Cellular prion protein (PrPC) of the neuron cell transformed to a PK-resistant protein under oxidative stress, comprising main mitochondrial damage in prion diseases

Journal of Molecular Neuroscience

Volumn 51, Issue 1, 2013, Pages 219-224

  Yuan, Fangzhong ^a   Yang, Lifeng ^a   Zhang, Zhuming ^a   Wu, Wenyu ^a   Zhou, Xiangmei ^a   Yin, Xiaomin ^a   Zhao, Deming ^a  

^a CHINA AGRICULTURAL UNIVERSITY   (China)

Author keywords

Iron; Mitochondria; Oxidative stress; PMCA; Prion; ROS

Indexed keywords

PRION PROTEIN;

ARTICLE; BRAIN MITOCHONDRION; CELL DAMAGE; DISEASE COURSE; ENZYME CONFORMATION; NERVE CELL; OXIDATIVE STRESS; PRION DISEASE; PROTEIN FOLDING; PROTEIN MISFOLDING;

CELL LINE, TUMOR; ENDOPEPTIDASE K; HUMANS; IRON; MITOCHONDRIA; NEURONS; OXIDATIVE STRESS; PEPTIDE FRAGMENTS; PRION DISEASES; PRIONS; PROTEIN FOLDING;

EID: 84882261910     PISSN: 08958696     EISSN: 15591166     Source Type: Journal    
DOI: 10.1007/s12031-013-0008-6     Document Type: Article

References (20)

1. Sc. J Mol Biol 346(2):645-659
2. res propagation as an early primary pathogenic event in prion disease. Brain Res Bull 68(5):346-354
3. Castilla J, Saá P, Morales R, Abid K, Maundrell K, Soto C (2006) Protein misfolding cyclic amplification for diagnosis and prion propagation studies. Method Enzymol 412:3-21
4. Chen B, Morales R, Barria MA, Soto C (2010) Estimating prion concentration in fluids and tissues by quantitative PMCA. Nat methods 7(7):519-520
5. Choi CJ, Kanthasamy A, Anantharam V, Kanthasamy AG (2006) Interaction of metals with prion protein: possible role of divalent cations in the pathogenesis of prion diseases. NeuroToxicology 27(5):777-787
6. + pumping as a link in aging/disease vicious cycle. Int J Biochem Cell Biol 40(9):1792-1805
7. Fioriti L, Quaglio E, Massignan T, Colombo L, Stewart RS, Salmona M, Harris DA, Forloni G, Chiesa R (2005) The neurotoxicity of prion protein (PrP) peptide 106-126 is independent of the expression level of PrP and is not mediated by abnormal PrP species. Mol Cell Neurosci 28(1):165-176
8. Haigh CL, McGlade AR, Lewis V, Masters CL, Lawson VA, Collins SJ (2011) Acute exposure to prion infection induces transient oxidative stress progressing to be cumulatively deleterious with chronic propagation in vitro. Free Radical Bio Med 51:594-608
9. Kim NH, Park SJ, Jin JK, Kwon MS, Choi EK, Carp RI, Kim YS (2000) Increased ferric iron content and iron-induced oxidative stress in the brains of scrapie-infected mice. Brain Res 884(1-2):98-103
10. Kozlowski H, Janicka-Klos A, Brasun J, Gaggelli E, Valensin D, Valensin G (2009) Copper, iron, and zinc ions homeostasis and their role in neurodegenerative disorders (metal uptake, transport, distribution and regulation). Coordin Chem Rev 253(21):2665-2685
11. Ma J, Lindquist S (1999) De novo generation of a PrPSc-like conformation in living cells. Nat Cell Biol 1(6):358-361
12. Milhavet O, Lehmann S (2002) Oxidative stress and the prion protein in transmissible spongiform encephalopathies. Brain Res Rev 38(3):328-339
13. Panza G, Stöhr J, Dumpitak C, Papathanassiou D, Weiß J, Riesner D, Willbold D, Birkmann E (2008) Spontaneous and BSE-prion-seeded amyloid formation of full length recombinant bovine prion protein. Biochem Bioph Res Co 373(4):493-497
14. Prusiner SB (1982) Novel proteinaceous infectious particles cause scrapie. Science 216(4542):136-144
15. Saá P, Castilla J, Soto C (2005) Cyclic amplification of protein misfolding and aggregation. Methods Mol Biol 299:53-65
16. Saretzki G (2009) Telomerase, mitochondria and oxidative stress. Exp Gerontol 44(8):485-492
17. Seo JS, Seol JW, Moon MH, Jeong JK, Lee YJ, Park SY (2010) Hypoxia protects neuronal cells from human prion protein fragment-induced apoptosis. J Neurochem 112(3):715-722
18. Sun K, Johnson BS, Gunn TM (2007) Mitochondrial dysfunction precedes neurodegeneration in mahogunin (Mgrn1) mutant mice. Neurobiol Aging 28(12):1840-1852
19. Valente EM, Abou-Sleiman PM, Caputo V, Muqit MMK, Harvey K, Gispert S, Ali Z, Del Turco D, Bentivoglio AR, Healy DG (2004) Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304(5674):1158-1160
20. Zheng W, Wang L, Hong Y, Sha Y (2009) PrP106-126 peptide disrupts lipid membranes: influence of C-terminal amidation. Biochem Bioph Res Co 379(2):298-303