The possible role of protein X, a putative auxiliary factor in pathological prion replication, in regulating a physiological endoproteolytic cleavage of cellular prion protein

Medical Hypotheses

Volumn 68, Issue 3, 2007, Pages 670-673

  Hachiya, Naomi S ^a   Imagawa, Midori ^a   Kaneko, Kiyotoshi ^a  

^a TOKYO MEDICAL UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CHAPERONE; ISOPROTEIN; PRION PROTEIN; PROTEIN X; PROTEINASE;

ARTICLE; CONFORMATION; HYDROPHOBICITY; MOLECULAR DYNAMICS; PATHOGENESIS; PATHOLOGY; PHYSIOLOGY; PRION; PRION DISEASE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN METABOLISM; PROTEIN STRUCTURE; REGULATORY MECHANISM; TRANSGENICS; VIRUS REPLICATION;

ANIMALS; DNA REPLICATION; HUMANS; MOLECULAR CHAPERONES; NERVE TISSUE PROTEINS; PEPTIDE HYDROLASES; PRIONS;

EID: 33845933773     PISSN: 03069877     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mehy.2006.07.038     Document Type: Article

References (38)

1. Prusiner S.B. Prions Proc Natl Acad Sci USA 95 (1998) 13363-13383
2. Wille H., Michelitsch M.D., Guenebaut V., et al. Structural studies of the scrapie prion protein by electron crystallography. Proc Natl Acad Sci USA 99 (2002) 3563-3568
3. Stahl N., Borchelt D.R., Hsiao K., and Prusiner S.B. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51 (1987) 229-240
4. Caughey B., Race R.E., Ernst D., Buchmeier M.J., and Chesebro B. Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells. J Virol 63 (1989) 175-181
5. Taraboulos A., Scott M., Semenov A., et al. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform. J Cell Biol 129 (1995) 121-132
6. Vey M., Pilkuhn S., Wille H., et al. Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains. Proc Natl Acad Sci USA 93 (1996) 14945-14949
7. Kaneko K., Vey M., Scott M., et al. COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform. Proc Natl Acad Sci USA 94 (1997) 2333-2338
8. Shyng S.L., Heuser J.E., and Harris D.A. A glycolipid-anchored prion protein is endocytosed via clathrin-coated pits. J Cell Biol 125 (1994) 1239-1250
9. Shyng S.L., Moulder K.L., Lesko A., and Harris D.A. The N-terminal domain of a glycolipid-anchored prion protein is essential for its endocytosis via clathrin-coated pits. J Biol Chem 270 (1995) 14793-14800
10. Nunziante M., Gilch S., and Schatzl H.M. Essential role of the prion protein N terminus in subcellular trafficking and half-life of cellular prion protein. J Biol Chem 278 (2003) 3726-3734
11. Lee K.S., Magalhaes A.C., Zanata S.M., et al. Internalization of mammalian fluorescent cellular prion protein and N-terminal deletion mutants in living cells. J Neurochem 79 (2001) 79-87
12. Magalhaes A.C., Silva J.A., Lee K.S., et al. Endocytic intermediates involved with the intracellular trafficking of a fluorescent cellular prion protein. J Biol Chem 277 (2002) 33311-33318
13. Negro A., Ballarin C., Bertoli A., Massimino M.L., and Sorgato M.C. The metabolism and imaging in live cells of the bovine prion protein in its native form or carrying single amino acid substitutions. Mol Cell Neurosci 17 (2001) 521-538
14. Lorenz H., Windl O., and Kretzschmar H.A. Cellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseases. J Biol Chem 277 (2002) 8508-8516
15. Ivanova L., Barmada S., Kummer T., and Harris D.A. Mutant prion proteins are partially retained in the endoplasmic reticulum. J Biol Chem 276 (2001) 42409-42421
16. Hachiya N.S., Watanabe K., Sakasegawa Y., and Kaneko K. Microtubules-associated intracellular localization of the NH(2)-terminal cellular prion protein fragment. Biochem Biophys Res Commun 313 (2004) 818-823
17. Hachiya N.S., Watanabe K., Yamada M., Sakasegawa Y., and Kaneko K. Anterograde and retrograde intracellular trafficking of fluorescent cellular prion protein. Biochem Biophys Res Commun 315 (2004) 802-807
18. Rogers M., Serban D., Gyuris T., et al. Epitope mapping of the Syrian hamster prion protein utilizing chimeric and mutant genes in a vaccinia virus expression system. J Immunol 147 (1991) 3568-3574
19. Pan K.M., Stahl N., and Prusiner S.B. Purification and properties of the cellular prion protein from Syrian hamster brain. Protein Sci 1 (1992) 1343-1352
20. Harris D.A., Huber M.T., van Dijken P., et al. Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites. Biochemistry 32 (1993) 1009-10016
21. Chen S.G., Teplow D.B., Parchi P., et al. Truncated forms of the human prion protein in normal brain and in prion diseases. J Biol Chem 270 (1995) 19173-19180
22. Jimenez-Huete A., Lievens P.M., Vidal R., et al. Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues. Am J Pathol 153 (1998) 1561-1572
23. Vincent B., Paitel E., Frobert Y., et al. Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons. J Biol Chem 275 (2000) 35612-35616
24. Vincent B., Paitel E., Saftig P., et al. The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J Biol Chem 276 (2001) 37743-37746
25. Donne D.G., Viles J.H., Groth D., et al. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc Natl Acad Sci USA 94 (1997) 13452-13457
26. James T.L., Liu H., Ulyanov N.B., et al. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc Natl Acad Sci USA 94 (1997) 10086-10091
27. Zahn R., Liu A., Luhrs T., et al. NMR solution structure of the human prion protein. Proc Natl Acad Sci USA 97 (2000) 145-150
28. Knaus K.J., Morillas M., Swietnicki W., et al. Crystal structure of the human prion protein reveals a mechanism for oligomerization. Nat Struct Biol 8 (2001) 770-774
29. Haire L.F., Whyte S.M., Vasisht N., et al. The crystal structure of the globular domain of sheep prion protein. J Mol Biol 336 (2004) 1175-1183
30. Pillot T., Lins L., Goethals M., et al. The 118-135 peptide of the human prion protein forms amyloid fibrils and induces liposome fusion. J Mol Biol 274 (1997) 381-393
31. Jobling M.F., Stewart L.R., White A.R., et al. The hydrophobic core sequence modulates the neurotoxic and secondary structure properties of the prion peptide 106-126. J Neurochem 73 (1999) 1557-1565
32. Saez-Cirion A., Nieva J.L., and Gallaher W.R. The hydrophobic internal region of bovine prion protein shares structural and functional properties with HIV type 1 fusion peptide. AIDS Res Hum Retroviruses 19 (2003) 969-978
33. Kaneko K., and Hachiya N.S. The alternative role of 14-3-3 zeta as a sweeper of misfolded proteins in disease conditions. Med Hypotheses 67 (2006) 169-171
34. Telling G.C., Scott M., Mastrianni J., et al. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83 (1995) 79-90
35. Kaneko K., Zulianello L., Scott M., et al. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc Natl Acad Sci USA 94 (1997) 10069-10074
36. Cohen F.E., and Prusiner S.B. Pathologic conformations of prion proteins. Annu Rev Biochem 67 (1998) 793-819
37. Prusiner S.B., Scott M.R., DeArmond S.J., and Cohen F.E. Prion protein biology. Cell 93 (1998) 337-348
38. +]. Science 268 (1995) 880-884