Fibril structure of human islet amyloid polypeptide

Journal of Biological Chemistry

Volumn 287, Issue 8, 2012, Pages 5235-5241

  Bedrood, Sahar ^a   Li, Yiyu ^b   Isas, J Mario ^a   Hegde, Balachandra G ^a   Baxa, Ulrich ^c,d   Haworth, Ian S ^b   Langen, Ralf ^a  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^b UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^c NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES   (United States)

^d NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL FORMATION; CONTINUOUS WAVE; FIBRIL FORMATION; FIBRIL STRUCTURE; HELICAL TWIST; HUMAN ISLETS; MISFOLDING; OUT-OF-PLANE; PROTOFILAMENTS; PULSED EPR; RELATIVE ORIENTATION; SECONDARY STRUCTURE ELEMENTS; SECONDARY STRUCTURES; SITE-DIRECTED SPIN LABELING; STRUCTURAL MODELS; TYPE-2 DIABETES;

GLYCOPROTEINS; MODEL STRUCTURES; MONOMERS;

POLYPEPTIDES;

AMYLIN;

ARTICLE; ATOMISTIC STRUCTURAL MODEL; BETA SHEET; CONTROLLED STUDY; ELECTRON MICROSCOPY; ELECTRON SPIN RESONANCE; MOLECULAR DYNAMICS; PHYSICAL MODEL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SPIN LABELING; STRUCTURE ANALYSIS;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; CELL MEMBRANE; ELECTRON SPIN RESONANCE SPECTROSCOPY; HUMANS; ISLET AMYLOID POLYPEPTIDE; MICROSCOPY, ELECTRON; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY;

EID: 84863116618     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.327817     Document Type: Article

References (34)

1. Stefani, M. (2004) Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim. Biophys. Acta 1739, 5-25
2. Clark, A., Lewis, C. E., Willis, A. C., Cooper, G. J., Morris, J. F., Reid, K. B., and Turner, R. C. (1987) Islet amyloid formed from diabetes-associated peptide may be pathogenic in type-2 diabetes. Lancet 330, 231-234
3. Clark, A., de Koning, E. J., Hattersley, A. T., Hansen, B. C., Yajnik, C. S., and Poulton, J. (1995) Pancreatic pathology in non-insulin-dependent diabetes (NIDDM). Diabetes Res. Clin. Pract. 28, S39-47
4. Westermark, P., Wernstedt, C., Wilander, E., Hayden, D. W., O'Brien, T. D., and Johnson, K. H. (1987) Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc. Natl. Acad. Sci. U.S.A. 84, 3881-3885 (Pubitemid 17088383)
5. Westermark, P., Wilander, E., and Johnson, K. H. (1987) Islet amyloid polypeptide. Lancet 2, 623 (Pubitemid 17123407)
6. Ahrén, B., Oosterwijk, C., Lips, C. J., and Höppener, J. W. (1998) Transgenic overexpression of human islet amyloid polypeptide inhibits insulin secretion and glucose elimination after gastric glucose gavage in mice. Diabetologia 41, 1374-1380
7. Gebre-Medhin, S., Mulder, H., Pekny, M., Westermark, G., Törnell, J., Westermark, P., Sundler, F., Ahrén, B., and Betsholtz, C. (1998) Increased insulin secretion and glucose tolerance in mice lacking islet amyloid polypeptide (amylin). Biochem. Biophys. Res. Commun. 250, 271-277 (Pubitemid 28463867)
8. Kahn, S. E., D'Alessio, D. A., Schwartz, M. W., Fujimoto, W. Y., Ensinck, J. W., Taborsky, G. J., Jr., and Porte, D., Jr. (1990) Evidence of co-secretion of islet amyloid polypeptide and insulin by β-cells. Diabetes 39, 634-638 (Pubitemid 20223792)
9. Young, A. (2005) Inhibition of food intake. Adv. Pharmacol. 52, 79-98
10. Butler, A. E., Jang, J., Gurlo, T., Carty, M. D., Soeller, W. C., and Butler, P. C. (2004) Diabetes due to a progressive defect in β-cell mass in rats transgenic for human islet amyloid polypeptide (HIP Rat): a new model for type 2 diabetes. Diabetes 53, 1509-1516 (Pubitemid 38697663)
11. Cooper, G. J., Willis, A. C., Clark, A., Turner, R. C., Sim, R. B., and Reid, K. B. (1987) Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc. Natl. Acad. Sci. U.S.A. 84, 8628-8632 (Pubitemid 18033465)
12. Janson, J., Soeller, W. C., Roche, P. C., Nelson, R. T., Torchia, A. J., Kreutter, D. K., and Butler, P. C. (1996) Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide. Proc. Natl. Acad. Sci. U.S.A. 93, 7283-7288 (Pubitemid 26243541)
13. Kahn, S.E., Andrikopoulos, S., and Verchere, C.B. (1999) Islet amyloid: a long-recognized but underappreciated pathological feature of type 2 diabetes. Diabetes 48, 241-253 (Pubitemid 29061094)
14. Higham, C. E., Jaikaran, E. T., Fraser, P. E., Gross, M., and Clark, A. (2000) Preparation of synthetic human islet amyloid polypeptide (IAPP) in a stable conformation to enable study of conversion to amyloid-like fibrils. FEBS Lett. 470, 55-60 (Pubitemid 30155623)
15. Radovan, D., Smirnovas, V., and Winter, R. (2008) Effect of pressure on islet amyloid polypeptide aggregation: revealing the polymorphic nature of the fibrillation process. Biochemistry 47, 6352-6360 (Pubitemid 351874226)
16. Sumner Makin, O., and Serpell, L. C. (2004) Structural characterization of islet amyloid polypeptide fibrils. J. Mol. Biol. 335, 1279-1288
17. Jayasinghe, S. A., and Langen, R. (2004) Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling. J. Biol. Chem. 279, 48420-48425 (Pubitemid 39540999)
18. Goldsbury, C. S., Cooper, G. J., Goldie, K. N., Müller, S. A., Saafi, E. L., Gruijters, W. T., Misur, M. P., Engel, A., Aebi, U., and Kistler, J. (1997) Polymorphic fibrillar assembly of human amylin. J. Struct. Biol. 119, 17-27 (Pubitemid 27294718)
19. Luca, S., Yau, W. M., Leapman, R., and Tycko, R. (2007) Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. Biochemistry 46, 13505-13522 (Pubitemid 350209947)
20. Wiltzius, J. J., Sievers, S. A., Sawaya, M. R., Cascio, D., Popov, D., Riekel, C., and Eisenberg, D. (2008) Atomic structure of the cross-β-spine of islet amyloid polypeptide (amylin). Protein Sci. 17, 1467-1474
21. Kajava, A. V., Aebi, U., and Steven, A. C. (2005) The parallel superpleated β-structure as a model for amyloid fibrils of human amylin. J. Mol. Biol. 348, 247-252 (Pubitemid 40462093)
22. Jao, C. C., Hegde, B. G., Chen, J., Haworth, I. S., and Langen, R. (2008) Structure of membrane-bound α-synuclein from site-directed spin labeling and computational refinement. Proc. Natl. Acad. Sci. U.S.A. 105, 19666-19671
23. Chiang, Y. W., Borbat, P. P., and Freed, J. H. (2005) The determination of pair distance distributions by pulsed ESR using Tikhonov regularization. J. Magn. Reson. 172, 279-295 (Pubitemid 40072533)
24. Jeschke, G., Chechik, V., Ionita, P., Godt, A., Zimmermann, H., Banham, J., Timmel, C. R., Hilger, D., and Jung, H. (2006) DeerAnalysis2006: a comprehensive software package for analyzing pulsed ELDOR data Appl. Magn. Reson. 30, 473-498
25. Mchaourab, H. S., Lietzow, M. A., Hideg, K., and Hubbell, W. L. (1996) Motion of spin-labeled side chains in T4 lysozyme: correlation with protein structure and dynamics. Biochemistry 35, 7692-7704 (Pubitemid 26202511)
26. Hatmal, M. M., Li, Y., Hegde, B. G., Hegde, P. B., Jao, C. C., Langen, R., and Haworth, I. S. (2012) Computer modeling of nitroxide spin labels on proteins. Biopolymers 97, 35-44
27. Case, D. A., Cheatham, T. E., 3rd, Darden, T., Gohlke, H., Luo, R., Merz, K. M., Jr., Onufriev, A., Simmerling, C., Wang, B., and Woods, R. J. (2005) The Amber biomolecular simulation programs. J. Comput. Chem. 26, 1668-1688 (Pubitemid 43076180)
28. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
29. Antzutkin, O. N., Leapman, R. D., Balbach, J. J., and Tycko, R. (2002) Supramolecular structural constraints on Alzheimer β-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance. Biochemistry 41, 15436-15450 (Pubitemid 36008156)
30. Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D., and Riek, R. (2005) Three-dimensional structure of Alzheimer amyloid-β(1-42) fibrils. Proc. Natl. Acad. Sci. U.S.A. 102, 17342-17347 (Pubitemid 41740868)
31. Petkova, A. T., Ishii, Y., Balbach, J. J., Antzutkin, O. N., Leapman, R. D., Delaglio, F., and Tycko, R. (2002) A structural model for Alzheimer β-amyloid fibrils based on experimental constraints from solid-state NMR. Proc. Natl. Acad. Sci. U.S.A. 99, 16742-16747 (Pubitemid 36034043)
32. Petkova, A. T., Yau, W. M., and Tycko, R. (2006) Experimental constraints on quaternary structure in Alzheimer β-amyloid fibrils. Biochemistry 45, 498-512 (Pubitemid 43100415)
33. Török, M., Milton, S., Kayed, R., Wu, P., McIntire, T., Glabe, C. G., and Langen, R. (2002) Structural and dynamic features of Alzheimer Aβ peptide in amyloid fibrils studied by site-directed spin labeling. J. Biol. Chem. 277, 40810-40815 (Pubitemid 35215666)
34. Jao, C. C., Hegde, B. G., Gallop, J. L., Hegde, P. B., McMahon, H. T., Haworth, I. S., and Langen, R. (2010) Roles of amphipathic helices and the bin/amphiphysin/rvs (BAR) domain of endophilin in membrane curvature generation. J. Biol. Chem. 285, 20164-20170