti A, Pierdomenico SD, Costantini F, Romano F, De Cesare D, Cuccurullo F, Imbastaro T, Riario-Sforza G, Di Giacomo F, Zuliani G, Fellin R: Copper/zinc ratio and systemic oxidant load: Effect of aging and aging-related degenerative diseases. Free Radical Biol Med 1998, 25:676-681.
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A novel glycosylphosphatidylinositol-anchored from of ceruloplasmin is expressed by mammalian astrocytes
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Patel BN, David S: A novel glycosylphosphatidylinositol-anchored from of ceruloplasmin is expressed by mammalian astrocytes. J Biol Chem 1997, 272:20185-20190. A novel membrane-bound form of ceruloplasmin (CP) expressed by astrocytes in the mammalian CNS is reported. In the liver, CP is the major Fe(II)-oxidizing enzyme, and this could be the same role for the CP in the CNS, as appears to be the case in aceruloplasminemia. Lack of this form could contribute to neuronal degeneration in Parkinson's disease and Alzheimer's disease.
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Patel, B.N.1
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Brown DR, Qin K, Herms JW, Madlung A, Manson J, Strome R, Fraser PE, Kruck T, von Bohlen A, Schulz-Schaeffer W et al.: The cellular prior protein binds copper in vivo. Nature 1997, 390:684-687. The normal cellular form of prion protein binds Cu(II) nearly as strongly as does serum albumin. Thus, binding of Cu(II) to prion protein may indicate a cytoprotective role of this protein.
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Pauly PC, Harris DA: Copper stimulates endocytosis of the prion protein. J Biol Chem 1998, 273:33107-33110. Binding of copper to prion protein rapidly and reversibly stimulates its endocytosis from the surface of neuroblastoma cells in culture. This finding suggests that the normal function of this cell-surface glycoprotein may be as a recycling receptor for uptake of extracellular free copper.
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