Anionic contribution for fibrous maturation of protofibrillar assemblies of the human tau repeat domain in a fluoroalcohol solution

Biochemistry

Volumn 43, Issue 42, 2004, Pages 13613-13620

  Konno, Takashi ^a   Oiki, Shigetoshi ^a   Hasegawa, Kazuhiro ^a   Naiki, Hironobu ^a  

^a UNIVERSITY OF FUKUI   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; BIOCHEMISTRY; BRAIN; DISEASES; ELECTRON MICROSCOPY; IONIC CONDUCTION; LIGHT SCATTERING; MICELLES; PATIENT MONITORING; REACTION KINETICS; SODIUM CHLORIDE;

FIBROUS MATURATION; PROTOFIBRILLAR ASSEMBLIES; TAU PROTEINS; TWO=PHASE KINETICS;

PROTEINS;

ALCOHOL DERIVATIVE; ANION; HEXAFLUORO 2 PROPANOL; INORGANIC SALT; SODIUM CHLORIDE; TAU PROTEIN; THIOFLAVINE;

ARTICLE; CIRCULAR DICHROISM; ELECTRON MICROSCOPY; IN VIVO STUDY; INFRARED SPECTROSCOPY; LIGHT SCATTERING; MOLECULAR DYNAMICS; NEUROFIBRILLARY TANGLE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; TRANSMISSION ELECTRON MICROSCOPY;

EID: 6344287664     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048549o     Document Type: Article

References (55)

1. Buee, L., Bussiere, T., Buee-Scherrer, V., Delacourte, A., and Hof, P. R. (2000) Tau protein isoforms, phosphorylation, and role in neurodegenerative disorders, Brain. Res. Rev. 33, 95-130.
2. Garcia, M. L., and Cleveland, D. W. (2001) Going new places using an old MAP: Tau, microtubules, and human neurodegenerative disease, Curr. Opin. Cell Biol. 13, 41-48.
3. Goedert, M., Spillantini, M. G., and Davies, S. W. (1998) Filamentous nerve cell inclusions in neurodegenerative diseases, Curr. Opin. Neurobiol. 8, 619-632.
4. Avila, J., Lucas, J. J., Perez, M., and Hernandez, F. (2004) Role of tau protein in both physiological and pathological conditions, Physiol. Rev. 84, 361-384.
5. Mena, R., Edwards, P. C., Harrington, C. R., Mukaetova-Ladinska, E. B., and Wischik, C. M. (1996) Staging the pathological assembly of truncated tau protein into paired helical filaments in Alzheimer's disease, Acta Neuropathol. 91, 633-641.
6. Galvan, M., David, J. P., Delacourte, A., Luna, J., and Mena, R. (2001) Sequence of neurofibrillary changes in aging and Alzheimer's disease: A confocal study with phospho-tau antibody, AD2, J. Alzheimer's Dis. 3, 417-425.
7. Garcia-Sierra, F., Hauw, J. J., Duyckaerts, C., Wischik, C. M., Luna-Munoz, J., and Mena, R. (2000) The extent of neurofibrillary pathology in perforant pathway neurons is the key determinant of dementia in the very old, Acta Neuropathol. 100, 29-35.
8. Mandelkow, E. M., and Mandelkow, E. (1998) Tau in Alzheimer's disease, Trends Cell Biol. 8, 425-427.
9. Friedhoff, P., von Bergen, M., Mandelkow, E. M., and Mandelkow, E. (2000) Structure of tau protein and assembly into paired helical filaments, Biochim. Biophys. Acta 1502, 122-132.
10. Gamblin, T. C., Berry, R. W., and Binder, L. I. (2003) Modeling tau polymerization in vitro: A review and synthesis, Biochemistry 42, 15009-15017.
11. Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., and Crowther, R. A. (1996) Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans, Nature 383, 550-553.
12. Perez, M., Valpuesta, J. M., Medina, M., Montejo de Garcini, E., and Avila, J. (1996) Polymerization of tau into filaments in the presence of heparin: The minimal sequence required for tau-tau interaction, J. Neurochem. 67, 1183-1190.
13. Kampers, T., Friedhoff, P., Biernat, J., Mandelkow, E. M., and Mandelkow, E. (1996) RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments, FEBS Lett. 399, 344-349.
14. Wilson, D. M., and Binder, L. I. (1997) Free fatty acids stimulate the polymerization of tau and amyloid β peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease, Am. J. Pathol. 150, 2181-2195.
15. King, M. E., Gamblin, T. C., Kuret, J., and Binder, L. I. (2000) Differential assembly of human tau isoforms in the presence of arachidonic acid, J. Neurochem. 74, 1749-1757.
16. Chirita, C. N., Necula, M., and Kuret, J. (2003) Anionic micelles and vesicles induce tau fibrillization in vitro, J. Biol. Chem. 278, 25644-25650.
17. Chirita, C. N., and Kuret, J. (2004) Evidence for an intermediate in tau filament formation, Biochemistry 43, 1704-1714.
18. Friedhoff, P., Schneider, A., Mandelkow, E. M., and Mandelkow, E. (1998) Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution, Biochemistry 37, 10223-10230.
19. Ackmann, M., Wiech, H., and Mandelkow, E. (2000) Nonsaturable binding indicates clustering of tau on the microtubule surface in a paired helical filament-like conformation, J. Biol. Chem. 275, 30335-30343.
20. Makrides, V., Shen, T. E., Bhatia, R., Smith, B. L., Thimm, J., Lal, R., and Feinstein, S. C. (2003) Microtubule-dependent oligomerization of tau. Implications for physiological tau function and tauopathies, J. Biol. Chem. 278, 33298-33304.
21. Nozaki, Y., and Tanford, C. (1971) The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale, J. Biol. Chem. 246, 2211-2217.
22. Buck, M. (1998) Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins, Q. Rev. Biophys. 31, 297-355.
23. Chiti, F., Taddei, N., Webster, P., Hamada, D., Fiaschi, T., Ramponi, G. and Dobson, C. M. (1999) Acceleration of the folding of acylphosphatase by stabilization of local secondary structure, Nat. Struct. Biol. 6, 380-387.
24. Kamatari, Y. O., Ohji, S., Konno, T., Seki, Y., Soda, K., Kataoka, M., and Akasaka, K. (1999) The compact and expanded denatured conformations of apomyoglobin in the methanol-water solvent, Protein Sci. 8, 873-882.
25. Ohnishi, S., Koide, A., and Koide, S. (2000) Solution conformation and amyloid-like fibril formation of a polar peptide derived from a β-hairpin in the OspA single-layer β-sheet, J. Mol. Biol 301, 477-489.
26. Konno, T., Iwashita, J., and Nagayama, K. (2000) Fluorinated alcohol, the third group of cosolvents that stabilize the molten-globule state relative to a highly denatured state of cytochrome c, Protein Sci. 9, 564-569.
27. Chiti, F., Taddei, N., Bucciantini, M., White, P., Ramponi, G., and Dobson, C. M. (2000) Mutational analysis of the propensity for amyloid formation by a globular protein, EMBO J. 19, 1441-1449.
28. Munishkina, L. A., Phelan, C., Uversky, V. N., and Fink, A. L. (2003) Conformational behavior and aggregation of α-synuclein in organic solvents: Modeling the effects of membranes, Biochemistry 42, 2720-2730.
29. Yamamoto, S., Yamaguchi, I., Hasegawa, K., Tsutsumi, S., Goto, Y., Gejyo, F., and Naiki, H. (2004) Glycosaminoglycans enhance the trifluoroethanol- induced extension of β 2-microglobulin-related amyloid fibrils at a neutral pH, J. Am. Soc. Nephrol. 15, 126-133.
30. Bychkova, V. E., Dujsekina, A. E., Klenin, S. I., Tiktopulo, E. I., Uversky, V. N., and Ptitsyn, O. B. (1996) Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface, Biochemistry 35, 6058-6063.
31. Sreerama, N., Venyaminov, S. Y., and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis, Anal. Biochem. 287, 243-251.
32. Wisniewski, H. M., Wen, G. Y., and Kim, K. S. (1989) Comparison of four staining methods on the detection of neuritic plaques, Acta Neuropathol. 78, 22-27.
33. Roher, A. E., Palmer, K. C., Chau, V., and Ball, M. J. (1988) Isolation and chemical characterization of Alzheimer's disease paired helical filament cytoskeletons: Differentiation from amyloid plaque core protein, J. Cell Biol. 107, 2703-2716.
34. Gjerde, D. T., Schmuckler, G., and Fritz, J. S. (1980) Anion chromatography with low-conductivity eluents. II, J. Chromatogr. 187, 35-45.
35. Sunde, M., and Blake, C. C. (1998) From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation, Q. Rev. Biophys. 31, 1-39.
36. von Bergen, M., Friedhoff, P., Biernat, J., Heberle, J., Mandelkow, E. M., and Mandelkow, E. (2000) Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming β structure, Proc. Natl. Acad. Sci. U.S.A. 97, 5129-5134.
37. Abraha, A., Ghoshal, N., Gamblin, T. C., Cryns, V., Berry, R. W., Kuret, J., and Binder, L. I. (2000) C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease, J. Cell Sci. 113 (Part 21), 3737-3745.
38. Giannetti, A. M., Lindwall, G., Chau, M. F., Radeke, M. J., Feinstein, S. C., and Kohlstaedt, L. A. (2000) Fibers of tau fragments, but not full length tau, exhibit a cross β-structure: Implications for the formation of paired helical filaments, Protein Sci. 9, 2427-2435.
39. Barghorn, S., Davies, P., and Mandelkow, E. (2004) Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on β-structure in the core domain, Biochemistry 43, 1694-1703.
40. Kamatari, Y. O., Konno, T., Kataoka, M., and Akasaka, K. (1996) The methanol-induced globular and expanded denatured states of cytochrome c: A study by CD fluorescence, NMR, and small-angle X-ray scattering, J. Mol. Biol. 259, 512-523.
41. Hirota, N., Mizuno, K., and Goto, Y. (1998) Group additive contributions to the alcohol-induced α-helix formation of melittin: Implication for the mechanism of the alcohol effects on proteins, J. Mol. Biol. 275, 365-378.
42. Diaz, M. D., Fioroni, M., Burger, K., and Berger, S. (2002) Evidence of complete hydrophobic coating of bombesin by trifluoroethanol in aqueous solution: An NMR spectroscopic and molecular dynamics study, Chemistry 8, 1663-1669.
43. Fioroni, M., Diaz, M. D., Burger, K., and Berger, S. (2002) Solvation phenomena of a tetrapeptide in water/trifluoroethanol and water/ethanol mixtures: A diffusion NMR, intermolecular NOE, and molecular dynamics study, J. Am. Chem. Soc. 124, 7737-7744.
44. Gast, K., Siemer, A., Zirwer, D., and Damaschun, G. (2001) Fluoroalcohol-induced structural changes of proteins: Some aspects of cosolvent-protein interactions, Eur. Biophys. J. 30, 273-283.
45. Roccatano, D., Colombo, G., Fioroni, M., and Mark, A. E. (2002) Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: A molecular dynamics study, Proc. Natl. Acad. Sci. U.S.A. 99, 12179-12184.
46. Padrick, S. B. and Miranker, A. D. (2002) Islet amyloid: Phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis, Biochemistry 41, 4694-4703.
47. Fezoui, Y., and Teplow, D. B. (2002) Kinetic studies of amyloid β-protein fibril assembly, J. Biol. Chem. 277, 36948-36954.
48. Wille, H., Zhang, G.-F., Baldwin, M. A., Cohen, F. E. and Prusiner, S. B. (1996) Separation of scrapie prion infectivity from PrP amyloid polymers, J. Mol. Biol. 259, 608-621.
49. Harper, J. D., and Lansbury, P. T., Jr. (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins, Annu. Rev. Biochem. 66, 385-407.
50. Friedhoff, P., von Bergen, M., Mandelkow, E. M., Davies, P., and Mandelkow, E. (1998) A nucleated assembly mechanism of Alzheimer paired helical filaments, Proc. Natl. Acad. Sci. U.S.A. 95, 15712-15727.
51. King, M. E., Ahuja, V., Binder, L. I., and Kuret, J. (1999) Ligand-dependent tau filament formation: Implications for Alzheimer's disease progression, Biochemistry 38, 14851-14859.
52. Minton, A. P. (2001) The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media, J. Biol. Chem. 276, 10577-10580.
53. Ellis, R. J. (2001) Macromolecular crowding: Obvious but underappreciated, Trends Biochem. Sci. 26, 597-604.
54. Bancher, C., Brunner, C., Lassmann, H., Budka, H., Jellinger, K., Wiche, G., Seitelberger, F., Grundke-Iqbal, I., Iqbal, K., and Wisniewski, H. M. (1989) Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease, Brain Res. 477, 90-99.
55. Barghorn, S., and Mandelkow, E. (2002) Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments, Biochemistry 41, 14885-14896.