Ultrastructural organization of ex vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant: An atomic force microscopy study

Biochimica et Biophysica Acta - Molecular Basis of Disease

Volumn 1690, Issue 1, 2004, Pages 33-41

  Relini, Annalisa ^a   Rolandi, Ranieri ^a   Bolognesi, Martino ^a,b   Aboudan, Manuela ^c,d   Merlini, Giampaolo ^c,d   Bellotti, Vittorio ^c,d   Gliozzi, Alessandra ^a  

^a UNIVERSITY OF GENOA   (Italy)

^b Ctr for Excellence in Biomed Res   (Italy)

^c UNIVERSITY OF PAVIA   (Italy)

^d FONDAZIONE IRCCS POLICLINICO SAN MATTEO   (Italy)

Author keywords

Amyloid; Apolipoprotein A I; Atomic force microscopy

Indexed keywords

AMYLOID; APOLIPOPROTEIN A; LEUCINE; SERINE;

AIR; ARTICLE; ATOMIC FORCE MICROSCOPY; CASE REPORT; HEART AMYLOIDOSIS; HEART TRANSPLANTATION; HISTOCOMPATIBILITY; HUMAN; HUMAN TISSUE; LIQUID; MORPHOLOGY; PRIORITY JOURNAL; ULTRASTRUCTURE;

AMYLOID; AMYLOIDOSIS, FAMILIAL; APOLIPOPROTEIN A-I; HUMANS; MICROSCOPY, ATOMIC FORCE; MYOCARDIUM; VARIATION (GENETICS);

EID: 4344678675     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2004.04.007     Document Type: Article

References (34)

1. Dobson C.M. Protein folding and its links with human disease. Biochem. Soc. Symp. 68:2001;1-26
2. Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M., Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 416:2002;507-511
3. Kelly J.W. Mechanisms of amyloidogenesis. Nat. Struct. Biol. 7:2000;824-826
4. Tjernberg L.O., Callaway D.J., Tjernberg A., Hahne S., Lilliehook C., Terenius L., Thyberg J., Nordstedt C. A molecular model of Alzheimer amyloid beta-peptide fibril formation. J. Biol. Chem. 274:1999;12619-12625
5. Antzuktin O.N., Leapman R.D., Balbach J.J., 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
6. Bauer H.H., Aebi U., Häner M., Hermann R., Müller M., Arvinte T., Merkle H.P. Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin. J. Struct. Biol. 115:1995;1-15
7. Kirschner D.A., Elliott-Bryant R., Szumowski K.E., Gonnerman W.A., Kindy M.S., Sipe J.D., Cathcart E.S. In vitro amyloid fibril formation by synthetic peptides corresponding to amino terminus of apoSAA isoforms from amyloid-susceptible and amyloid-resistant mice. J. Struct. Biol. 124:1998;88-98
8. Goldsbury C., Goldie K., Pellaud J., Seelig J., Frey P., Muller S.A., Kistler J., Cooper G.J., Aebi U. Amyloid fibril formation from full-length and fragments of amylin. J. Struct. Biol. 130:2000;352-362
9. Inouye H., Kirschner D.A. X-ray diffraction analysis of scrapie prion: intermediate and folded structures in a peptide containing two putative alpha-helices. J. Mol. Biol. 268:1997;375-389
10. Jiménez J.L., Guijarro J.I., Orlova E., Zurdo J., Dobson C.M., Sunde M., Saibil H.R. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18:1999;815-821
11. Ionescu-Zanetti C., Khurana R., Gillespie J.R., Petrick J.S., Trabachino L.C., Minert L.J., Carter S.A., Fink A.L. Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy. Proc. Natl. Acad. Sci. U. S. A. 96:1999;13175-13179
12. 2-microglobulin amyloid in vitro revealed by atomic force microscopy. J. Mol. Biol. 330:2003;785-797
13. Cardoso I., Goldsbury C.S., Muller S.A., Olivieri V., Wirtz S., Damas A., Aebi U., Saraiva M.J. Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils. J. Mol. Biol. 317:2002;683-695
14. Jimenez J.L., Tennent G., Pepys M., Saibil H.R. Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy. J. Mol. Biol. 311:2001;241-247
15. Hatters D.M., MacRaild C.A., Daniels R., Gosal W.S., Thomson N.H., Jones J.A., Davis J.J., MacPhee C.E., Dobson C.M., Howlett G.J. The circularization of amyloid fibrils formed by apolipoprotein C-II. Biophys. J. 85:2003;3979-3990
16. Chamberlain A.K., MacPhee C.E., Zurdo J., Morozova-Roche L., Hill H.A.O., Dobson J.J., Davis J.J. Ultrastructural organization of amyloid fibrils by atomic force microscopy. Biophys. J. 79:2000;3282-3293
17. Mangione P., Sunde M., Giorgetti S., Stoppini M., Esposito G., Gianelli L., Obici L., Asti L., Andreola A., Viglino P., Merlini G., Bellotti V. Amyloid fibrils derived from the apolipoprotein A-I Leu174Ser variant contain elements of ordered helical structure. Protein Sci. 10:2001;187-199
18. Serpell L.C., Sunde M., Benson M.D., Tennent G.A., Pepys M.B., Fraser P.E. The protofilament substructure of amyloid fibrils. J. Mol. Biol. 300:2000;1033-1039
19. 174→Ser causes hereditary cardiac amyloidosis, and the amyloid fibrils are constituted by the 93-residue N-terminal polypeptide. Am. J. Pathol. 155:1999;695-702
20. Pras M., Schubert D., Zucker-Franklin D., Rimon A., Franklin A.C. The characterization of soluble amyloid prepared in water. J. Clin. Invest. 47:1968;924-933
21. LeVine H. Quantification of β-sheet amyloid fibril structure Method. Enzymology. 309:1999;274-284
22. Andreola A., Bellotti V., Giorgetti S., Mangione P., Obici L., Stoppini M., Torres J., Monzani E., Merlini G., Sunde M. Conformational switching and fibrillogenesis in amyloidogenic fragment of apolipoprotein A-I. J. Biol. Chem. 278:2003;2444-2451
23. Watkins B.A., Feng S.L., Strom A.K., DeVitt A.A., Yu L., Li Y. Conjugated linoleic acids alter the fatty acid composition and physical properties of egg yolk and albumen. J. Agric. Food Chem. 51:2003;6870-6876
24. Ramirez-Aguilar K.A., Rowlen K.L. Tip characterization from AFM images of nanometric spherical particles. Langmuir. 14:1998;2562-2566
25. Perutz M.F., Finch J.T., Berriman J., Lesk A. Amyloid fibers are water filled nanotubes. Proc. Natl. Acad. Sci. U. S. A. 99:2002;5591-5595
26. Raiteri R., Martinoia S., Grattarola M. pH dependent charge density at the insulator-electrolyte interface probed by a scanning probe microscope. Biosens. Bioelectron. 11:1996;1009-1017
27. Müller D.J., Engel A. The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions. Biophys. J. 73:1997;1633-1644
28. Grégoire C., Marco S., Thimonier J., Duplan L., Laurine E., Chauvin J.-P., Michel B., Peyrot V., Verdier J.-M. Three-dimensional structure of lithostathine protofibril, a protein involved in Alzheimer's disease. EMBO J. 20:2001;3313-3321
29. Stefani M., Dobson C.M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81:2003;678-699
30. Harper J.D., Wong S.S., Lieber C.M., Lansbury P.T. Assembly of Aβ amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease. Biochemistry. 38:1999;8972-8980
31. Hoshi M., Sato M., Matsumoto S., Noguchi A., Yasutake K., Yoshida N., Sato K. Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β Proc. Natl. Acad. Sci. U. S. A. 100:2003;6370-6375
32. Kayed R., Head E., Thompson J.L., McIntire T.M., Milton S.C., Cotman C.W., Glabe C.G. Common structure of soluble amyloid oligomers implies common mechanisms of pathogenesis. Science. 300:2003;486-489
33. Relini A., Canale C., Torrassa S., Rolandi R., Gliozzi A., Rosano C., Bolognesi M., Plakoutsi G., Bucciantini M., Chiti F., Stefani M. Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. J. Mol. Biol. 338:2004;943-957
34. Antzutkin O.N. Amyloidosis of Alzheimer's A beta peptides: solid-state nuclear magnetic resonance, transmission electron microscopy, scanning trasmission electron microscopy and atomic force microscopy studies. Magn. Reson. Chem. 42:2004;231-246