Subtyping of human cellular prion proteins and their differential solubility

Experimental Neurology

Volumn 227, Issue 1, 2011, Pages 188-194

  Kuczius, Thorsten ^a   Wohlers, Janet ^a   Karch, Helge ^a   Groschup, Martin H ^b  

^a UNIVERSITY HOSPITAL MÜNSTER   (Germany)

^b FEDERAL RESEARCH INSTITUTE FOR ANIMAL HEALTH   (Germany)

Author keywords

Detergent; Heterogeneous cellular prion proteins; Protein solubility; Solvent; Subtyping

Indexed keywords

3 [(3 CHOLAMIDOPROPYL)DIMETHYLAMMONIO] 1 PROPANESULFONIC ACID; DODECYL SULFATE SODIUM; OCTYL GLUCOSIDE; PRION PROTEIN; TRITON X 100;

ARTICLE; CONTROLLED STUDY; HUMAN; HUMAN TISSUE; PRION DISEASE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN GLYCOSYLATION; SOLUBILITY;

BRAIN; DETERGENTS; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; PHOSPHOPYRUVATE HYDRATASE; PRIONS; PROTEIN FOLDING; PROTEIN ISOFORMS; SOLUBILITY;

EID: 78650946173     PISSN: 00144886     EISSN: 10902430     Source Type: Journal    
DOI: 10.1016/j.expneurol.2010.10.014     Document Type: Article

References (37)

1. Arnold T., Linke D. The use of detergents to purify membrane proteins. Curr. Protoc. Protein Sci. 2008, Supplement 53, (Chapter 4:Unit 4.8.1-4.8.30).
2. Beringue V., Mallinson G., Kaisar M., Tayebi M., Sattar Z., Jackson G., Anstee D., Collinge J., Hawke S. Regional heterogeneity of cellular prion protein isoforms in the mouse brain. Brain 2003, 126:2065-2073.
3. Caughey B. Scrapie associated PrP accumulation and its prevention: insights from cell culture. Br. Med. Bull. 1993, 49:860-872.
4. Chen S.G., Teplow D.B., Parchi P., Teller J.K., Gambetti P., Autilio-Gambetti L. Truncated forms of the human prion protein in normal brain and in prion diseases. J. Biol. Chem. 1995, 270:19173-19780.
5. Collinge J., Sidle K.C., Meads J., Ironside J., Hill A.F. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 1996, 383:685-690.
6. c glycoform heterogeneity as a function of brain region: implications for selective targeting of neurons by prion strains. J. Neuropathol. Exp. Neurol. 1999, 58:1000-1009.
7. Demart S., Fournier J.G., Creminon C., Frobert Y., Lamoury F., Marce D., Lasmezas C., Dormont D., Grassi J., Deslys J.P. New insight into abnormal prion protein using monoclonal antibodies. Biochem. Biophys. Res. Commun. 1999, 265:652-657.
8. Jimenez-Huete A., Lievens P.M., Vidal R., Piccardo P., Ghetti B., Tagliavini F., Frangione B., Prelli F. Endogenous proteolytic cleavage of normal and diseaseassociated isoforms of the human prion protein in neural and non-neural tissues. Am. J. Pathol. 1998, 153:1561-1572.
9. Jimi T., Wakayama Y., Shibuya S., Nakata H., Tomaru T., Takahashi Y., Kosaka K., Asano T., Kato K. High levels of nervous system-specific proteins in cerebrospinal fluid in patients with early stage Creutzfeldt-Jakob disease. Clin. Chim. Acta 1992, 211:37-46.
10. 0 / 0 mice. Mol. Med. 1996, 2:725-734.
11. Sc by Western blotting. Neurochem. Int. 2007, 50:102-108.
12. Kuczius T., Koch R., Keyvani K., Karch H., Grassi J., Groschup M.H. Regional and phenotype heterogeneity of cellular prion proteins in the human brain. Eur. J. Neurosci. 2007, 25:2649-2655.
13. Kuczius T., Karch H., Groschup M.H. Differential solubility of prions is associated in manifold phenotypes. Mol. Cell. Neurosci. 2009, 42:226-233.
14. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
15. Levavasseur E., Laffont-Proust I., Morain E., Faucheux B.A., Privat N., Peoc'h K., Sazdovitch V., Brandel J.P., Hauw J.J., Haïk S. Regulating factors of PrP glycosylation in Creutzfeldt-Jakob disease-implications for the dissemination and the diagnosis of human prion strains. PLoS ONE 2008, 3:e2786.
16. Marangos P.J., Schmechel D.E. Neuron specific enolase, a clinically useful marker for neurons and neuroendocrine cells. Annu. Rev. Neurosci. 1987, 10:269-295.
17. Markwell M.A., Haas S.M., Bieber L.L., Tolbert N.E. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 1978, 87:206-210.
18. Sc formation in vitro. Biochemistry 2006, 45:14129-14139.
19. Pan K.M., Baldwin M., Nguyen J., Gasset M., Serban A., Groth D., Melhorn I., Huang Z., Fletterick R.J., Cohen F.E., Prusiner S.B. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl Acad. Sci. USA 1993, 90:10962-10966.
20. Pan T., Li R., Wong B.S., Liu T., Gambetti P., Sy M.S. Heterogeneity of normal prion protein in two-dimensional immunoblot: presence of various glycosylated and truncated forms. J. Neurochem. 2002, 81:1092-1101.
21. Sc types in individuals with Creutzfeldt-Jakob disease. Lancet Neurol. 2005, 4:805-814.
22. Prusiner S.B. Prions. Proc. Natl Acad. Sci. USA 1998, 95:13363-13383.
23. Prusiner S.B., Groth D.F., Cochran S.P., Masiarz F.R., McKinley M.P., Martinez H.M. Molecular properties, partial purification, and assay by incubation period measurements of the hamster scrapie agent. Biochemistry 1980, 19:4883-4891.
24. Riesner D. Biochemistry and structure of PrP(C) and PrP(Sc). Br. Med. Bull. 2003, 66:21-33.
25. Rudd P.M., Endo T., Colominas C., Groth D., Wheeler S.F., Harvey D.J., Wormald M.R., Serban H., Prusiner S.B., Kobata A., Dwek R.A. Glycosylation differences between the normal and pathogenic prion protein isoforms. Proc. Natl Acad. Sci. USA 1999, 96:13044-13049.
26. Rudd P.M., Merry A.H., Wormald M.R., Dwek R.A. Glycosylation and prion protein. Curr. Opin. Struct. Biol. 2002, 12:578-586.
27. Salès N., Rodolfo K., Hässig R., Faucheux B., Di Giamberardino L., Moya K.L. Cellular prion protein localization in rodent and primate brain. Eur. J. Neurosci. 1998, 10:2464-2471.
28. Soto C., Saborio G.P., Anderes L. Cyclic amplification of protein misfolding: application to prion-related disorders and beyond. Trends Neurosci. 2002, 25:390-394.
29. Stahl N., Prusiner S.B. Prions and prion proteins. FASEB J. 1991, 5:2799-2807.
30. Stahl N., Baldwin M.A., Burlingame A.L., Prusiner S.B. Identification of glycoinositol phospholipids linked and truncated forms of the scrapie prion protein. Biochemistry 1990, 29:8879-8884.
31. Taraboulos A., Rogers M., Borchelt D.R., McKinley M.P., Scott M., Serban D., Prusiner S.B. Acquisition of protease resistance by prion proteins in scrapie-infected cells does not require asparagine-linked glycosylation. Proc. Natl Acad. Sci. USA 1990, 87:8262-8266.
32. Tuzi N.L., Cancellotti E., Baybutt H., Blackford L., Bradford B., Plinston C., Coghill A., Hart P., Piccardo P., Barron R.M., Manson J.C. Host PrP glycosylation: a major factor determining the outcome of prion infection. PLoS Biol. 2008, 6:e100.
33. Vorberg I., Priola S.A. Molecular basis of scrapie strain glycoform variation. J. Biol. Chem. 2002, 277:36775-36781.
34. Wadsworth J.D., Joiner S., Hill A.F., Campbell T.A., Desbruslais M., Luthert P.J., Collinge J. Tissue distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunoblotting assay. Lancet 2001, 358:171-180.
35. Wormald M.R., Dwek R.A. Glycoproteins: glycan presentation and protein-fold stability. Structure 1999, 7:155-160.
36. Yuan J., Xiao X., McGeehan J., Dong Z., Cali I., Fujioka H., Kong Q., Kneale G., Gambetti P., Zou W.Q. Insoluble aggregates and protease-resistant conformers of prion protein in uninfected human brains. J. Biol. Chem. 2006, 281:34848-34858.
37. Yull H.M., Ritchie D.L., Langeveld J.P., van Zijderveld F.G., Bruce M.E., Ironside J.W., Head M.W. Detection of type 1 prion protein in variant Creutzfeldt-Jakob disease. Am. J. Pathol. 2006, 168:151-157.