Heat-triggered conversion of protofibrils into mature amyloid fibrils of β2-microglobulin

Biochemistry

Volumn 46, Issue 11, 2007, Pages 3286-3293

  Sasahara, Kenji ^a   Yagi, Hisashi ^a   Naiki, Hironobu ^b   Goto, Yuji ^a  

^a OSAKA UNIVERSITY   (Japan)

^b UNIVERSITY OF FUKUI   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DICHROISM SPECTROSCOPY; DIFFERENTIAL SCANNING CALORIMETRY; ELECTRON MICROSCOPY; HEATING RATE; PH EFFECTS; PROTEINS; THERMAL EFFECTS;

AMYLOID FIBRILS; MICROGLOBULIN; PROTOFIBRILS; TEMPERATURE DEPENDENCE;

BIOLOGICAL MEMBRANES;

AMYLOID; BETA 2 MICROGLOBULIN; SODIUM CHLORIDE; THIOFLAVINE;

AMYLOIDOSIS; ARTICLE; CHEMICAL REACTION KINETICS; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; DIALYSIS; DIFFERENTIAL SCANNING CALORIMETRY; HEATING; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE; THERMODYNAMICS;

AMYLOID; BETA 2-MICROGLOBULIN; CALORIMETRY, DIFFERENTIAL SCANNING; HEAT; HUMANS; LIGHT; MICROSCOPY, ELECTRON, TRANSMISSION; SCATTERING, RADIATION;

EID: 33947377892     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi602403v     Document Type: Article

References (39)

1. Thirumalai, D., Klimov, D. K., and Dima, R. I. (2003) Emerging ideas on the molecular basis of protein and peptide aggregation, Curr. Opin. Struct. Biol. 13, 146-159.
2. Ross, C. A., and Poirier, M. A. (2004) Protein aggregation and neurodegenerative disease, Nat. Med. 10, s10-s17.
3. Dobson, C. M. (2006) Protein aggregation and its consequences for human disease, Protein Pept. Lett. 13, 219-227.
4. Sunde, M., and Blake, C. (1997) The structure of amyloid fibrils by electron microscopy and X-ray diffraction, Adv. Protein Chem. 50, 123-159.
5. Tycko, R. (2004) Progress towards a molecular-level structural understanding of amyloid fibrils, Curr. Opin. Struct. Biol. 14, 96-103.
6. Makin, O. S., and Serpell, L. C. (2005) Structures for amyloid fibrils, FEBS Lett. 272, 5950-5961.
7. Fändrich, M., and Dobson, C. M. (2002) The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation, EMBO J. 21, 5682-5690.
8. Chiti, F., Webster, P., Taddei, N., Clark, A., Stefani, M., Ramponi, G., and Dobson, C. M. (1999) Designing conditions for in vitro formation of amyloid protofilaments and fibrils, Proc. Natl. Acad. Sci. U.S.A. 96, 3590-3594.
9. Bjorkman, P. J., Saper, M. A., Samraoui, B., Bennett, W. S., Strominger, J. L., and Wiley, D. C. (1987) Structure of the human class I histocompatibility antigen, HLA-A2, Nature 329, 506-512.
10. Yamamoto, S., and Gejyo, F. (2005) Historical background and clinical treatment of dialysis-related amyloidosis, Biochim. Biophys. Acta 1753, 4-10.
11. Naiki, H., Hashimoto, N., Suzuki, S., Kimura, H., Nakakuki, K., and Gejyo, F. (1997) Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro, Amyloid 4, 223-232.
12. Ban, T., Hamada, D., Hasegawa, K., Naiki, H., and Goto, Y. (2003) Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence, J. Biol. Chem. 278, 16462-16465.
13. Kardos, J., Yamamoto, K., Hasegawa, K., Naiki, H., and Goto, Y. (2004) Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry, J. Biol. Chem. 279, 55308-55314.
14. 2-microglobulin amyloid formation at neutral pH, Biochemistry 45, 2311-2321.
15. 2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond, J. Biol. Chem. 277, 21554-21560.
16. 2- microglobulin amyloid fibril growth and stability, Biochemistry 44, 1288-1299.
17. 2-microglobulin into amyloid, J. Mol. Biol. 351, 850-864.
18. 2-microglobulin amyloid formation in vitro, Biochim. Biophys. Acta 1753, 51-63.
19. LeVine, H., III (1999) Quantification of β-sheet amyloid fibril structures with thioflavin T, Methods Enzymol. 309, 274-284.
20. Uversky, V. N., and Fink, A. L. (2004) Conformational constraints for amyloid fibrillation: The importance of being unfolded, Biochim. Biophys. Acta 1698, 131-153.
21. Sanchez-Ruiz, J. M., Lopez-Lacomba, J. L., Cortijo, M., and Mateo, P. L. (1988) Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin, Biochemistry 27, 1648-1652.
22. Weijers, M., Barneveld, P. A., Cohen Stuart, M. A., and Visschers, R. W. (2003) Heat-induced denaturation and aggregation of ovalbumin at neutral pH described by irreversible first-order kinetics, Protein Sci. 12, 2693-2703.
23. Azuaga, A. I., Dobson, C. M., Mateo, P. L., and Conejero-Lara, F. (2002) Unfolding and aggregation during the thermal denaturation of streptokinase, Eur. J. Biochem. 269, 4121-4133.
24. Rezaei, H., Choiset, Y., Eghiaian, F., Treguer, E., Mentre, P., Debey, P., Grosclaude, J., and Haertle, T. (2002) Amyloidogenic unfolding intermediates differentiate sheep prion protein variants, J. Mol. Biol. 322, 799-814.
25. 2-microglobulin amyloid fibrils, J. Mol. Biol. 352, 700-711.
26. 2-microglobulin monomers in the presence of amyloid seeds, Biochemistry 45, 8760-8769.
27. 2-microglobulin, J. Biol. Chem. 278, 47016-47024.
28. 2-microglobulin amyloid in vitro revealed by atomic force microscopy, J. Mol. Biol. 330, 785-797.
29. Goldsbury, C., Frey, P., Olivieri, V., Aebi, U., and Müller, S. A. (2005) Multiple assembly pathways underlie amyloid-β fibril polymorphisms, J. Mol. Biol. 352, 282-298.
30. Stathopulos, P. B., Scholz, G. A., Hwang, Y. M., Rumfeldt, J. A., Lepock, J. R., and Meiering, E. M. (2004) Sonication of proteins causes formation of aggregates that resemble amyloid, Protein Sci. 13, 3017-3027.
31. 2- microglobulin, J. Biol. Chem. 280, 32843-32848.
32. Dill, K. A. (1990) Dominant forces in protein folding, Biochemisrtry 29, 7133-7155.
33. Perutz, M. F., Finch, J. T., Berriman, J., and Lesk, A. (2002) Amyloid fibers are water-filled nanotubes, Proc. Natl. Acad. Sci. U.S.A. 99, 5591-5595.
34. Cordeiro, Y., Kraineva, J., Ravindra, R., Lima, L. M., Gomes, M. P. B., Foguel, D., Winter, R., and Silva, J. L. (2004) Hydration and packing effects on prion folding and β-sheet conversion. High pressure spectroscopy and pressure perturbation calorimetry studies, J. Biol. Chem. 279, 32354-32359.
35. Cooper, A. (2005) Heat capacity effects in protein folding and ligand binding: A re-evaluation of the role of water in biomolecular thermodynamics, Biophys. Chem. 115, 89-97.
36. Modler, A. J., Gast, K., Lutsch, G., and Damaschun, G. (2003) Assembly of amyloid protofibrils via critical oligomers: A novel pathway of amyloid formation, J. Mol. Biol. 325, 135-148.
37. Carrotta, R., Manno, M., Bulone, D., Martorana, V., and San, Biagio, P. L. (2005) Protofibril formation of amyloid β-protein at low pH via a non-cooperative elongation mechanism, J. Biol. Chem. 280, 30001-30008.
38. Hurshman, A. R., White, J. T., Powers, E. T., and Kelly, J. W. (2004) Transthyretin aggregation under partially denaturing conditions is a downhill polymerization, Biochemistry 43, 7365-7381.
39. Bader, R., Bamford, R., Zurdo, J., Luisi, B. F., and Dobson, C. M. (2006) Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation, J. Mol. Biol. 356, 189-208.