Exothermic effects observed upon heating of β2- microglobulin monomers in the presence of amyloid seeds

Biochemistry

Volumn 45, Issue 29, 2006, Pages 8760-8769

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

^a OSAKA UNIVERSITY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; DIFFERENTIAL SCANNING CALORIMETRY; PH EFFECTS; PROTEINS; SPECIFIC HEAT;

AMYLOID FIBRILS; MICROGLOBULIN; SALT-INDUCED PROTOFIBRILS; SIGMOIDAL TRANSITION;

MONOMERS;

AMYLOID BETA PROTEIN; BETA 2 MICROGLOBULIN; MONOMER; RECOMBINANT PROTEIN;

AMYLOIDOSIS; ARTICLE; ATOMIC FORCE MICROSCOPY; DIALYSIS; DIFFERENTIAL SCANNING CALORIMETRY; ESCHERICHIA COLI; HEATING; KINETICS; LIGHT SCATTERING; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STRUCTURE; TEMPERATURE; THERMAL ANALYSIS; ULTRACENTRIFUGATION;

AMYLOID; BETA 2-MICROGLOBULIN; CALORIMETRY, DIFFERENTIAL SCANNING; HEAT; HUMANS; KINETICS; LIGHT; PROTEIN CONFORMATION; PROTEIN DENATURATION; SCATTERING, RADIATION; ULTRACENTRIFUGATION;

EID: 33746224052     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0606748     Document Type: Article

References (45)

1. Kelly, J. W. (1998) The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways, Curr. Opin. Struct. Biol. 8, 101-106.
2. Dobson, C. M. (2003) Protein folding and misfolding, Nature 426, 884-890.
3. Ross, C. A., and Poirier, M. A. (2004) Protein aggregation and neurodegenerative disease, Nat. Med. 10, s10-s17.
4. Tycko, R. (2004) Progress towards a molecular-level structural understanding of amyloid fibrils, Curr. Opin. Struct. Biol. 14, 96-103.
5. Fandrich, 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.
6. Saiki, M., Honda, S., Kawasaki, K., Zhou, D., Kaito, A., Konakahara, T., and Morii, H. (2005) Higher-order molecular packing in amyloid-like fibrils constructed with linear arrangements of hydrophobic and hydrogen-bonding side-chains, J. Mol. Biol. 348, 983-998.
7. Makin, O. S., and Serpell, L. C. (2005) Structures for amyloid fibrils, FEBS J. 272, 5950-5961.
8. 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.
9. 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.
10. Uversky, V. N., and Fink, A. L. (2004) Conformational constraints for amyloid fibrillation: the importance of being unfolded, Biochim. Biophys. Acta 1698, 131-153.
11. 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.
12. Garrotta, 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.
13. Bhattacharyya, A. M., Thakur, A. K., and Wetzel, R. (2005) Polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction, Proc. Natl. Acad. Sci. U.S.A. 102, 15400-15405.
14. Bader, R., Bamford, R., Zurdo, J., Luisi, B. P., 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.
15. 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.
16. Yamamoto, S., and Gejyo, F. (2005) Historical background and clinical treatment of dialysis-related amyloidosis, Biochim. Biophys. Acta 1753, 4-10.
17. 2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond, J. Biol. Chem. 277, 21554-21560.
18. 2-microglobulin amyloid fibril by H/D exchange, Nat. Struct. Biol. 9, 332-336.
19. 2- microglobulin amyloid in vitro revealed by atomic force microscopy, J. Mol. Biol. 330, 785-797.
20. 2-microglobulin, J. Boil. Chem. 278, 47016-47024.
21. 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.
22. 2-microglobulin under physiological conditions, J. Biol. Chem. 279, 10814-10821.
23. Yamaguchi, K., Takahashi, S., Kawai, T., Naiki, H., and Goto, Y. (2005) Seeding-dependent propagation and maturation of amyloid fibril conformation, J. Mol. Biol. 352, 952-960.
24. 2-microglobulin, Biochemistry 44, 157-164.
25. 2-microglobulin amyloid fibril growth and stability, Biochemistry 44, 1288-1299.
26. Ivanova, M. I., Sawaya, M. R., Gingery, M., Attinger, A., and Eisenberg, D. (2004) An amyloid-forming segment of β2-microglobulin suggests a molecular model for the fibril, Proc. Natl. Acad. Sci. U.S.A. 101, 10584-10589.
27. 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.
28. Chatani, E., Kato, M., Kawai, T., Naiki, H., and Goto, Y. (2005) Main-chain dominated amyloid structures demonstrated by the effect of high pressure, J. Mol. Biol. 352, 941-951.
29. 2-microglobulin into amyloid, J. Mol. Biol. 351, 850-864.
30. Balbirnie, M., Grothe, R., and Eisenberg, D. S. (2001) An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid, Proc. Natl. Acad. Sci. U.S.A. 98, 2375-2380.
31. 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.
32. 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.
33. Broome, B. M., and Hecht, M. H. (2000) Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis, J. Mol. Biol. 296, 961-968.
34. 2-Microglobulin amyloidosis: insights from conservation analysis and fibril modelling by protein docking techniques, J. Mol. Biol. 330, 159-174.
35. 2-microglobulin amyloid fibrils, J. Mol. Biol. 352, 700-711.
36. Berkowitz, S. A., Velicelebi, G., Sutherland, J. W. H., and Sturtevant, J. M. (1980) Observation of an exothermic process associated with the in vitro polymerization of brain tubulin, Proc. Natl. Acad. Sci. U.S.A. 77, 4425-4429.
37. Dzwolak, W., Ravindra, R., Lendermann, J., and Winter, R. (2003) Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy, Biochemistry 42, 11347-11355.
38. 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.
39. Stites, W. E. (1997) Protein-protein interactions: interface structure, binding thermodynamics, and mutational analysis, Chem. Rev. 97, 1233-1250.
40. Bergqvist, S., Williams, M. A., O'Brien, R., and Ladbury, J. E. (2004) Heat capacity effects of water molecules and ions at protein-DNA interface, J. Mol. Biol. 336, 829-842.
41. Dill, K. A. (1990) Dominant forces in protein folding, Biochemistry 29, 7133-7155.
42. 2- microglobulin amyloid formation in vitro, Biochim. Biophys. Acta 1753, 51-63.
43. 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.
44. 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.
45. Morel, B., Casares, S., and Conejero-Lara, F. (2006) A single mutation induces amyloid aggregation in the α-spectrin SH3 domain: analysis of the early stages of fibril formation, J. Mol. Biol. 356, 453-468.