On the lag phase in amyloid fibril formation

Rates of microscopic processes taking place during the lag phase of amyloid fibril formation for a reaction starting from an initially monomeric 4 μm solution of Aβ42.

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Sequence-independent recognition of the amyloid structural motif by GFP protein family

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.2001457117 ◽

2020 ◽

Vol 117 (36) ◽

pp. 22122-22127 ◽

Cited By ~ 1

Author(s):

Sherry C. S. Xu ◽

Josephine G. LoRicco ◽

Anthony C. Bishop ◽

Nathan A. James ◽

Welby H. Huynh ◽

...

Keyword(s):

Amyloid Fibrils ◽

Amyloid Fibril ◽

Fluorescent Protein ◽

Protein Localization ◽

Fibril Formation ◽

Structural Motif ◽

Diagnostic Tools ◽

Lag Phase ◽

Dependent Manner ◽

Amyloid Fibril Formation

Cnidarian fluorescent protein (FP) derivatives such as GFP, mCherry, and mEOS2 have been widely used to monitor gene expression and protein localization through biological imaging because they are considered functionally inert. We demonstrate that FPs specifically bind amyloid fibrils formed from many natural peptides and proteins. FPs do not bind other nonamyloid fibrillar structures such as microtubules or actin filaments and do not bind to amorphous aggregates. FPs can also bind small aggregates formed during the lag phase and early elongation phase of fibril formation and can inhibit amyloid fibril formation in a dose-dependent manner. These findings suggest caution should be taken in interpreting FP-fusion protein localization data when amyloid structures may be present. Given the pathological significance of amyloid-related species in some diseases, detection and inhibition of amyloid fibril formation using FPs can provide insights on developing diagnostic tools.

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Very rapid amyloid fibril formation by a bacterial lipase in the absence of a detectable lag phase

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics ◽

10.1016/j.bbapap.2017.03.004 ◽

2017 ◽

Vol 1865 (6) ◽

pp. 652-663 ◽

Cited By ~ 7

Author(s):

Fatemeh Rashno ◽

Khosro Khajeh ◽

Claudia Capitini ◽

Reza H. Sajedi ◽

Maryam Monsef Shokri ◽

...

Keyword(s):

Amyloid Fibril ◽

Fibril Formation ◽

Lag Phase ◽

Amyloid Fibril Formation

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

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100079632 ◽

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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