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DOI: 10.1055/s-2002-19641
Intestinal Entry of Prions
Prioneneintritt über den DünndarmPublikationsverlauf
4.10.2001
4.10.2001
Publikationsdatum:
21. Januar 2002 (online)
Abstract
Variant Creutzfeldt-Jakob disease is thought to be caused by infected prion protein via ingestion of contaminated beef. After ingestion of infected prion proteins, uptake by small intestine may be by either M-cell dependent or M-cell independent routes. A receptor for prion protein, laminin receptor precursor is expressed on the brush border of small intestinal epithelium in 40 % of subjects. The cellular prion protein expressed on the enteric nervous system might serve as the target for conversion to infectious prion protein and a route for spread to the central nervous system.
Zusammenfassung
Eine Variante der Creutzfeldt-Jakob-Krankheit soll über die Aufnahme kontaminierten Rindfleischs durch infektiöses Prionenprotein hervorgerufen werden. Nach dem Verzehr können die Prionenproteine im Dünndarm durch Vermittlung der M-Zellen oder unabhängig davon aufgenommen werden. Bei 40 % aller Menschen wird am Bürstensaum des Dünndarmepithels ein Rezeptor für Prionenproteine, der Lamininrezeptor, exprimiert. Das im enterischen Nervensystem exprimierte zelluläre Prionenprotein könnte als Ziel für die Umwandlung in infektiöses Protein dienen und den Weg zur Ausbreitung ins Zentralnervensystem darstellen.
Key words
Prions - Variant CJD - Laminin Receptor Protein - Small Intestine
Schlüsselwörter
Prionen - CJD-Variante - Laminin-Rezeptorprotein - Dünndarm
References
- 1 Prusiner S B. Novel proteinaceous infectious particles cause scrapie. Science. 1982; 216 136-144
- 2 Prusiner S B. Prions. Proc Natl Acad Sci. 1998; 95 13 363-13 383
- 3 Prusiner S B. Molecular biology of prion diseases. Science. 1991; 252 1515-1522
- 4 Harris D A. Cellular biology of prion diseases. Clin Microbiol Rev. 1999; 12 429-444
- 5 Pan K M, Baldwin M, Nguyen J . et al . Conversion of alpha-helices into β-sheets features in the formation of scrapie prion proteins. Proc Natl Acad Sci. 1993; 90 10 962-10 966
- 6 Will R G, Ironside J W, Zeidler M . et al . A new-variant of Creutzfeldt- Jakob disease in the UK. Lancet. 1996; 347 921-925
- 7 Collee J G, Bradley R. BSE: A decade on-part I. Lancet. 1997; 349 636-641
- 8 Ghani A C, Ferguson N M, Donnelly C A, Anderson R M. Predicted vCJD mortality in Great Britain. Nature. 2000; 406 583-584
- 9 Cousens S, Smith P G, Ward H . et al . Geographical distribution of variant Creutzfeldt-Jakob disease in Great Britain, 1996-2000. Lancet. 2001; 357 1002-1007
- 10 Cohen F E, Prusiner S B. Pathologic conformations of prion proteins. Ann Rev Biochem. 1998; 67 793-819
- 11 Beekes M, McBride P A. Early accumulation of pathological PrP in the enteric nervous system and gut-associated lymphoid tissue of hamsters orally infected with scrapie. Neurosci Lett. 2000; 278 181-184
- 12 Rieger R, Edenhofer F, Lasmezas C I, Weiss S. The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nat Med. 1997; 3 1383-1388
- 13 Shmakov A N, Bode J, Kilshaw P J, Ghosh S. Diverse patterns of expression of the 67-kD laminin receptor in human small intestinal mucosa: Potential binding sites for prion proteins. J Pathol. 2000; 191 318-322
- 14 Shmakov A N, McLennan N F, McBride P . et al . Cellular prion protein is expressed in the human enteric nervous system. Nat Med. 2000; 6 840-841
- 15 Wadsworth J DF, Joiner S, Hill A F . et al . Tissue distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunoblotting assay. Lancet. 2001; 358 171-180
- 16 Ironside J W, Head M W, Bell J E, McCardle L, Will R G. Laboratory diagnosis of variant Creutzfeldt-Jakob disease. Histopathology. 2000; 37 1-9
- 17 Hilton D A, Fathers E, Edwards P, Ironside J W, Zajicek J. Prion immunoreactivity in appendix before clinical onset of variant Creutzfeldt-Jakob disease. Lancet. 1998; 352 703-704
- 18 Bruce M E, McConnell I, Will R G, Ironside J W. Detection of variant Creutzfeldt-Jakob disease infectivity in extraneural tissues. Lancet. 2001; 358 208-209
Prof. S. Ghosh
Gastroenterology Section, Imperial College School of
Medicine
Hammersmith Campus
London W12 0NN
eMail: s.ghosh@ic.ac.uk