Nanomedicine: Nanotechnology, Biology and Medicine
Volume 1, Issue 1 , Pages 52-57 , March 2005

Atomic force microscopy analysis of the Huntington protein nanofibril formation

  • Paul R. Dahlgren

      Affiliations

    • School of Life Sciences, Arizona State University, Tempe, Arizona
    • Department of Pharmacology and Experimental Therapeutics, Loyola University Chicago, Maywood, Illinois
    • ,
  • Mikhail A. Karymov

      Affiliations

    • School of Life Sciences, Arizona State University, Tempe, Arizona
    • Department of Pharmaceutical Sciences, 986025 Nebraska Medical Center, Omaha, NE 68198-6025
    • ,
  • John Bankston

      Affiliations

    • Massachusetts Institute of Technology, Cambridge, Massachusetts
    • ,
  • Tina Holden

      Affiliations

    • Massachusetts Institute of Technology, Cambridge, Massachusetts
    • ,
  • Peter Thumfort

      Affiliations

    • Department of Chemistry, Princeton University, Princeton, New Jersey
    • ,
  • Vernon M. Ingram

      Affiliations

    • Massachusetts Institute of Technology, Cambridge, Massachusetts
    • ,
  • Yuri L. Lyubchenko

      Affiliations

    • School of Life Sciences, Arizona State University, Tempe, Arizona
    • Department of Pharmaceutical Sciences, 986025 Nebraska Medical Center, Omaha, NE 68198-6025
    • Corresponding Author InformationCorresponding author. Department of Pharmaceutical Sciences, 986025 Nebraska Medical Center, Omaha, NE 68198-6025.

Received 18 October 2004 ,Accepted 30 November 2004.

References 

  1. DiFiglia M, Sapp E, Chase K, Schwarz C, Meloni A, Young C, et al. Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons. Neuron. 1995;14:1075–1081
  2. Gutekunst CA, Levey AI, Heilman CJ, Whaley WL, Yi H, Nash NR, et al. Identification and localization of huntingtin in brain and human lymphoblastoid cell lines with anti-fusion protein antibodies. Proc Natl Acad Sci USA. 1995;92:8710–8714
  3. Sharp AH, Loev SJ, Schilling G, Li SH, Li XJ, Bao J, et al. Widespread expression of Huntington's disease gene (IT15) protein product. Neuron. 1995;14:1065–1074
  4. Perutz MF. Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem Sci. 1999;24:58–63
  5. Rubinsztein DC, Leggo J, Coles R, Almqvist E, Biancalana E, Cassiman JJ, et al. Phenotypic characterization of individuals with 30-40 CAG repeats in the Huntington disease (HD) gene reveals HD cases with 36 repeats and apparently normal elderly individuals with 36-39 repeats. Am J Hum Genet. 1996;59:16–22
  6. Sathasivam K, Amaechi I, Mangiarini L, Bates G. Identification of an HD patient with a (CAG)180 repeat expansion and the propagation of highly expanded CAG repeats in lambda phage. Hum Genet. 1997;99:692–695
  7. Mangiarini L, Sathasivam K, Seller M, Cozens B, Harper A, Hetherington C, et al. Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell. 1996;87:493–506
  8. Davies SW, Turmaine M, Cozens BA, DiFiglia M, Sharp AH, Ross CA, et al. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell. 1997;90:537–548
  9. Scherzinger E, Lurz R, Turmaine M, Mangiarini L, Hollenbach B, Hasenbank R, et al. Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell. 1997;90:549–558
  10. Hollenbach B, Scherzinger E, Schweiger K, Lurz R, Lehrach H, Wanker EE, et al. Aggregation of truncated GST-HD exon 1 fusion proteins containing normal range and expanded glutamine repeats. Philos Trans R Soc Lond B Biol Sci. 1999;354:991–994
  11. Scherzinger E, Sittler A, Schweiger K, Heiser V, Lurz R, Hasenbank R, et al. Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology. Proc Natl Acad Sci USA. 1999;96:4604–4609
  12. Poirier MA, Li H, Macosko J, Cai S, Amzel M, Ross CA. Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization. J Biol Chem. 2002;277:41032–41037
  13. Perutz MF, Johnson T, Suzuki M, Finch JT. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci USA. 1994;91:5355–5358
  14. Serpell LC. Alzheimer's amyloid fibrils: structure and assembly. Biochim Biophys Acta. 2000;1502:16–30
  15. Sunde M, Serpell LC, Bartlam M, Fraser PE, Pepys MB, Blake CC. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J Mol Biol. 1997;273:729–739
  16. Perutz MF, Finch JT, Berriman J, Lesk A. Amyloid fibers are water-filled nanotubes. Proc Natl Acad Sci USA. 2002;99:5591–5595
  17. Shlyakhtenko LS, Potaman VN, Sinden RR, Gall AA, Lyubchenko YL. Structure and dynamics of three-way DNA junctions: atomic force microscopy studies. Nucleic Acids Res. 2000;28:3472–3477
  18. Oussatcheva EA, Shlyakhtenko LS, Glass R, Sinden RR, Lyubchenko YL, Potaman VN. Structure of branched DNA molecules: gel retardation and atomic force microscopy studies. J Mol Biol. 1999;292:75–86
  19. Shlyakhtenko LS, Potaman VN, Sinden RR, Lyubchenko YL. Structure and dynamics of supercoil-stabilized DNA cruciforms. J Mol Biol. 1998;280:61–72
  20. McAllister C, Karymov M, Lushnikov A, Ohara Y, Uversky VN, Lyubchenko YL. Fatal attraction: protein folding leads to a dramatic increase in the interprotein interaction. In: In: Drug discovery in neurodegenerative diseases 2004. Cold Spring Harbor Laboratory (NY): CSHL Press; 2004;
  21. Ma B, Nussinov R. Stabilities and conformations of Alzheimer's beta-amyloid peptide oligomers (Abeta 16-22, Abeta 16-35, and Abeta 10-35): sequence effects. Proc Natl Acad Sci USA. 2002;99:14126–14131
  22. Tycko R. Insights into the amyloid folding problem from solid-state NMR. Biochemistry. 2003;42:3151–3159
  23. Petkova AT, Ishii Y, Balbach JJ, Antzutkin ON, Leapman RD, Delaglio F, et al. A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci USA. 2002;99:16742–16747
  24. Der-Sarkissian A, Jao CC, Chen J, Langen R. Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling. J Biol Chem. 2003;278:37530–37535

PII: S1549-9634(04)00005-X

doi: 10.1016/j.nano.2004.11.004

Nanomedicine: Nanotechnology, Biology and Medicine
Volume 1, Issue 1 , Pages 52-57 , March 2005

Article Tools

* Image Usage & Resolution