Molecular electron microscopy approaches to elucidating the mechanisms of protein fibrillogenesis

Methods in Molecular Biology

Volumn 299, Issue , 2005, Pages 81-101

  Lashuel, Hilal A ^a   Wall, Joseph S ^b  

^a Brigham and Women's Hospital Center for Neurologic Diseases   (United States)

^b BROOKHAVEN NATIONAL LABORATORY   (United States)

Author keywords

Amyloid fibrils; Amyloid (A ); Electron microscopy (EM); Negative staining; Oligomers; Protofibrils; Scanning transmission electron microscopy (STEM); Sedimentation velocity analytical ultracentrifugation (SVAU); Single particle analysis; synuclein

Indexed keywords

AMYLOID;

CRYOELECTRON MICROSCOPY; ELECTRON MICROSCOPY; EX VIVO STUDY; IMAGE PROCESSING; IMAGE RECONSTRUCTION; IN VITRO STUDY; PROTEIN QUATERNARY STRUCTURE; SCANNING TRANSMISSION ELECTRON MICROSCOPY; SINGLE PARTICLE MOLECULAR AVERAGING ELECTRON MICROSCOPY; THREE DIMENSIONAL IMAGING;

EID: 22844440807     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1385/1-59259-874-9:081     Document Type: Chapter

References (40)

1. Selkoe, D. J. (2003) Folding proteins in fatal ways. Nature 426(6968), 900-904.
2. Rochet, J. C. and Lansbury, P. T. Jr. (2000) Amyloid fibrillogenesis: themes and variations. Curr. Opin. Struct. Biol. 10(1), 60-68.
3. Paul, W. E. and Cohen, A. S. (1963) Electron microscopic studies of amyloid fibrils with ferritinconjugated antibody. Am. J. Pathol. 43, 721-738.
4. Cohen, A. S. (1965) The constitution and genesis of amyloid. Int. Rev. Exp. Pathol. 4, 159-243.
5. Bladen, H. A., Nylen, M. U., and Glenner, G. G. (1966) The ultrastructure of human amyloid as revealed by the negative staining technique. J. Ultrastruct. Res. 14(5), 449-459.
6. Harper, J. D., Lieber, C. M., and Lansbury, P. T. Jr. (1997) Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein. Chem. Biol. 4(12), 951-959.
7. Harper, J. D., et al. (1997) Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chem. Biol. 4(2), 119-125.
8. Walsh, D. M., et al. (1997) Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 272(35), 22364-22372.
9. Lambert, M. P., et al. (1998) Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. USA 95(11), 6448-6453.
10. Hartley, D. M., et al. (1999) Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19(20), 8876-8884.
11. Walsh, D. M., et al. (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416(6880), 535-539.
12. Bucciantini, M., et al. (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416(6880), 507-511.
13. Goldberg, M. S. and Lansbury, P. T. Jr. (2000) Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nat. Cell Biol. 2(7), E115-E119.
14. Caughey, B. and Lansbury, P. (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from their innocent bystandards. Annu. Rev. Neurosci. 26, 267-298.
15. Serpell, L. C., Fraser, P. E., and Sunde, M. (1999) X-ray fiber diffraction of amyloid fibrils. Methods Enzymol. 309, 526-536.
16. Serpell, L. C. (2000) Alzheimer's amyloid fibrils: structure and assembly. Biochim. Biophys. Acta 1502(1), 16-30.
17. Saibil, H. R. (2000) Macromolecular structure determination by cryo-electron microscopy. Acta Crystallogr. D Biol. Crystallogr. 56(Pt 10), 1215-1222.
18. Radermacher, M., et al. (1987) Three-dimensional reconstruction from a singleexposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J. Microsc. 146(Pt 2), 113-136.
19. Serpell, L. C., et al. (1995) Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs. J. Mol. Biol. 254(2), 113-118.
20. Jimenez, J. L., et al. (1999) Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. Embo J. 18(4), 815-821.
21. Jimenez, J. L., et al. (2002) The protofilament structure of insulin amyloid fibrils. Proc. Natl. Acad. Sci. USA 99(14), 9196-9201.
22. Lashuel, H., et al. (2003) Mixtures of wild-type and “Arctic” Abeta40 in vitro accumulate protofibrils, including amyloid pores. J. Mol. Biol. 332(4), 795-808.
23. Lashuel, H., et al. (2002) alpha-Synuclein, especially the Parkinson's diseaseassociated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol. 322(5), 1089.
24. Lashuel, H. A., et al. (2002) Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 418(6895), 291.
25. Wang, L., et al. (2002) Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel. Proc. Natl. Acad. Sci. USA 99(25), 15947-15952.
26. Makin, O. S. and Serpell, L. C. (2002) Examining the structure of the mature amyloid fibril. Biochem. Soc. Trans. 30(4), 521-525.
27. Frank, J., et al. (1996) SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116(1), 190-199.
28. Serpell, L. C., et al. (2000) The protofilament substructure of amyloid fibrils. J. Mol. Biol. 300(5), 1033-1039.
29. Volles, M. J., et al. (2001) Vesicle permeabilization by protofibrillar alphasynuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry 40(26), 7812-7819.
30. Volles, M. J. and Lansbury, P. T. Jr. (2002) Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism. Biochemistry 41(14), 4595-4602.
31. Kagan, B. L., et al. (2002) The channel hypothesis of Alzheimer's disease: current status. Peptides 23(7), 1311-1315.
32. Kourie, J. I., et al. (2002) Heterogeneous amyloid-formed ion channels as a common cytotoxic mechanism: implications for therapeutic strategies against amyloidosis. Cell. Biochem. Biophys. 36(2-3), 191-207.
33. King, M. E., et al. (2001) Structural analysis of Pick's disease-derived and in vitro-assembled tau filaments. Am. J. Pathol. 158(4), 1481-1490.
34. Ksiezak-Reding, H., et al. (1996) Ultrastructural instability of paired helical filaments from corticobasal degeneration as examined by scanning transmission electron microscopy. Am. J. Pathol. 149(2), 639-651.
35. Antzutkin, O. N., et al. (2002) Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance. Biochemistry 41(51), 15436-15450.
36. Antzutkin, O. N. (2004) Amyloidosis of Alzheimer's Abeta peptides: solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies. Magn. Reson. Chem. 42(2), 231-246.
37. Goldsbury, C. S., et al. (2000) Studies on the in vitro assembly of a beta 1-40: implications for the search for a beta fibril formation inhibitors. J. Struct. Biol. 130(2-3), 217-231.
38. Cardoso, I., et al. (2002) Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils. J. Mol. Biol. 317(5), 683-695.
39. Baxa, U., et al. (2003) Architecture of Ure2p prion filaments: the N-terminal domains form a central core fiber. J. Biol. Chem. 278(44), 43717-43727.
40. Tracz, E., et al. (1997) Paired helical filaments in corticobasal degeneration: the fine fibrillary structure with NanoVan. Brain Res. 773(1-2), 33-44.