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Redox metals and oxidative abnormalities in human prion diseases.
Acta Neuropathol. 2005 Sep; 110(3):232-8.AN

Abstract

Prion diseases are characterized by the accumulation of diffuse and aggregated plaques of protease-resistant prion protein (PrP) in the brains of affected individuals and animals. Whereas prion diseases in animals appear to be almost exclusively transmitted by infection, human prion diseases most often occur sporadically and, to a lesser extent, by inheritance or infection. In the sporadic cases (sporadic Creutzfeld-Jakob disease, sCJD), PrP-containing plaques are infrequent, whereas in transmitted (variant CJD) and inherited (Gerstmann-Straussler-Scheinker Syndrome) cases, plaques are a usual feature. In the current study, representative cases from each of the classes of human prion disease were analyzed for the presence of markers of oxidative damage that have been found in other neurodegenerative diseases. Interestingly, we found that the pattern of deposition of PrP, amyloid-beta, and redox active metals was distinct for the various prion diseases. Whereas 8-hydroxyguanosine has been shown to be increased in sCJD, and inducible NOS is increased in scrapie-infected mice, well-studied markers of oxidative damage that accumulate in the lesions of other neurodegenerative diseases (such as Alzheimer's disease, progressive supranuclear palsy, and Parkinson's disease), such as heme oxygenase-1 and lipid peroxidation, were not found around PrP deposits or in vulnerable neurons. These findings suggest an important distinction in prion-related oxidative stress, indicating that different neurodegenerative pathways are involved in different prion diseases.

Authors+Show Affiliations

Institute of Pathology, Case Western Reserve University, 2085 Adelbert Road, Cleveland, OH 44106, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

16096758

Citation

Petersen, Robert B., et al. "Redox Metals and Oxidative Abnormalities in Human Prion Diseases." Acta Neuropathologica, vol. 110, no. 3, 2005, pp. 232-8.
Petersen RB, Siedlak SL, Lee HG, et al. Redox metals and oxidative abnormalities in human prion diseases. Acta Neuropathol. 2005;110(3):232-8.
Petersen, R. B., Siedlak, S. L., Lee, H. G., Kim, Y. S., Nunomura, A., Tagliavini, F., Ghetti, B., Cras, P., Moreira, P. I., Castellani, R. J., Guentchev, M., Budka, H., Ironside, J. W., Gambetti, P., Smith, M. A., & Perry, G. (2005). Redox metals and oxidative abnormalities in human prion diseases. Acta Neuropathologica, 110(3), 232-8.
Petersen RB, et al. Redox Metals and Oxidative Abnormalities in Human Prion Diseases. Acta Neuropathol. 2005;110(3):232-8. PubMed PMID: 16096758.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Redox metals and oxidative abnormalities in human prion diseases. AU - Petersen,Robert B, AU - Siedlak,Sandra L, AU - Lee,Hyoung-gon, AU - Kim,Yong-Sun, AU - Nunomura,Akihiko, AU - Tagliavini,Fabrizio, AU - Ghetti,Bernardino, AU - Cras,Patrick, AU - Moreira,Paula I, AU - Castellani,Rudy J, AU - Guentchev,Marin, AU - Budka,Herbert, AU - Ironside,James W, AU - Gambetti,Pierluigi, AU - Smith,Mark A, AU - Perry,George, Y1 - 2005/08/11/ PY - 2005/03/01/received PY - 2005/04/18/accepted PY - 2005/04/18/revised PY - 2005/8/13/pubmed PY - 2007/12/8/medline PY - 2005/8/13/entrez SP - 232 EP - 8 JF - Acta neuropathologica JO - Acta Neuropathol. VL - 110 IS - 3 N2 - Prion diseases are characterized by the accumulation of diffuse and aggregated plaques of protease-resistant prion protein (PrP) in the brains of affected individuals and animals. Whereas prion diseases in animals appear to be almost exclusively transmitted by infection, human prion diseases most often occur sporadically and, to a lesser extent, by inheritance or infection. In the sporadic cases (sporadic Creutzfeld-Jakob disease, sCJD), PrP-containing plaques are infrequent, whereas in transmitted (variant CJD) and inherited (Gerstmann-Straussler-Scheinker Syndrome) cases, plaques are a usual feature. In the current study, representative cases from each of the classes of human prion disease were analyzed for the presence of markers of oxidative damage that have been found in other neurodegenerative diseases. Interestingly, we found that the pattern of deposition of PrP, amyloid-beta, and redox active metals was distinct for the various prion diseases. Whereas 8-hydroxyguanosine has been shown to be increased in sCJD, and inducible NOS is increased in scrapie-infected mice, well-studied markers of oxidative damage that accumulate in the lesions of other neurodegenerative diseases (such as Alzheimer's disease, progressive supranuclear palsy, and Parkinson's disease), such as heme oxygenase-1 and lipid peroxidation, were not found around PrP deposits or in vulnerable neurons. These findings suggest an important distinction in prion-related oxidative stress, indicating that different neurodegenerative pathways are involved in different prion diseases. SN - 0001-6322 UR - https://www.unboundmedicine.com/medline/citation/16096758/Redox_metals_and_oxidative_abnormalities_in_human_prion_diseases_ L2 - https://dx.doi.org/10.1007/s00401-005-1034-4 DB - PRIME DP - Unbound Medicine ER -