Polymorphism of Amyloid Fibrils In Vivo

作者: Karthikeyan Annamalai , Karl-Heinz Gührs , Rolf Koehler , Matthias Schmidt , Henri Michel

DOI: 10.1002/ANIE.201511524

关键词:

摘要: Polymorphism is a wide-spread feature of amyloid-like fibrils formed in vitro, but it has so far remained unclear whether the within patient are also affected by this phenomenon. In study we show that amyloid diseased individual can vary considerably their three-dimensional architecture. We demonstrate heterogeneity with deposited different organs, from sequentially non-homologous polypeptide chains and affecting human or animals. Irrespective type source, found vivo to be polymorphic. These data imply chemical principles fibril assembly lead such polymorphism fundamentally conserved vitro.

参考文章(23)
JoAnne McLaurin, Trudy Franklin, Xiaoqiong Zhang, Jianping Deng, Paul E. Fraser, Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth. FEBS Journal. ,vol. 266, pp. 1101- 1110 ,(1999) , 10.1046/J.1432-1327.1999.00957.X
Marcus Fändrich, Jessica Meinhardt, Nikolaus Grigorieff, Structural polymorphism of Alzheimer Aβ and other amyloid fibrils Prion. ,vol. 3, pp. 89- 93 ,(2009) , 10.4161/PRI.3.2.8859
Joakim Bergström, Åsa Gustavsson, Ulf Hellman, Knut Sletten, Charles L Murphy, Deborah T Weiss, Alan Solomon, Bert-Ove Olofsson, Per Westermark, Amyloid deposits in transthyretin-derived amyloidosis: cleaved transthyretin is associated with distinct amyloid morphology. The Journal of Pathology. ,vol. 206, pp. 224- 232 ,(2005) , 10.1002/PATH.1759
Jessica Meinhardt, Carsten Sachse, Peter Hortschansky, Nikolaus Grigorieff, Marcus Fändrich, Aβ(1-40) Fibril Polymorphism Implies Diverse Interaction Patterns in Amyloid Fibrils Journal of Molecular Biology. ,vol. 386, pp. 869- 877 ,(2009) , 10.1016/J.JMB.2008.11.005
Claire S. Goldsbury, Garth J.S. Cooper, Kenneth N. Goldie, Shirley A. Müller, Etuate L. Saafi, W.T.M. Gruijters, Martin P. Misur, Andreas Engel, Ueli Aebi, Joerg Kistler, Polymorphic fibrillar assembly of human amylin Journal of Structural Biology. ,vol. 119, pp. 17- 27 ,(1997) , 10.1006/JSBI.1997.3858
Karolin Klement, Karin Wieligmann, Jessica Meinhardt, Peter Hortschansky, Walter Richter, Marcus Fändrich, Effect of Different Salt Ions on the Propensity of Aggregation and on the Structure of Alzheimer’s Aβ(1-40) Amyloid Fibrils Journal of Molecular Biology. ,vol. 373, pp. 1321- 1333 ,(2007) , 10.1016/J.JMB.2007.08.068
David Eisenberg, Mathias Jucker, The amyloid state of proteins in human diseases Cell. ,vol. 148, pp. 1188- 1203 ,(2012) , 10.1016/J.CELL.2012.02.022
Riccardo Pellarin, Philipp Schuetz, Enrico Guarnera, Amedeo Caflisch, Amyloid fibril polymorphism is under kinetic control. Journal of the American Chemical Society. ,vol. 132, pp. 14960- 14970 ,(2010) , 10.1021/JA106044U
Jean D. Sipe, Merrill D. Benson, Joel N. Buxbaum, Shu-ichi Ikeda, Giampaolo Merlini, Maria J. M. Saraiva, Per Westermark, Nomenclature 2014: Amyloid fibril proteins and clinical classification of the amyloidosis Amyloid. ,vol. 21, pp. 221- 224 ,(2014) , 10.3109/13506129.2014.964858
Adriano Aguzzi, Aaron D. Gitler, A Template for New Drugs against Alzheimer’s Disease Cell. ,vol. 154, pp. 1182- 1184 ,(2013) , 10.1016/J.CELL.2013.08.049