Aβ-globulomers are formed independently of the fibril pathway

Neurobiology of Disease

Volumn 30, Issue 2, 2008, Pages 212-220

  Gellermann, Gerald P ^a   Byrnes, Helga ^a   Striebinger, Andreas ^a   Ullrich, Kathrin ^b   Mueller, Reinhold ^a   Hillen, Heinz ^a   Barghorn, Stefan ^a  

^a ABBOTT GMBH AND CO KG   (Germany)

^b FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

Author keywords

Alzheimer's disease; Conformational diseases; Dementia, Amyloid protein; Fibrils; Monocyte; Oligomers

Indexed keywords

AMYLOID BETA GLOBULOMER; AMYLOID BETA PROTEIN; CONGO RED; THIOFLAVINE; AMYLOID; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

ALZHEIMER DISEASE; ARTICLE; FIBER; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE; SENILE PLAQUE; AMYLOID PLAQUE; ANIMAL; ASTROCYTE; C57BL MOUSE; CELL CULTURE; CHEMISTRY; COMPARATIVE STUDY; METABOLISM; MOUSE; NEUROFIBRILLARY TANGLE; PATHOLOGY; PHYSIOLOGY; SIGNAL TRANSDUCTION;

ALZHEIMER DISEASE; AMYLOID; AMYLOID BETA-PEPTIDES; ANIMALS; ASTROCYTES; CELLS, CULTURED; MICE; MICE, INBRED C57BL; NEUROFIBRILLARY TANGLES; PEPTIDE FRAGMENTS; PLAQUE, AMYLOID; PROTEIN CONFORMATION; SIGNAL TRANSDUCTION;

EID: 43049131763     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbd.2008.01.010     Document Type: Article

References (54)

1. Antzutkin O.N., Leapman R.D., Balbach J.J., and Tycko R. Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance. Biochemistry 41 (2002) 15436-15450
2. Bard F., Cannon C., Barbour R., Burke R.L., Games D., Grajeda H., Guido T., Hu K., Huang J., Johnson-Wood K., Khan K., Kholodenko D., Lee M., Lieberburg I., Motter R., Nguyen M., Soriano F., Vasquez N., Weiss K., Welch B., Seubert P., Schenk D., and Yednock T. Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat. Med. 6 (2000) 916-919
3. Barghorn S., Nimmrich V., Striebinger A., Krantz C., Keller P., Janson B., Bahr M., Schmidt M., Bitner R.S., Harlan J., Barlow E., Ebert U., and Hillen H. Globular amyloid beta-peptide oligomer - a homogenous and stable neuropathological protein in Alzheimer's disease. J. Neurochem. 95 (2005) 834-847
4. Baskakov I.V., Legname G., Baldwin M.A., Prusiner S.B., and Cohen F.E. Pathway complexity of prion protein assembly into amyloid. J. Biol. Chem. 277 (2002) 21140-21148
5. Bateman R.J., Munsell L.Y., Morris J.C., Swarm R., Yarasheski K.E., and Holtzman D.M. Human amyloid-beta synthesis and clearance rates as measured in cerebrospinal fluid in vivo. Nat. Med. 12 (2006) 856-861
6. Carulla N., Caddy G.L., Hall D.R., Zurdo J., Gairi M., Feliz M., Giralt E., Robinson C.V., and Dobson C.M. Molecular recycling within amyloid fibrils. Nature 436 (2005) 554-558
7. Caughey B., and Lansbury P.T. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26 (2003) 267-298
8. Cerda-Costa N., Esteras-Chopo A., Aviles F.X., Serrano L., and Villegas V. Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates. J. Mol. Biol. 366 (2007) 1351-1363
9. Chung H., Brazil M.I., Soe T.T., and Maxfield F.R. Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid beta-peptide by microglial cells. J. Biol. Chem. 274 (1999) 32301-32308
10. Cohen E., Bieschke J., Perciavalle R.M., Kelly J.W., and Dillin A. Opposing activities protect against age-onset proteotoxicity. Science 313 (2006) 1604-1610
11. Elimova E., Kisilevsky R., Szarek W.A., and Ancsin J.B. Amyloidogenesis recapitulated in cell culture: a peptide inhibitor provides direct evidence for the role of heparan sulfate and suggests a new treatment strategy. FASEB J. 18 (2004) 1749-1751
12. Gellermann G.P., Appel T.R., Tannert A., Radestock A., Hortschansky P., Schroeckh V., Leisner C., Lutkepohl T., Shtrasburg S., Rocken C., Pras M., Linke R.P., Diekmann S., and Fandrich M. Raft lipids as common components of human extracellular amyloid fibrils. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 6297-6302
13. Gellermann G.P., Ullrich K., Tannert A., Unger C., Habicht G., Sauter S.R., Hortschansky P., Horn U., Mollmann U., Decker M., Lehmann J., and Fandrich M. Alzheimer-like plaque formation by human macrophages is reduced by fibrillation inhibitors and lovastatin. J. Mol. Biol. 360 (2006) 251-257
14. Gellermann G.P., Ullrich K., Unger C., Fandrich M., Sauter S., and Diekmann S. Identification of molecular compounds critical to Alzheimer's-like plaque formation. J. Neurosci. Res. 85 (2007) 2037-2044
15. Goedert M., and Spillantini M.G. A century of Alzheimer's disease. Science 314 (2006) 777-781
16. Goldsbury C., Frey P., Olivieri V., Aebi U., and Muller S.A. Multiple assembly pathways underlie amyloid-beta fibril polymorphisms. J. Mol. Biol. 352 (2005) 282-298
17. Gong Y., Chang L., Viola K.L., Lacor P.N., Lambert M.P., Finch C.E., Krafft G.A., and Klein W.L. Alzheimer's disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 10417-10422
18. Gosal W.S., Morten I.J., Hewitt E.W., Smith D.A., Thomson N.H., and Radford S.E. Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. J. Mol. Biol. 351 (2005) 850-864
19. Gsponer J., and Caflisch A. Molecular dynamics simulations of protein folding from the transition state. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 6719-6724
20. Haass C., and Selkoe D.J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev., Mol. Cell Biol. 8 (2007) 101-112
21. Heiser V., Engemann S., Brocker W., Dunkel I., Boeddrich A., Waelter S., Nordhoff E., Lurz R., Schugardt N., Rautenberg S., Herhaus C., Barnickel G., Bottcher H., Lehrach H., and Wanker E.E. Identification of benzothiazoles as potential polyglutamine aggregation inhibitors of Huntington's disease by using an automated filter retardation assay. Proc. Natl. Acad. Sci. U. S. A. 99 Suppl 4 (2002) 16400-16406
22. Hepler R.W., Grimm K.M., Nahas D.D., Breese R., Dodson E.C., Acton P., Keller P.M., Yeager M., Wang H., Shughrue P., Kinney G., and Joyce J.G. Solution state characterization of amyloid beta-derived diffusible ligands. Biochemistry 45 (2006) 15157-15167
23. Kayed R., Head E., Thompson J.L., McIntire T.M., Milton S.C., Cotman C.W., and Glabe C.G. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300 (2003) 486-489
24. Kisilevsky R. Review: amyloidogenesis-unquestioned answers and unanswered questions. J. Struct. Biol. 130 (2000) 99-108
25. Kluve-Beckerman B., Liepnieks J.J., Wang L., and Benson M.D. A cell culture system for the study of amyloid pathogenesis. Amyloid formation by peritoneal macrophages cultured with recombinant serum amyloid A. Am. J. Pathol. 155 (1999) 123-133
26. Kluve-Beckerman B., Manaloor J.J., and Liepnieks J.J. A pulse-chase study tracking the conversion of macrophage-endocytosed serum amyloid A into extracellular amyloid. Arthritis Rheum. 46 (2002) 1905-1913
27. Krebs M.R., Bromley E.H., and Donald A.M. The binding of thioflavin-T to amyloid fibrils: localisation and implications. J. Struct. Biol. 149 (2005) 30-37
28. Kuo Y.M., Emmerling M.R., Vigo-Pelfrey C., Kasunic T.C., Kirkpatrick J.B., Murdoch G.H., Ball M.J., and Roher A.E. Water-soluble Abeta (N-40, N-42) oligomers in normal and Alzheimer disease brains. J. Biol. Chem. 271 (1996) 4077-4081
29. Lacor P.N., Buniel M.C., Furlow P.W., Clemente A.S., Velasco P.T., Wood M., Viola K.L., and Klein W.L. Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J. Neurosci. 27 (2007) 796-807
30. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
31. Lambert M.P., Barlow A.K., Chromy B.A., Edwards C., Freed R., Liosatos M., Morgan T.E., Rozovsky I., Trommer B., Viola K.L., Wals P., Zhang C., Finch C.E., Krafft G.A., and Klein W.L. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 6448-6453
32. Lansbury Jr. P.T. Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 3342-3344
33. Lesne S., Koh M.T., Kotilinek L., Kayed R., Glabe C.G., Yang A., Gallagher M., and Ashe K.H. A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440 (2006) 352-357
34. LeVine III H. Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309 (1999) 274-284
35. Lorenzo A., and Yankner B.A. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 12243-12247
36. Lue L.F., Kuo Y.M., Roher A.E., Brachova L., Shen Y., Sue L., Beach T., Kurth J.H., Rydel R.E., and Rogers J. Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am. J. Pathol. 155 (1999) 853-862
37. Ma B., and Nussinov R. Simulations as analytical tools to understand protein aggregation and predict amyloid conformation. Curr. Opin. Chem. Biol. 10 (2006) 445-452
38. Masters C.L., Simms G., Weinman N.A., Multhaup G., McDonald B.L., and Beyreuther K. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 4245-4249
39. McLean C.A., Cherny R.A., Fraser F.W., Fuller S.J., Smith M.J., Beyreuther K., Bush A.I., and Masters C.L. Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann. Neurol. 46 (1999) 860-866
40. Necula M., Breydo L., Milton S., Kayed R., van der Veer W.E., Tone P., and Glabe C.G. Methylene blue inhibits amyloid Abeta oligomerization by promoting fibrillization. Biochemistry 46 (2007) 8850-8860
41. Necula M., Kayed R., Milton S., and Glabe C.G. Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct. J. Biol. Chem. 282 (2007) 10311-10324
42. Nguyen H.D., and Hall C.K. Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 16180-16185
43. Pellarin R., and Caflisch A. Interpreting the aggregation kinetics of amyloid peptides. J. Mol. Biol. 360 (2006) 882-892
44. Petkova A.T., Leapman R.D., Guo Z., Yau W.M., Mattson M.P., and Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307 (2005) 262-265
45. Poduslo J.F., Curran G.L., Kumar A., Frangione B., and Soto C. Beta-sheet breaker peptide inhibitor of Alzheimer's amyloidogenesis with increased blood-brain barrier permeability and resistance to proteolytic degradation in plasma. J. Neurobiol. 39 (1999) 371-382
46. Pollack S.J., Sadler I.I., Hawtin S.R., Tailor V.J., and Shearman M.S. Sulfonated dyes attenuate the toxic effects of beta-amyloid in a structure-specific fashion. Neurosci. Lett. 197 (1995) 211-214
47. Puchtler H., and Sweat F. Congo red as a stain for fluorescence microscopy of amyloid. J. Histochem. Cytochem. 13 (1965) 693-694
48. Rocken C., and Shakespeare A. Pathology, diagnosis and pathogenesis of AA amyloidosis. Virchows Arch. 440 (2002) 111-122
49. Schenk D., Hagen M., and Seubert P. Current progress in beta-amyloid immunotherapy. Curr. Opin. Immunol. 16 (2004) 599-606
50. Shankar G.M., Bloodgood B.L., Townsend M., Walsh D.M., Selkoe D.J., and Sabatini B.L. Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J. Neurosci. 27 (2007) 2866-2875
51. Tomiyama T., Asano S., Suwa Y., Morita T., Kataoka K., Mori H., and Endo N. Rifampicin prevents the aggregation and neurotoxicity of amyloid beta protein in vitro. Biochem. Biophys. Res. Commun. 204 (1994) 76-83
52. Townsend M., Cleary J.P., Mehta T., Hofmeister J., Lesne S., O'Hare E., Walsh D.M., and Selkoe D.J. Orally available compound prevents deficits in memory caused by the Alzheimer amyloid-beta oligomers. Ann. Neurol. 60 (2006) 668-676
53. Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., Rowan M.J., and Selkoe D.J. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002) 535-539
54. Wood S.J., MacKenzie L., Maleeff B., Hurle M.R., and Wetzel R. Selective inhibition of Abeta fibril formation. J. Biol. Chem. 271 (1996) 4086-4092