Conformational transitions and fibrillation mechanism of human calcitonin as studied by high-resolution solid-state 13C NMR

Protein Science

Volumn 9, Issue 5, 2000, Pages 867-877

  Kamihira, Miya ^a   Naito, Akira ^a   Tuzi, Satoru ^a   Nosaka, Atsuko Y ^b   Saitô, Hazime ^a  

^a UNIVERSITY OF HYOGO   (Japan)

^b CIBA GEIGY LTD   (Switzerland)

Author keywords

Autocatalytic reaction; Conformational transition; Fibril formation; Human calcitonin; Solid state 13C NMR

Indexed keywords

CALCITONIN;

AQUEOUS SOLUTION; ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; HUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS;

EID: 0034090046     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.5.867     Document Type: Article

References (51)

1. Arvinte T, Cudd A, Drake AF. 1993. The structure and mechanism of formation of human calcitonin fibrils. J Biol Chem 268:6415-6422.
2. Arvinte T, Ryman K. 1992. Pharmaceutical compositions comprising calcitonin. European Patent Application, Publication number 0490549A1.
3. Austin LA, Heath H. 1981. Calcitonin: Physiology and pathophysiology. N Engl J Med 304:269-278.
4. Bauer HH, Müller M, Goette J, Merkle HP, Fringeli UP. 1994. Interfacial adsorption and aggregation associated changes in secondary structure of human calcitonin monitored by ATR-FTIR spectroscopy. Biochemistry 33:12276-12282.
5. Cohen FE, Pan KM, Huang Z, Baldwin M, Fletterick RJ, Prusiner SB. 1994. Structural clues to prion replication. Science 264:530-531.
6. Copp DH. 1970. Endocrine regulation of calcium metabolism. Anna Rev Physiol 32:61-86.
7. Copp DH, Cameron EC, Cheney BA, Davidson AGF, Henze KG. 1962. Evidence for calcitonin. A new hormone from the parathyroid that lowers blood calcium. Endocrinology 70:638-649.
8. Dixon WT. 1982. Spinning-sideband-free and spinning-sideband-only NMR spectra in spinning samples. J Chem Phys 77:1800-1809.
9. Doi M, Kobayashi Y, Kyogoku Y, Takimoto M, Goda K. 1990. Structure study of human calcitonin. In: River JE, Marshall GR, eds. Peptides: Chemistry, structure & biology. La Jolla, California, 11th Proc Am Pept Symp, July 9-14, 1989, pp 165-167.
10. Ellman GL. 1959. Tissue sulfhydryl groups. Arch Biochem Biophys 82:70-77.
11. Epand RM, Epand RF, Orlowski RC, Schlueter RJ, Boni LT, Hui SW. 1983. Amphipathic helix and its relationship to the interaction of calcitonin with phospholipids. Biochemistry 22:5074-5084.
12. Ferrone FA, Hofrichter J, Eaton WA. 1985. Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism. J Mol Biol 183:631-631.
13. Ferrone FA, Hofrichter J, Sunshine HR, Eaton WA. 1980. Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism. Biophys J 32:361-380.
14. Goltzman D. 1980. Examination of interspecies differences in renal and skeletal receptor binding and adenylate cyclase stimulation with human calcitonin. Endocrinology 106:510-518.
15. Greenfield N, Fasman GD. 1969. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8:4108-4116.
16. Gullion T, Schaefer J. 1989. Rotational-echo double-resonance NMR. J Magn Reson 81:196-200.
17. Habener JF, Singer FR, Deftos LJ, Neer RM, Potts JT Jr. 1971. Explanation for unusual potency of salmon calcitonin. Nat New Biol 232:91-92.
18. 13C NMR spectroscopy. Macromolecules 23:88-94.
19. Jarrett JT, Berger EP, Lansbury PT Jr. 1993. The carbonyl terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implication for the pathogenesis of Alzheimer's disease. Biochemistry 32:4693-4697.
20. Jeon YH, Kanaori K, Takashima H, Kosiba T, Nosaka YA. 1998. Comparative studies on human calcitonin fibrillation in aqueous and trifluoroethanol solution by proton NMR spectroscopy. Proc ICMRBS XVIII. Tokyo, p 61.
21. Kanaori K, Nosaka AY. 1995. Study of human calcitonin fibrillation by proton nuclear magnetic resonance spectroscopy. Biochemistry 34:12138-12143.
22. 1H NMR spectroscopy. Biochemistry 35:12671-12676.
23. Kern D, Drakenberg T, Wikström M, Forsén S, Bang H, Fischer G. 1993. The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin. FEBS Lett 323:198-202.
24. Keutmann HT, Parsons JA, Potts JT Jr, Schlueter RJ. 1970. Isolation and chemical properties of two calcitonins from salmon ultimobranchial glands. J Biol Chem 245:1491-1496.
25. Kumar MA, Foster GV, MacIntyre I. 1963. Further evidence for calcitonin. A rapid-acting hormone which lowers plasma-calcium. Lancet 480-482.
26. Lomakin A, Chung DS, Benedek GB, Kirschner DA, Teplow DB. 1996. On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants. Proc Natl Acad Sci USA 93:125-1129.
27. Lomakin A, Teplow DB, Kirschner DA, Benedek GB. 1997. Kinetics theory of fibrillogenesis of amyloid β-protein. Proc Natl Acad Sci USA 94:7942-7947.
28. Meadows RP, Nikonowicz EP, Jones CR, Bastian JW, Gorenstein DG. 1991. Two-dimensional NMR and structure determination of salmon calcitonin in methanol. Biochemistry 30:1247-1254.
29. Meyer JP, Pelton JT, Hoflack J, Saudek V. 1991. Solution structure of salmon calcitonin. Biopolymers 31:233-241.
30. Motta A, Pastore A, Goud NA, Castiglione MM. 1991a. Solution conformation of salmon calcitonin in sodium dodecyl sulfate micelles as determined by two-dimensional NMR and distance geometry calculations. Biochemistry 30:10444-10450.
31. 1H NMR study of human calcitonin in solution. Biochemistry 30:2364-2371.
32. 13C REDOR, X-ray diffraction and molecular dynamics calculation. J Phys Chem 100:14995-15004.
33. 13C chemical shifts. J Phys Chem 102:7476-7483.
34. Orlowski RC, Epand RM, Stafford AR. 1987. Biologically potent analogues of salmon calcitonin which do not contain an N-terminal disulfide-bridged ring structure. Eur J Biochem 162:399-402.
35. Paquet A. 1982. Introduction of 9-fluorenylmethyloxycarbonyl, trichloroethoxycarbonyl, and benzyloxycarbonyl amine protecting groups into O-unprotected hydroxyamino acids using succinimidyl carbonates. Can J Chem 60:976-980.
36. Rittel W, Maier R, Brugger M, Kamber B, Riniker B, Sicber P. 1976. Structure-activity relationship of human calcitonin. III. Biological activity of synthetic analogues with shortened or terminally modified peptide chains. Experientia 32:246-248.
37. 13C chemical shifts: A new means of conformational characterization as obtained by high-resolution solid-state NMR. Magn Res Chem 24:835-852.
38. Saitô H, Ando I. 1989. High-resolution solid-state NMR studies of synthetic and biological macromolecules. Annu Rep NMR Spectrosc 21:209-290.
39. Saitô H, Tuzi S, Naito A. 1998. Empirical versus nonempirical evaluation of secondary structure of fibrous and membrane proteins by solid-state NMR: A practical approach. Annu Rep NMR Spectrosc 36:79-121.
40. Samuel RE, Salmon ED, Briehl RW. 1990. Nucleation and growth of fibres and gel formation in sickle cell haemoglohin. Nature 345:833-835.
41. Sieber P, Riniker B, Brugger M, Kamber B, Rittel W. 1970. Human calcitonin. VI. Synthesis of calcitonin M. Helv Chim Acta 53:2135-2150.
42. Sipe JD. 1992. Amyloidosis. Annu Rev Biochem 61:947-975.
43. 13C] Ala-labeled protein: Arg82 may function as an information mediator. Biophys J 77: 1577-1584.
44. Taubes G. 1996. Misfolding the way to disease. Science 271:1493-1495.
45. 13C magnetic resonance. Biopolymers 13:97-114.
46. 13C NMR. Biophys J 76:1523-1531.
47. 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J Biomol NMR 5:67-81.
48. Wishart DS, Sykes BD. 1994. Chemical shifts as a tool for structure determination. Methods Enzymol 239:363-392.
49. Wishart DS, Sykes BD, Richards FM. 1991. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol 222:311-333.
50. Wüthrich K. 1976. NMR in biological research: Peptides and proteins. Amsterdam, Holland: North-Holland Publishing Company, pp 65-72.
51. Zagorski MG, Barrow CJ. 1992. NMR studies of amyloid beta-peptides: Proton assignments, secondary structure, and mechanism of an alpha-helix → beta-sheet conversion for a homologous, 28-residue, N-terminal fragment. Biochemistry 31:5621-5631.