scholarly journals 2P114 Amyloid fibril formation of a peptide fragment of transthyretin(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

2006 ◽  
Vol 46 (supplement2) ◽  
pp. S324
Author(s):  
Makoto Takeuchi ◽  
Mineyuki Mizuguchi ◽  
Mizuki Dobashi ◽  
Yoshihiro Mori ◽  
Hiroyuki Shinoda ◽  
...  
Keyword(s):  
Protein Folding ◽  
Poster Session ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Peptide Fragment ◽  
Meeting Program ◽  
Amyloid Fibril Formation

Dead-End Street of Protein Folding: Thermodynamic Rationale of Amyloid Fibril Formation

2007 ◽  
Vol 129 (48) ◽  
pp. 14959-14965 ◽  
Author(s):  
András Perczel ◽  
Péter Hudáky ◽  
Villö K. Pálfi
Keyword(s):  
Protein Folding ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Dead End

scholarly journals Amyloid as a natural product

2003 ◽  
Vol 161 (3) ◽  
pp. 461-462 ◽  
Author(s):  
Jeffery W. Kelly ◽  
William E. Balch
Keyword(s):  
Natural Product ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Integral Membrane Protein ◽  
Fibril Formation ◽  
Proteolytic Processing ◽  
Biological Pathway ◽  
Peptide Fragment ◽  
Amyloid Fibril Formation ◽  
Amyloid Diseases

Amyloid fibrils, such as those found in Alzheimer's and the gelsolin amyloid diseases, result from the misassembly of peptides produced by either normal or aberrant intracellular proteolytic processing. A paper in this issue by Marks and colleagues (Berson et al., 2003) demonstrates that intra-melanosome fibrils are formed through normal biological proteolytic processing of an integral membrane protein. The resulting peptide fragment assembles into fibrils promoting the formation of melanin pigment granules. These results, along with the observation that amyloid fibril formation by bacteria is highly orchestrated, suggest that fibril formation is an evolutionary conserved biological pathway used to generate natural product nanostructures.

Immunocytochemical Localization of Amyloid Protein AA in the “Dense Fibrillar Inclusions” of the Reticuloendothelical Cells

1977 ◽  
Vol 35 ◽  
pp. 438-439
Author(s):  
T. Shirahama ◽  
M. Skinner ◽  
A.S. Cohen
Keyword(s):  
Amyloid Fibril ◽  
Close Association ◽  
Gel Filtration ◽  
Fibril Formation ◽  
Amyloid Protein ◽  
Electron Microscopic ◽  
Amyloid Deposits ◽  
Amyloid Fibril Formation ◽  
Electron Microscopic Technique ◽  
Lysosomal System

A1thought the mechanisms of amyloidogenesis have not been entirely clarified, proteolysis of the parent proteins may be one of the important steps in the amyloid fibril formation. Recently, we reported that "dense fibrillar inclusions" (DFI), which had the characteristics of lysosomes and contained organized fibrillar profiles as well, were observed in the reticuloendothelial cells in close association with the foci of new amyloid deposits. We considered the findings as evidence for the involvement of lysosomal system in amyloid fibril formation (l). In the present study, we attempted to determine the identity of the contents of the DFI by the use of antisera against the amyloid protein (AA) and an immuno-electron microscopic technique.Amyloidosis was induced in CBA/J mice by daily injections of casein (l). AA was isolated from amyloid-laden spleens by gel filtration and antibody to it was produced in rabbits (2). For immunocytochemistry, the unlabeled antibody enzyme method (3) was employed.

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