Amino acid sequence determinants and molecular chaperones in amyloid fibril formation

Biochemical and Biophysical Research Communications

Volumn 396, Issue 1, 2010, Pages 2-6

  Nerelius, Charlotte ^a   Fitzen, Michael ^a   Johansson, Jan ^b  

^a KAROLINSKA INSTITUTE   (Sweden)

^b SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

Author keywords

Alzheimer's disease; Brichos; Prion; Protein misfolding; Secondary structure; Surfactant protein C

Indexed keywords

ALPHA 2 MACROGLOBULIN; ALPHA CRYSTALLIN; AMYLOID; AMYLOID BETA PROTEIN; BETA CRYSTALLIN; CHAPERONE; CLUSTERIN; HAPTOGLOBIN; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PRION PROTEIN; SURFACTANT PROTEIN C;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOIDOSIS; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION;

AMINO ACID SEQUENCE; AMYLOID; AMYLOIDOSIS; HUMANS; MOLECULAR CHAPERONES; NEURODEGENERATIVE DISEASES; PROTEIN FOLDING; PULMONARY SURFACTANT-ASSOCIATED PROTEIN C;

EID: 77952307171     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.02.105     Document Type: Article

References (46)

1. Johansson J., Curstedt T., Robertson B., and Jörnvall H. Size and structure of the hydrophobic low molecular weight surfactant-associated polypeptide. Biochemistry 27 (1988) 3544-3547
2. Johansson J. Structure and properties of surfactant protein C. Biochim. Biophys. Acta 1408 (1998) 161-172
3. Szyperski T., Vandenbussche G., Curstedt T., Ruysschaert J.M., Wüthrich K., and Johansson J. Pulmonary surfactant-associated polypeptide C in a mixed organic solvent transforms from a monomeric α-helical state into insoluble β-sheet aggregates. Protein Sci. 7 (1998) 2533-2540
4. Gustafsson M., Thyberg J., Näslund J., Eliasson E., and Johansson J. Amyloid fibril formation by pulmonary surfactant protein C. FEBS Lett. 464 (1999) 138-142
5. Johansson J., Some M., Linderholm B.M., Almlén A., Curstedt T., and Robertson B. A synthetic surfactant based on a poly-Leu SP-C analog and phospholipids: effects on tidal volumes and lung gas volumes in ventilated immature newborn rabbits. J. Appl. Physiol. 95 (2003) 2055-2063
6. Nerelius C., Martin E., Peng S., Gustafsson M., Nordling K., Weaver T., and Johansson J. Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C. Biochem. J. 416 (2008) 201-209
7. Eanes E.D., and Glenner G.G. X-ray diffraction studies on amyloid filaments. J. Histochem. Cytochem. 16 (1968) 673-677
8. Fowler D.M., Koulov A.V., Balch W.E., and Kelly J.W. Functional amyloid - from bacteria to humans. Trends Biochem. Sci. 32 (2007) 217-224
9. Maji S.K., Perrin M.H., Sawaya M.R., Jessberger S., Vadodaria K., Rissman R.A., Singru P.S., Nilsson K.P., Simon R., Schubert D., Eisenberg D., Rivier J., Sawchenko P., Vale W., and Riek R. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325 (2009) 328-332
10. Hardy J., and Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 (2002) 353-356
11. Chiti F., Stefani M., Taddei N., Ramponi G., and Dobson C.M. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424 (2003) 805-808
12. Fernandez-Escamilla A.-M., Rousseau F., Schymkowitz J., and Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotech. 22 (2004) 1302-1306
13. Chiti F., Webster P., Taddei N., Clark A., Stefani M., Ramponi G., and Dobson C.M. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl. Acad. Sci. USA 96 (1999) 3590-3594
14. Tjernberg L., Hosia W., Bark N., Thyberg J., and Johansson J. Charge attraction and β propensity are necessary for amyloid fibril formation from tetrapeptides. J. Biol. Chem. 277 (2002) 43243-43246
15. Hosia W., Bark N., Liepinsh E., Tjernberg A., Persson B., Hallen D., Thyberg J., Johansson J., and Tjernberg L. Folding into a β-hairpin can prevent amyloid fibril formation. Biochemistry 43 (2004) 4655-4661
16. Gazit E. A possible role for π-stacking in the self-assembly of amyloid fibrils. FASEB J. 16 (2002) 77-83
17. Reches M., and Gazit E. Casting metal nanowires within discrete self-assembled peptide nanotubes. Science 300 (2003) 625-627
18. Sawaya M.R., Sambashivan S., Nelson R., Ivanova M., Sievers S.A., Apostol M.I., Thompson M.J., Balbirnie M., Wiltzius J.J.W., McFarlane H.T., Madsen A.Ø., Riekel C., and Eisenberg D. Atomic structures of amyloid cross-β spines reveal varied steric zippers. Nature 447 (2007) 453-457
19. Nelson R., Sawaya M.R., Balbirnie M., Madsen A.Ø., Riekel C., Grothe R., and Eisenberg D. Structure of the cross-β spine of amyloid-like fibrils. Nature 435 (2005) 747-749
20. Luhrs T., Ritter C., Adrian M., Riek-Loher D., Bohrmann B., Dobeli H., Schubert D., and Riek R. 3D structure of Alzheimer's amyloid-β(1-42) fibrils. Proc. Natl. Acad. Sci. USA 102 (2005) 17342-17347
21. Lopez de la Paz M., Lacroix E., Ramirez-Alvarado M., and Serrano L. Computer-aided design of β-sheet peptides. J. Mol. Biol. 312 (2001) 229-246
22. Kallberg Y., Gustafsson M., Persson B., Thyberg J., and Johansson J. Prediction of amyloid fibril-forming proteins. J. Biol. Chem. 276 (2001) 12945-12950
23. Li J., Hosia W., Hamvas A., Thyberg J., Jörnvall H., Weaver T.E., and Johansson J. The N-terminal propeptide of lung surfactant protein C is necessary for biosynthesis and prevents unfolding of a metastable α-helix. J. Mol. Biol. 338 (2004) 857-862
24. Hammarstrom P., Schneider F., and Kelly J.W. Trans-suppression of misfolding in an amyloid disease. Science 293 (2001) 2459-2462
25. Nerelius C., Sandegren A., Sargsyan H., Raunak R., Leijonmarck H., Chatterjee U., Fisahn A., Imarisio S., Lomas D.A., Crowther D.C., Strömberg R., and Johansson J. Α-helix targeting reduces amyloid-β peptide toxicity. Proc. Natl. Acad. Sci. USA 106 (2009) 9191-9196
26. Sanchez-Pulido L., Devos D., and Valencia A. BRICHOS: a conserved domain in proteins associated with dementia, respiratory distress and cancer. Trends Biochem. Sci. 27 (2002) 329-332
27. Nerelius C., Gustafsson M., Nordling K., Larsson A., and Johansson J. Anti-amyloid activity of the C-terminal domain of proSP-C against amyloid β-peptide and medin. Biochemistry 48 (2009) 3778-3786
28. Johansson H., Nerelius C., Nordling K., and Johansson J. Preventing amyloid formation by catching unfolded transmembrane segments. J. Mol. Biol. 389 (2009) 227-229
29. S. Peng, M. Fitzen, H. Jörnvall, J. Johansson, The extracellular domain of Bri2 (ITM2B) binds the ABri peptide (1-23) and amyloid β-peptide (Aβ1-40). Implications for Bri2 effects on processing of amyloid precursor protein and Aβ aggregation. Biochem. Biophys. Res. Commun. (2010). doi:10.1016/j.bbrc.2009.12.122.
30. Hamos J.E., Oblas B., Pulaski-Salo D., Welch W.J., Bole D.G., and Drachman D.A. Expression of heat shock proteins in Alzheimer's disease. Neurology 41 (1991) 345-350
31. Kakimura J., Kitamura Y., Takata K., Umeki M., Suzuki S., Shibagaki K., Taniguchi T., Nomura Y., Gebicke-Haerter P.J., Smith M.A., Perry G., and Shimohama S. Microglial activation and amyloid-β clearance induced by exogenous heat-shock proteins. FASEB J. 16 (2002) 601-603
32. Evans C.G., Wisen S., and Gestwicki J.E. Heat shock proteins 70 and 90 inhibit early stages of amyloid β-(1-42) aggregation in vitro. J. Biol. Chem. 281 (2006) 33182-33191
33. Dedmon M.M., Christodoulou J., Wilson M.R., and Dobson C.M. Heat shock protein 70 inhibits α-synuclein fibril formation via preferential binding to prefibrillar species. J. Biol. Chem. 280 (2005) 14733-14740
34. Arimon M., Grimminger V., Sanz F., and Lashuel H.A. Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Aβ fibrils and protofibrils. J. Mol. Biol. 384 (2008) 1157-1173
35. Shorter J., and Lindquist S. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304 (2004) 1793-1797
36. Wilhelmus M.M., Boelens W.C., Otte-Holler I., Kamps B., De Waal R.M., and Verbeek M.M. Small heat shock proteins inhibit amyloid-β protein aggregation and cerebrovascular amyloid-β protein toxicity. Brain Res. 1089 (2006) 67-78
37. Santhoshkumar P., and Sharma K.K. Inhibition of amyloid fibrillogenesis and toxicity by a peptide chaperone. Mol. Cell. Biochem. 267 (2004) 147-155
38. Yerbury J.J., Stewart E.M., Wyatt A.R., and Wilson M.R. Quality control of protein folding in extracellular space. EMBO Rep. 6 (2005) 1131-1136
39. Humphreys D.T., Carver J.A., Easterbrook-Smith S.B., and Wilson M.R. Clusterin has chaperone-like activity similar to that of small heat shock proteins. J. Biol. Chem. 274 (1999) 6875-6881
40. Yerbury J.J., Rybchyn M.S., Easterbrook-Smith S.B., Henriques C., and Wilson M.R. The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterin. Biochemistry 44 (2005) 10914-10925
41. 2-macroglobulin modulates a chaperone-like action with broad specificity. Biochemistry 47 (2008) 1176-1185
42. 2-macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species. J. Biol. Chem. 284 (2009) 4246-4254
43. Yerbury J.J., Poon S., Meehan S., Thompson B., Kumita J.R., Dobson C.M., and Wilson M.R. The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. FASEB J. 21 (2007) 2312-2322
44. Wilson M.R., Yerbury J.J., and Poon S. Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity. Mol. Biosyst. 4 (2008) 42-52
45. Wilhelmus M.M., Otte-Holler I., Wesseling P., De Waal R.M., Boelens W.C., and Verbeek M.M. Specific association of small heat shock proteins with the pathological hallmarks of Alzheimer's disease brains. Neuropathol. Appl. Neurobiol. 32 (2006) 119-130
46. 2-microglobulin. Biochem. J. 392 (2005) 573-581