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Evidence for oxidative damage to prion protein in prion diseases

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Chinese Science Bulletin

Abstract

In prion diseases the irreversible protein structural transformation process is completed in the brains of mammals within a few months, the uniformly generated infectivity displays extraordinary resistance to inactivation, suggesting that a vital energy source is required for the production of infectious particles. Considering the high oxygen-respiration rate in the brains, prion protein oxidative damage can be the crucial factor. Both theoretical consideration of the nature of protein radical reactions and a large body of previously unraveled feature of scrapie and prion diseases have provided multiple distinct lines of compelling evidence which persuasively support a suggestion that the infectious agents may be prion (free) radicals produced from protein oxidative damage. This paper describes that scrapie prions are most likely formed from prion radicals and oxidative species-mediated sequence-specific cross-linking of benign prion proteins.

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Authors and Affiliations

  1. Institute for Life Science and Health at UCSD, P. O. Box 12035, 92039, La Jolla, CA, USA

    Chiming Yang

  2. Shanghai JiaoTong University, College of Life Science & Biotechnology, 200030, Shanghai, China

    Chiming Yang

  3. Nankai University, College of Chemistry, 300071, Tianjin, China

    Chiming Yang

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Correspondence to Chiming Yang.

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Yang, C. Evidence for oxidative damage to prion protein in prion diseases. Chin.Sci.Bull. 45, 1546–1554 (2000). https://doi.org/10.1007/BF02886210

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  • DOI: https://doi.org/10.1007/BF02886210

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