1887

Abstract

In Creutzfeldt–Jakob disease (CJD), the type (type 1 or 2) of abnormal isoform of the prion protein (PrP) in the brain and the genotype at codon 129 of the PrP gene are major determinants of clinicopathological phenotype. Little is known about the difference in biochemical properties between the two types of PrP, except for the different proteinase K cleavage sites. To investigate the size of aggregates formed by PrP types 1 and 2, brain homogenates from various cases of CJD with the same genotype (homozygous for methionine at codon 129) were passed through filters with a mean pore size of 72±4 nm. Type 2 PrP was efficiently removed from the filtrates by the filters, in contrast to type 1. Even type 2 PrP from a patient without amyloid plaques was removed more efficiently than type 1 from patients with amyloid plaques. These results indicate that type 2 PrP has a larger aggregation size than type 1, irrespective of the existence of amyloid plaques.

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2005-01-01
2019-11-12
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References

  1. Bockman, J. M., Kingsbury, D. T., McKinley, M. P., Bendheim, P. E. & Prusiner, S. B. ( 1985; ). Creutzfeldt–Jakob disease prion proteins in human brains. N Engl J Med 312, 73–78.[CrossRef]
    [Google Scholar]
  2. Collinge, J., Sidle, K. C., Meads, J., Ironside, J. & Hill, A. F. ( 1996; ). Molecular analysis of prion strain variation and the aetiology of ‘new variant’ CJD. Nature 383, 685–690.[CrossRef]
    [Google Scholar]
  3. Kitamoto, T., Shin, R.-W., Doh-ura, K., Tomokane, N., Miyazono, M., Muramoto, T. & Tateishi, J. ( 1992; ). Abnormal isoform of prion proteins accumulates in the synaptic structures of the central nervous system in patients with Creutzfeldt–Jakob disease. Am J Pathol 140, 1285–1294.
    [Google Scholar]
  4. Kitamoto, T., Ohta, M., Doh-ura, K., Hitoshi, S., Terao, Y. & Tateishi, J. ( 1993; ). Novel missense variants of prion protein in Creutzfeldt–Jakob disease or Gerstmann–Sträussler syndrome. Biochem Biophys Res Commun 191, 709–714.[CrossRef]
    [Google Scholar]
  5. Parchi, P., Castellani, R., Capellari, S. & 9 other authors ( 1996; ). Molecular basis of phenotypic variability in sporadic Creutzfeldt–Jakob disease. Ann Neurol 39, 767–778.[CrossRef]
    [Google Scholar]
  6. Parchi, P., Capellari, S., Chen, S. G. & 8 other authors ( 1997; ). Typing prion isoforms. Nature 386, 232–234.[CrossRef]
    [Google Scholar]
  7. Parchi, P., Giese, A., Capellari, S. & 15 other authors ( 1999; ). Classification of sporadic Creutzfeldt–Jakob disease based on molecular and phenotypic analysis of 300 subjects. Ann Neurol 46, 224–233.[CrossRef]
    [Google Scholar]
  8. Parchi, P., Zou, W., Wang, W. & 10 other authors ( 2000; ). Genetic influence on the structural variations of the abnormal prion protein. Proc Natl Acad Sci U S A 97, 10168–10172.[CrossRef]
    [Google Scholar]
  9. Prusiner, S. B., McKinley, M. P., Bowman, K. A., Bolton, D. C., Bendheim, P. E., Groth, D. F. & Glenner, G. G. ( 1983; ). Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35, 349–358.[CrossRef]
    [Google Scholar]
  10. Prusiner, S. B., Scott, M. R., DeArmond, S. J. & Cohen, F. E. ( 1998; ). Prion protein biology. Cell 93, 337–348.[CrossRef]
    [Google Scholar]
  11. Puoti, G., Giaccone, G., Rossi, G., Canciani, B., Bugiani, O. & Tagliavini, F. ( 1999; ). Sporadic Creutzfeldt–Jakob disease: co-occurrence of different types of PrPSc in the same brain. Neurology 53, 2173–2176.[CrossRef]
    [Google Scholar]
  12. Satoh, K., Muramoto, T., Tanaka, T. & 7 other authors ( 2003; ). Association of an 11–12 kDa protease-resistant prion protein fragment with subtypes of dura graft-associated Creutzfeldt–Jakob disease and other prion diseases. J Gen Virol 84, 2885–2893.[CrossRef]
    [Google Scholar]
  13. Taguchi, Y., Mohri, S., Ironside, J. W., Muramoto, T. & Kitamoto, T. ( 2003; ). Humanized knock-in mice expressing chimeric prion protein showed varied susceptibility to different human prions. Am J Pathol 163, 2585–2593.[CrossRef]
    [Google Scholar]
  14. Tateishi, J., Kitamoto, T., Ishikawa, G. & Manabe, S. ( 1993; ). Removal of causative agent of Creutzfeldt–Jakob disease (CJD) through membrane filtration method. Membrane 18, 357–362.[CrossRef]
    [Google Scholar]
  15. Tateishi, J., Kitamoto, T., Ishikawa, G., Manabe, S. & Yamaguchi, K. ( 1995; ). Removal of the prion protein using validatable filter (BMM®). In Animal Cell Technology: Development Towards the 21st Century, pp. 637–640. Edited by E. C. Beuvery, J. B. Griffiths & W. P. Zeijlemaker. Dordrecht: Kluwer Academic Publishers.
  16. Tateishi, J., Kitamoto, T., Mohri, S., Satoh, S., Sato, T., Shepherd, A. & Macnaughton, M. R. ( 2001; ). Scrapie removal using Planova® virus removal filters. Biologicals 29, 17–25.[CrossRef]
    [Google Scholar]
  17. Tzaban, S., Friedlander, G., Schonberger, O., Horonchik, L., Yedidia, Y., Shaked, G., Gabizon, R. & Taraboulos, A. ( 2002; ). Protease-sensitive scrapie prion protein in aggregates of heterogeneous sizes. Biochemistry 41, 12868–12875.[CrossRef]
    [Google Scholar]
  18. Van Holten, R. W., Autenrieth, S., Boose, J. A., Hsieh, W.-T. & Dolan, S. ( 2002; ). Removal of prion challenge from an immune globulin preparation by use of a size-exclusion filter. Transfusion 42, 999–1004.[CrossRef]
    [Google Scholar]
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