1887

Abstract

Creutzfeldt–Jakob disease can develop in subjects given a cadaveric dura mater graft (dCJD). This disease has a phenotypic heterogeneity despite the lack of genetic variation. Numerous plaque-type prion protein (PrP) deposits are found in the brain of some but not all subjects; hence, there may be two subtypes of this clinical entity. To validate dCJD subtypes further, we carried out a larger-scale clinicopathological analysis and typing of protease-resistant PrP (PrP) in dCJD cases. Cases with plaque-type PrP deposits (p-dCJD) were shown to be distinct from those without PrP plaques (np-dCJD), from several clinicopathological aspects. Analysis of PrP revealed that, while the major PrP species from both subtypes was of 21 kDa after deglycosylation (type 1 PrP), a C-terminal PrP fragment of 11–12 kDa (fPrP11–12) was associated with np-dCJD but not with p-dCJD. The disease type-specific association of fPrP11–12 was also observed in subjects with other prion diseases. An fPrP11–12-like C-terminal PrP fragment was detected in brain lysates from patients associated with fPrP11–12, but not from patients or normal subjects unassociated with fPrP11–12. Results indicated that fPrP was produced by CJD-associated processes . The present data provide several lines of evidence that support the need for subtyping of dCJD and contribute to the understanding of the processing of disease-specific PrP species. The unique relationship of fPrP11–12 with CJD phenotype supports the view that the phenotypic heterogeneity of CJD is related to the formation of different types of disease-specific PrP and fragments thereof.

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2003-10-01
2020-07-14
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References

  1. Brown P., Preece M., Brandel J. P.. 12 other authors 2000; Iatrogenic Creutzfeldt–Jakob disease at the millennium. Neurology55:1075–1081
    [Google Scholar]
  2. Capellari S., Parchi P., Russo C. M., Sanford J., Sy M.-S., Gambetti P., Petersen R. B.. 2000; Effect of the E200K mutation on prion protein metabolism: comparative study of a cell model and human brain. Am J Pathol157:613–622
    [Google Scholar]
  3. Chen S. G., Teplow D. B., Parchi P., Teller J. K., Gambetti P., Autilio-Gambetti L.. 1995; Truncated forms of the human prion protein in normal brain and in prion diseases. J Biol Chem270:19173–19180
    [Google Scholar]
  4. Collinge J., Sidle K. C. L., Meads J., Ironside J., Hill A. F.. 1996; Molecular analysis of prion strain variation and the aetiology of ‘new variant’ CJD. Nature383:685–690
    [Google Scholar]
  5. de Silva R., Ironside J. W., McCardle L.. 7 other authors 1994; Neuropathological phenotype and prion protein genotype: correlation in sporadic Creutzfeldt–Jakob disease. Neurosci Lett179:50–52
    [Google Scholar]
  6. Doh-ura K., Kitamoto T., Sakaki Y., Tateishi J.. 1991; CJD discrepancy. Nature353:801–802
    [Google Scholar]
  7. Fischer M., Rülicke T., Raeber A., Sailer A., Moser M., Oesch B., Brandner S., Aguzzi A., Weissmann C.. 1996; Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J15:1255–1264
    [Google Scholar]
  8. Hoshi K., Yoshino H., Urata J., Nakamura Y., Yanagawa H., Sato T.. 2000; Creutzfeldt–Jakob disease associated with cadaveric dura mater grafts in Japan. Neurology55:718–721
    [Google Scholar]
  9. Kascsak R. J., Rubenstein R., Merz P. A., Tonna-DeMasi M., Fersko R., Carp R. I., Wisniewski H. M., Diringer H.. 1987; Mouse polyclonal and monoclonal antibody to scrapie-associated fibril protein. J Virol61:3688–3693
    [Google Scholar]
  10. Kimura K., Nonaka A., Tashiro H., Yaginuma M., Shimokawa R., Okeda R., Yamada M.. 2001; Atypical form of dural graft associated Creutzfeldt–Jakob disease: report of a postmortem case with review of the literature. J Neurol Neurosurg Psychiatry70:696–699
    [Google Scholar]
  11. Kitamoto T., Tateishi J.. 1994; Human prion diseases with variant prion protein. Philos Trans R Soc Lond Ser B Biol Sci343:391–398
    [Google Scholar]
  12. Kitamoto T., Shin R.-W., Doh-ura K., Tomokane N., Miyazono M., Muramoto T., Tateishi J.. 1992; Abnormal isoform of prion protein accumulates in the synaptic structures of the central nervous system in patients with Creutzfeldt–Jakob disease. Am J Pathol140:1285–1294
    [Google Scholar]
  13. Kitamoto T., Mohri S., Ironside J. W.. 9 other authors 2002; Follicular dendritic cell of the knock-in mouse provides a new bioassay for human prions. Biochem Biophys Res Commun294:280–286
    [Google Scholar]
  14. Kopp N., Streichenberger N., Deslys J. P., Laplanche J. L., Chazot G.. 1996; Creutzfeldt–Jakob disease in a 52-year-old woman with florid plaques. Lancet348:1239–1240
    [Google Scholar]
  15. Lane K. L., Brown P., Howell D. N., Crain B. J., Hulette C. M., Burger P. C., DeArmond S. J.. 1994; Creutzfeldt–Jakob disease in a pregnant woman with an implanted dura mater graft. Neurosurgery34:737–739
    [Google Scholar]
  16. Lang C. J. G., Heckmann J. G., Neundörfer B.. 1998; Creutzfeldt–Jakob disease via dural and corneal transplants. J Neurol Sci160:128–139
    [Google Scholar]
  17. Martin J. J.. 1975; Thalamic degenerations. In Handbook of Clinical Neurology vol 21 pp 587–604 Edited by Vinken P. J., Bruyn G. W.. Amsterdam: North-Holland;
    [Google Scholar]
  18. Miyashita K., Inuzuka T., Kondo H.. 7 other authors 1991; Creutzfeldt–Jakob disease in a patient with a cadaveric dural graft. Neurology41:940–941
    [Google Scholar]
  19. Miyazono M., Kitamoto T., Doh-ura K., Iwaki T., Tateishi J.. 1992; Creutzfeldt–Jakob disease with codon 129 polymorphism (valine): a comparative study of patients with codon 102 point mutation or without mutations. Acta Neuropathol84:349–354
    [Google Scholar]
  20. Muramoto T., Tanaka T., Kitamoto N., Sano C., Hayashi Y., Kutomi T., Yutani C., Kitamoto T.. 2000; Analyses of Gerstmann–Straussler syndrome with 102Leu219Lys using monoclonal antibodies that specifically detect human prion protein with 219Glu. Neurosci Lett288:179–182
    [Google Scholar]
  21. Parchi P., Castellani R., Capellari S.. 9 other authors 1996; Molecular basis of phenotypic variability in sporadic Creutzfeldt–Jakob disease. Ann Neurol39:767–778
    [Google Scholar]
  22. Parchi P., Capellari S., Chen S. G.. 8 other authors 1997; Typing prion isoforms. Nature386:232–234
    [Google Scholar]
  23. Parchi P., Chen S. G., Brown P.. 9 other authors 1998; Different patterns of truncated prion protein fragments correlate with distinct phenotypes in P102L Gerstmann–Sträussler–Scheinker disease. Proc Natl Acad Sci U S A95:8322–8327
    [Google Scholar]
  24. 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 Neurol46:224–233
    [Google Scholar]
  25. 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 A97:10168–10172
    [Google Scholar]
  26. Radbauer C., Hainfellner J. A., Gaudernak T., Deecke L., Budka H.. 1998; Creutzfeldt–Jakob disease in a dura transplant recipient: first observation in Austria. Wien Klin Wochenschr110:496–500
    [Google Scholar]
  27. Shimizu S., Hoshi K., Muramoto T., Homma M., Ironside J., Kuzuhara S., Sato T., Yamamoto T., Kitamoto T.. 1999; Creutzfeldt–Jakob disease with florid-type plaques after cadaveric dura mater grafting. Arch Neurol56:357–362
    [Google Scholar]
  28. Shmerling D., Hegyi I., Fischer M.. 10 other authors 1998; Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell93:203–214
    [Google Scholar]
  29. Supattapone S., Muramoto T., Legname G., Mehlhorn I., Cohen F. E., DeArmond S. J., Prusiner S. B., Scott M. R.. 2001; Identification of two prion protein regions that modify scrapie incubation time. J Virol75:1408–1413
    [Google Scholar]
  30. Tagliavini F., Prelli F., Ghiso J., Bugiani O., Serban D., Prusiner S. B., Farlow M. R., Ghetti B., Frangione B.. 1991; Amyloid protein of Gerstmann–Sträussler–Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58. EMBO J10:513–519
    [Google Scholar]
  31. Tagliavini F., Lievens P. M.-J., Tranchant C.. 12 other authors 2001; A 7-kDa prion protein (PrP) fragment, an integral component of the PrP region required for infectivity, is the major amyloid protein in Gerstmann–Sträussler–Scheinker disease A117V. J Biol Chem276:6009–6015
    [Google Scholar]
  32. Takahashi S., Tateishi J., Taguchi Y., Hirade S., Inoue H., Matsui Y., Furukawa H.. 1997; Creutzfeldt–Jakob disease with a widespread presence of kuru-type plaques after cadaveric dural graft replacement: an autopsy case. Rinsho Shinkeigaku37:824–828 (in Japanese
    [Google Scholar]
  33. Takashima S., Tateishi J., Taguchi Y., Inoue H.. 1997; Creutzfeldt–Jakob disease with florid plaques after cadaveric dural graft in a Japanese woman. Lancet350:865–866
    [Google Scholar]
  34. Thadani V., Penar P. L., Partington J., Kalb R., Janssen R., Schonberger L. B., Rabkin C. S., Prichard J. W.. 1988; Creutzfeldt–Jakob disease probably acquired from a cadaveric dura mater graft. J Neurosurg69:766–769
    [Google Scholar]
  35. Yamada S., Aiba T., Endo Y., Hara M., Kitamoto T., Tateishi J.. 1994; Creutzfeldt–Jakob disease transmitted by a cadaveric dura mater graft. Neurosurgery34:740–743
    [Google Scholar]
  36. Yamada M., Itoh Y., Suematsu N., Matsushita M., Otomo E.. 1997; Panencephalopathic type of Creutzfeldt–Jakob disease associated with cadaveric dura mater graft. J Neurol Neurosurg Psychiatry63:524–527
    [Google Scholar]
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