Ageing and exposure to oxidative stress in vivo differentially affect cellular levels of PrPc in mouse cerebral microvessels and brain parenchyma

Neuropathology and Applied Neurobiology

Volumn 30, Issue 2, 2004, Pages 161-168

  Williams, W M ^a,b   Stadtman, E R ^a   Moskovitz, J ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

^b LOUIS STOKES CLEVELAND VA MEDICAL CENTER   (United States)

Author keywords

Ageing; Brain; Hyperoxia; Microvessel; Mouse; Oxidative stress; PrPc

Indexed keywords

METHIONINE SULFOXIDE REDUCTASE; NUCLEAR PROTEIN; PRION PROTEIN;

AGE DISTRIBUTION; AGING; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTIOXIDANT ACTIVITY; ARTICLE; BRAIN BLOOD VESSEL; BRAIN HOMOGENATE; CONTROLLED STUDY; CORRELATION ANALYSIS; ELECTROPHORESIS; HYPEROXIA; IN VIVO STUDY; KNOCKOUT MOUSE; MOUSE; NONHUMAN; OXIDATIVE STRESS; PARENCHYMA; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN GLYCOSYLATION; PROTEIN METABOLISM; UPREGULATION; WESTERN BLOTTING;

AGING; ANIMALS; BLOTTING, WESTERN; BRAIN; BRAIN CHEMISTRY; ELECTROPHORESIS; HYPEROXIA; MALE; MICE; OXIDATIVE STRESS; PROTEIN ISOFORMS; PRPC PROTEINS;

EID: 1942502252     PISSN: 03051846     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2990.2003.00523.x     Document Type: Article

References (28)

1. c. Neuroreport 2000; 11: 3931-6
2. Laine J, Marc ME, Sy MS, Axelrad H. Cellular and subcellular morphological localization of normal prion protein in rodent brain. Eur J Neurosci 2001; 14: 47-56
3. Moya KL, Sales N, Hassig R, Creminon C, Grassi J, Di Giamberardino L. Immunolocalization of the cellular prion protein in normal brain. Microsc Res Tech 2000; 50: 58-65
4. Brown DR, Wong BS, Hafiz F, Clive C, Haswell S, Jones IM. Normal prion protein has superoxide dismutase-like activity. Biochem J 1999; 344: 1-5
5. Mouillet-Richard S, Ermonval M, Chebassier C, Laplanche JL, Lehmann S, Launay JM, Kellermann O. Signal transduction through prion protein. Science 2000; 289: 1925-8
6. Prusiner SB. Prions. Proc Natl Acad Sci USA 1998; 95: 13363-83
7. Harris DA. Cellular biology of prion diseases. Clin Microbiol Rev 1999; 12: 429-44
8. Voigtlander T, Kloppel S, Birner P, Jarius C, Flicker H, Verghese-Nikolakaki S, Sklaviadis T, Guentchev M, Budka H. Marked increase of neuronal prion protein immunoreactivity in Alzheimer's disease and human prion diseases. Acta Neuropathol 2001; 101: 417-23
9. Moskovitz J, Poston M, Berlett B, Nosworthy N, Szcvepanowski R, Stadtman ER. Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity. Proc Natl Acad Sci USA 2000; 95: 14167-72
10. Moskovitz J, Berlett B, Poston M, Stadtman ER. The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc Natl Acad Sci USA 1997; 94: 9585-9
11. Moskovitz J, Flescher E, Berlett S, Azare J, Poston M, Stadtman ER. Overexpression of peptide methionine sulfoxide reductase (MsrA) in Saccaromyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc Natl Acad Sci USA 1998; 95: 14071-5
12. Moskovitz J, Bar-Noy S, Williams WM, Requena J, Berlett BS, Stadtman ER. Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc Nat Acad Sci 2001; 98: 12920-5
13. Gabbita SP, Aksenov MY, Lovell MA, Markesbery WR. Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain. J Neurochem 1999; 73: 1660-6
14. Wong BS, Wang H, Brown DR, Jones IM. Prion disease: a loss of antioxidant function? Biochem Biophys Res Commun 1999; 259: 352-5
15. Williams WM, Reichman M, McNeill TH. Cerebral microvascular and parenchymal phospholipid composition in the mouse. Neurochem Res 1988; 13: 743-7
16. Brown DR. Copper and prion disease. Brain Res Bull 2001; 55: 165-73
17. Wong BS, Pan T, Liu T, Li R, Peterson RB, Jones IM, Gambetti P, Brown DR, Sy M-S. Prion disease: a loss of antioxidant function? Biochem Biophys Res Commun 2000; 275: 249-52
18. Brown DR, Clive C, Haswell S. Antioxidant activity related to copper binding of native prion protein. J Neurochem 2001; 76: 69-76
19. Kellermann O, Lafay-Chebassier C, Ermonval M, Lehmann S, Mouillet-Richard S. From stem cells to prion signaling. C R Acad Sci III 2002; 325: 9-15
20. Satoh J, Kuroda Y, Katamine S. Gene expression profile in prion protein-deficient fibroblasts in culture. Am J Pathol 2000; 157: 59-68
21. Maley F, Trimble RB, Tarentino AL, Plummer TH Jr. Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal Biochem 1989; 180: 195-204
22. Priola SA, Caughey B, Wehrly K, Chesbro B. A 60-kDa prion protein (PrP) with properties of both normal and scrapie-associated forms of PrP*. J Biol Chem 1995; 270: 3299-305
23. Riley ML, Leucht C, Gauczynski S, Hundt C, Brecelj M, Dodson G, Weiss S. High-level expression and characterization of a glycosylated covalently linked dimer of the prion protein. Protein Eng 2002; 15: 529-37
24. c) not observed with recombinant PrP*. J Biol Chem 2000; 275: 38081-7
25. Massimino ML, Griffoni C, Spisni E, Toni M, Tomasi V. Involvement of caveolae and caveolae-like domains in signaling cell survival and angiogenesis. Cell Signal 2002; 14: 93-8
26. Peterson TE, Poppa V, Ueba H, Wu A, Yan C, Berk BC. Opposing effects of reactive oxygen species and cholesterol on endothelial nitric oxide synthase and endothelial cell caveolae. Circ Res 1999; 85: 29-37
27. Bratosiewicz J, Liberski P, Kulczycki J, Kordek R. Codon 129 polymorphism of the PRNP gene in normal Polish population and in Creutzfeldt-Jakob disease, and the search for new mutations in PRNP gene. Acta Neurobiol Exp (Warsz) 2001; 61: 151-6
28. Erginel-Unaltuna N, Peoc'h K, Komurcu E, Acuner T, Issever H, Laplanche J. Distribution of the M129V polymorphism of the prion protein gene in a Turkish population suggests a high risk for Creutzfeldt-Jakob disease. Eur J Hum Genet 2001; 9: 965-8