Disruption of the toxic conformation of the expanded polyglutamine stretch leads to suppression of aggregate formation and cytotoxicity

Biochemical and Biophysical Research Communications

Volumn 317, Issue 4, 2004, Pages 1200-1206

  Popiel, Helena A ^a,b   Nagai, Yoshitaka ^a   Onodera, Osamu ^c   Inui, Takashi ^d   Fujikake, Nobuhiro ^a   Urade, Yoshihiro ^e   Strittmatter, Warren J ^f   Burke, James R ^f   Ichikawa, Atsushi ^g   Toda, Tatsushi ^a  

^a OSAKA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^b KYOTO UNIVERSITY   (Japan)

^c NIIGATA UNIVERSITY   (Japan)

^d Tsu City College   (Japan)

^e OSAKA BIOSCIENCE INSTITUTE   (Japan)

^f DUKE UNIVERSITY MEDICAL CENTER   (United States)

^g MUKOGAWA WOMEN'S UNIVERSITY   (Japan)

Author keywords

Aggregation; Huntington's disease; Neurodegeneration; Polyglutamine; Proline mutagenesis; Protein conformation

Indexed keywords

POLYGLUTAMINE; PROLINE;

ANIMAL CELL; ARTICLE; CELL CULTURE; CORRELATION ANALYSIS; CYTOTOXICITY; DEGENERATIVE DISEASE; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BLOTTING, WESTERN; CELL AGGREGATION; CIRCULAR DICHROISM; COS CELLS; ESCHERICHIA COLI; NEPHELOMETRY AND TURBIDIMETRY; PEPTIDES; PROLINE; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY, ULTRAVIOLET;

INSERTION SEQUENCES;

EID: 11144358201     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.03.161     Document Type: Article

References (29)

1. Zoghbi H.Y., Orr H.T. Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci. 23:2000;217-247.
2. Margolis R.L., Ross C.A. Expansion explosion: new clues to the pathogenesis of repeat expansion neurodegenerative diseases. Trends Mol. Med. 7:2001;479-482.
3. Gusella J.F., MacDonald M.E. Molecular genetics: unmasking polyglutamine triggers in neurodegenerative disease. Nat. Rev. Neurosci. 1:2000;109-115.
4. Trottier Y., Lutz Y., Stevanin G., Imbert G., Devys D., Cancel G., Saudou F., Weber C., David G., Tora L., Agid Y., Brice A., Mandel J. Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias. Nature. 378:1995;403-406.
5. Scherzinger E., Lurz R., Turmaine M., Mangiarini L., Hollenbach B., Hasenbank R., Bates G.P., Davies S.W., Lehrach H., Wanker E.E. Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell. 90:1997;549-558.
6. Tanaka M., Morishima I., Akagi T., Hashikawa T., Nukina N. Intra- and intermolecular β-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases. J. Biol. Chem. 276:2001;45470-45475.
7. Chen S., Berthelier V., Hamilton J.B., O'Nuallain B., Wetzel R. Amyloid-like features of polyglutamine aggregates and their assembly kinetics. Biochemistry. 41:2002;7391-7399.
8. Quan F., Janas J., Popovich B.W. A novel CAG repeat configuration in the SCA1 gene: implications for the molecular diagnostics of spinocerebellar ataxia type 1. Hum. Mol. Genet. 4:1995;2411-2413.
9. Frontali M., Novelletto A., Annesi G., Jodice C. CAG repeat instability, cryptic sequence variation and pathogenicity: evidence from different loci. Philos. Trans. R. Soc. Lond. B Biol. Sci. 354:1999;1089-1094.
10. Chiba T., Hagihara Y., Higurashi T., Hasegawa K., Naiki H., Goto Y. Amyloid fibril formation in the context of full-length protein: effects of proline mutations on the amyloid fibril formation of β2-microglobulin. J. Biol. Chem. 278:2003;47016-47024.
11. Wood S.J., Wetzel R., Martin J.D., Hurle M.R. Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4. Biochemistry. 34:1995;724-730.
12. Soto C., Kindy M.S., Baumann M., Frangione B. Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation. Biochem. Biophys. Res. Commun. 226:1996;672-680.
13. Soto C., Sigurdisson E.M., Morelli L., Kumar R.A., Castano E.M., Frangione B. β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nat. Med. 4:1998;822-826.
14. Richardson J.S., Richardson D.C. Principles and patterns of protein conformation. Fasman G. Prediction of Protein Structure and Principles of Protein Conformation. 1989;43-75 Plenum Press, New York.
15. Zhu H., Braun W. Sequence specificity, statistical potentials, and three-dimensional structure prediction with self-correcting distance geometry calculations of β-sheet formation in proteins. Protein Sci. 8:1999;326-342.
16. Peters M.F., Ross C.A. Preparation of human cDNAas encoding expanded polyglutamine repeats. Neurosci. Lett. 275:1999;129-132.
17. Nagai Y., Tucker T., Ren H., Kenan D.J., Henderson B.S., Keene J.D., Strittmatter W.J., Burke J.R. Inhibition of polyglutamine protein aggregation and cell death by novel peptides identified by phage display screening. J. Biol. Chem. 275:2000;10437-10442.
18. Onodera O., Burke J.R., Miller S.E., Hester S., Tsuji S., Roses A.D., Strittmatter W.J. Oligomerization of expanded-polyglutamine domain fluorescent fusion proteins in cultured mammalian cells. Biochem. Biophys. Res. Commun. 238:1997;599-605.
19. Calabresi V., Guida S., Servadio A., Jodice C. Phenotypic effects of expanded ataxin-1 polyglutamines with interruptions in vitro. Brain Res. Bull. 56:2001;337-342.
20. Sen S., Dash D., Pasha S., Brahmachari S.K. Role of histidine interruption in mitigating the pathological effects of long polyglutamine stretches in SCA1: a molecular approach. Protein Sci. 12:2003;953-962.
21. Thakur A.K., Wetzel R. Mutational analysis of the structural organization of polyglutamine aggregates. Proc. Natl. Acad. Sci. USA. 99:2002;17014-17019.
22. Perutz M.F., Windle A.H. Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats. Nature. 412:2001;143-144.
23. Sherman M.Y., Goldberg A.L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron. 29:2001;15-32.
24. Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M., Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 416:2002;507-511.
25. Taylor J.P., Hardy J., Fischbeck K.H. Toxic proteins in neurodegenerative disease. Science. 296:2002;1991-1995.
26. Chai Y., Koppenhafer S.L., Bonini N.M., Paulson H.L. Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J. Neurosci. 19:1999;10338-10347.
27. Nagai Y., Fujikake N., Ohno K., Higashiyama H., Popiel H.A., Rahadian J., Yamaguchi M., Strittmatter W.J., Burke J.R., Toda T. Prevention of polyglutamine oligomerization and neurodegeneration by the peptide inhibitor QBP1 in Drosophila. Hum. Mol. Genet. 12:2003;1253-1259.
28. Sanchez I., Mahlke C., Yuan J. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature. 421:2003;373-379.
29. Caughey B., Lansbury P.T. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26:2003;267-298.