Low concentrations of sodium dodecyl sulfate induce the extension of β2-microglobulin-related amyloid fibrils at a neutral pH

Biochemistry

Volumn 43, Issue 34, 2004, Pages 11075-11082

  Yamamoto, Suguru ^a,b   Hasegawa, Kazuhiro ^a   Yamaguchi, Itaru ^a   Tsutsumi, Shinobu ^a   Kardos, József ^c,d   Goto, Yuji ^c,d   Gejyo, Fumitake ^b   Naiki, Hironobu ^a  

^a UNIVERSITY OF FUKUI   (Japan)

^b NIIGATA UNIVERSITY GRADUATE SCHOOL OF MEDICAL AND DENTAL SCIENCES   (Japan)

^c OSAKA UNIVERSITY   (Japan)

^d JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CONCENTRATION (PROCESS); CONFORMATIONS; ELECTRON MICROSCOPY; ENZYME KINETICS; ETHANOL; MICELLES; PH EFFECTS; PHYSIOLOGY;

CIRCULAR DICHROISM; DESTABILIZATION; FIBRILS; MICROGLOBULIN;

BIOCHEMISTRY;

AMYLOID; BETA 2 MICROGLOBULIN; DODECYL SULFATE SODIUM; PHOSPHOLIPID; THIOFLAVINE; TRIFLUOROETHANOL; DETERGENT; DODECYLTRIMETHYLAMMONIUM; OCTOXINOL; POLYMER; QUATERNARY AMMONIUM DERIVATIVE; RECOMBINANT PROTEIN; SURFACTANT; ZWITTERGENT 3 12; ZWITTERGENT 3-12;

AMYLOIDOSIS; ARTICLE; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; ELECTRON MICROSCOPY; FLUORESCENCE SPECTROSCOPY; MICELLE; PH; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; CHEMISTRY; DOSE RESPONSE; HUMAN; METABOLISM; SPECTROFLUOROMETRY; ULTRASTRUCTURE;

AMYLOID; BETA 2-MICROGLOBULIN; CIRCULAR DICHROISM; DETERGENTS; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; HYDROGEN-ION CONCENTRATION; MICELLES; OCTOXYNOL; POLYMERS; PROTEIN CONFORMATION; PROTEIN FOLDING; QUATERNARY AMMONIUM COMPOUNDS; RECOMBINANT PROTEINS; SODIUM DODECYL SULFATE; SPECTROMETRY, FLUORESCENCE; SURFACE-ACTIVE AGENTS;

EID: 4644335370     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049262u     Document Type: Article

References (53)

1. Koch, K. M. (1992) Dialysis-related amyloidosis, Kidney Int. 41, 1416-1429.
2. Charra, B., Calemard, E., Uzan, M., Terrat, J. C., Vanel, T., and Laurent, G. (1985) Carpal tunnel syndrome, shoulder pain and amyloid deposits in long-term haemodialysis patients, Proc. Eur. Dial. Transplant. Assoc. 21, 291-295.
3. Gejyo, F., and Arakawa, M. (1990) Dialysis amyloidosis: current disease concepts and new perspectives for its treatment, Contrib. Nephrol. 78, 47-60.
4. 2-microglobulin, Biochem. Biophys. Res. Commun. 129, 701-706.
5. 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis, Proc. Natl. Acad. Sci. U.S.A. 83, 7908-7912.
6. 2-microglobulin amyloid fibrils in peripheral blood mononuclear cell culture, Am. J. Pathol. 141, 241-247.
7. 2-microglobulin as the amyloidogenic protein in dialysis-amyloidosis, Kidney Int. 50, 1262-1267.
8. 2-microglobulin as a new form of amyloid protein in patients undergoing long-term hemodialysis, N. Engl. J. Med. 314, 585-586.
9. Chanard, J., Bindi, P., Lavaud, S., Toupance, O., Maheut, H., and Lacour, F. (1989) Carpal tunnel syndrome and type of dialysis membrane, Br. Med. J. 298, 867-868.
10. van Ypersele de Strihou, C., Jadoul, M., Malghem, J., Maldague, B., Jamart, J., and the Working Party on Dialysis Amyloidosis (1991) Effect of dialysis membrane and patient's age on signs of dialysis-related amyloidosis, Kidney Int. 39, 1012-1019.
11. 2-Microglobulin and amyloidosis: who is at risk? Nephrol. Dial. Transplant. 10 (Suppl. 10), 48-51.
12. Naiki, H., Higuchi, K., Nakakuki, K., and Takeda, T. (1991) Kinetic analysis of amyloid fibril polymerization in vitro, Lab. Invest. 65, 104-110.
13. Jarrett, J. T., and Lansbury, P. T., Jr. (1993) Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058.
14. Naiki, H., and Nakakuki, K. (1996) First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro, Lab. Invest. 74, 374-383.
15. Naiki, H., Gejyo, F., and Nakakuki, K. (1997) Concentration-dependent inhibitory effects of apolipoprotein E on Alzheimer's β-amyloid fibril formation in vitro, Biochemistry 36, 6243-6250.
16. 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.
17. 2-Microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro, J. Mol. Biol. 313, 559-571.
18. Yamaguchi, I., Hasegawa, K., Takahashi, N., Gejyo, F., and Naiki, H. (2001) Apolipoprotein E inhibits the depolymerization of β2-microglobulin- related amyloid fibrils at a neutral pH, Biochemistry 40, 8499-8507.
19. Yamamoto, S., Yamaguchi, I., Hasegawa, K., Tsutsumi, S., Goto, Y., Gejyo, F., and Naiki, H. (2004) Glycosaminoglycans enhance the trifluoroethanol- induced extension of β2-microglobulin-related amyloid fibrils at a neutral pH, J. Am. Soc. Nephrol. 15, 126-133.
20. Kelly, J. W. (1996) Alternative conformations of amyloidogenic proteins govern their behavior, Curr. Opin. Struct. Biol. 6, 11-17.
21. 2-microglobulin amyloid fibril by H/D exchange, Nat. Struct. Biol. 9, 332-336.
22. Ohishi, H., Skinner, M., Sato-Araki, N., Okuyama, T., Gejyo, F., Kimura, A., Cohen, A. S., and Schmid, K. (1990) Glycosaminoglycans of the hemodialysis-associated carpal synovial amyloid and of amyloid-rich tissues and fibrils of heart, liver, and spleen, Clin. Chem. 36, 88-91.
23. Ohashi, K., Hara, M., Yanagishita, M., Kawai, R., Tachibana, S., and Ogura, Y. (1995) Proteoglycans in haemodialysis-related amyloidosis, Virchows Arch. 427, 49-59.
24. Yamada, T., Kakihara, T., Gejyo, F., and Okada, M. (1994) A monoclonal antibody recognizing apolipoprotein E peptides in systemic amyloid deposits, Ann. Clin. Lab. Sci. 24, 243-249.
25. García-García, M., García-Valero, J., Mourad, G., and Argilés, A. (1994) Protein constituents of amyloid deposits in beta 2-microglobulin amyloidosis, Rev. Rhum. [Engl. Ed.] 61 (Suppl. 9), 7-11.
26. 2-microglobulin amyloid deposits, Kidney Int. 42, 915-923.
27. 2-microglobulin amyloid deposition in the vertebral column, Kidney Int. 41, 1646-1652.
28. Garbar, C., Jadoul, M., Noël, H., and van Ypersele de Strihou, C. (1999) Histological characteristics of sternoclavicular β2-microglobulin amyloidosis and clues for its histogenesis, Kidney Int. 55, 1983-1990.
29. 2-microglobulin amyloid fibrils in vitro, Kidney Int. 64, 1080-1088.
30. Andreola, A., Bellotti, V., Giorgetti, S., Mangione, P., Obici, L., Stoppini, M., Torres, J., Monzani, E., Merlini, G., and Sunde, M. (2003) Conformational switching and fibrillogenesis in the amyloidogenic fragment of apolipoprotein A-I, J. Biol. Chem. 278, 2444-2451.
31. Morillas, M., Swietnicki, W., Gambetti, P., and Surewicz, W. K. (1999) Membrane environment alters the conformational structure of the recombinant human prion protein, J. Biol. Chem. 274, 36859-36865.
32. Ji, S., Wu, Y., and Sui, S. (2002) Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (Aβ1-40), which may potentially inhibit the fibril formation, J. Biol. Chem. 277, 6273-6279.
33. Reynolds, J. A., and Tanford, C. (1970) The gross conformation of protein-sodium dodecyl sulfate complexes, J. Biol. Chem. 245, 5161-5165.
34. Jirgensons, B. (1967) Effect of n-propyl alcohol and detergents on the optical rotatory dispersion of α-chymotrypsinogen, β-casein, histone fraction F1, and soybean trypsin inhibitor, J. Biol. Chem. 242, 912-918.
35. Mattice, W. L., Riser, J. M., and Clark, D. S. (1976) Conformational properties of the complexes formed by proteins and sodium dodecyl sulfate, Biochemistry 15, 4264-4272.
36. Yonath, A., Podjarny, A., Honig, B., Sielecki, A., and Traub, W. (1977) Crystallographic studies of protein denaturation and renaturation. 2. Sodium dodecyl sulfate induced structural changes in triclinic lysozyme, Biochemistry 16, 1418-1424.
37. 2-glycoprotein I induced by sodium lauryl sulfate and lysophospholipids, Biochemistry 41, 1020-1026.
38. Pertinhez, T. A., Bouchard, M., Smith, R. A. G., Dobson, C. M., and Smith, L. J. (2002) Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS, FEBS lett. 529, 193-197.
39. 2-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH, J. Biochem. 131, 45-52.
40. Yamaguchi, I., Hasegawa, K., Naiki, H., Mitsu, T., Matuo, Y., and Gejyo, F. (2001) Extension of Aβ2M amyloid fibrils with recombinant human β2-microglobulin, Amyloid: J. Protein Folding Disord. 8, 30-40.
41. Ortner, M. J., Sik, R. H., Chignell, C. F., and Sokoloski, E. A. (1979) A nuclear magnetic resonance study of compound 48/80, Mol. Pharmacol. 15, 179-188.
42. Sreerama, N., and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set, Anal. Biochem. 287, 252-260.
43. Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., and Klenk, D. C. (1985) Measurement of protein using bicinchoninic acid, Anal. Biochem. 150, 76-85.
44. Helenius, A., McCaslin, D. R., Fries, E., and Tanford, C. (1979) Properties of detergents, Methods Enzymol. 54, 734-749.
45. 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.
46. Buck, M. (1998) Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins, Q. Rev. Biophy. 31, 297-355.
47. Shiraki, K., Nishikawa, K., and Goto, Y. (1995) Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: implication for nonhierarchical protein folding, J. Mol. Biol. 245, 180-194.
48. Hamada, D., Chiti, F., Guijarro, J. I., Kataoka, M., Taddei, N., and Dobson, C. M. (2000) Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol, Nat. Struct. Biol. 7, 58-61.
49. 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.
50. Shao, H., Jao, S., Ma, K., and Zagorski, M. G. (1999) Solution structures of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer's disease, J. Mol. Biol. 285, 755-773.
51. Yanagisawa, K., Odaka, A., Suzuki, N., and Ihara, Y. (1995) GM1 ganglioside-bound amyloid β-protein (Aβ): a possible form of preamyloid in Alzheimer's disease, Nat. Med. 1, 1062-1066.
52. Kakio, A., Nishimoto, S., Yanagisawa, K., Kozutsumi, Y., and Matsuzaki, K. (2001) Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid, J. Biol. Chem. 276, 24985-24990.
53. Sasagawa, T., Suzuki, K., Shiota, T., Kondo, T., and Okita, M. (1998) The significance of plasma lysophospholipids in patients with renal failure on hemodialysis, J. Nutr. Sci. Vitaminol. 44, 809-818.