scholarly journals Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins

2018 ◽  
Vol 9 (13) ◽  
pp. 3290-3298 ◽  
Author(s):  
Gaetano Malgieri ◽  
Gianluca D'Abrosca ◽  
Luciano Pirone ◽  
Angelo Toto ◽  
Maddalena Palmieri ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Homologous Proteins ◽  
Amyloid Fibril Formation ◽  
Molecular Determinants ◽  
Folding Pathways

Understanding the molecular determinants of fibrillogenesis by studying the aggregation propensities of high homologous proteins with different folding pathways.

scholarly journals Antioxidants From the Class of Polyphenols, NAC and Vitamin C Act Differently on Amyloid Fibril Formation by Two Human Cystatins: Stefin B and Cystatin C.

2020 ◽  
Author(s):  
Alma Jahic Mujkic ◽  
Samra Hasanbasic ◽  
Magda Tušek Žnidarič ◽  
Selma Berbic ◽  
Eva Zerovnik
Keyword(s):  
Vitamin C ◽  
Cystatin C ◽  
Amyloid Fibril ◽  
Synergistic Effects ◽  
Fibril Formation ◽  
Homologous Proteins ◽  
Amyloid Fibril Formation ◽  
Transmission Electron ◽  
Amyloid Fibrillation ◽  
Anti Oxidant

We compare the effect on amyloid fibril formation by two homologous proteins from the family of cystatins, human stefin B (stB) and cystatin C (cysC) in presence of 3 polyphenols: curcumin, resveratrol and quercetin and 2 non-phenolic anti-oxidants: vitamin C (VitC) and N-acetyl cystein (NAC). Some of the experimental data have already been presented, here we compare, further discuss and highlight the results. The amyloid fibril formation was followed by ThT fluorescence and transmission electron microscopy. Inhibitory effects on amyloid fibrillation reaction depended on anti-oxidant class and concentration. The fact that different effect of polyphenols was observed with the two cystatins; Cur acted inhibitory on stB but not on cysC fibril formation, could be explained if the 3 polyphenols would not bind to the same binding site in the fibrils core. Other differences are pointed out and discussed. Synergistic effects of VitC and chosen polyphenols on amyloid fibrilllation of human stB have been explored and are reported here for the first time.

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.

Monitoring the prevention of amyloid fibril formation by α-crystallin

FEBS Journal ◽  
2007 ◽  
Vol 274 (24) ◽  
pp. 6290-6304 ◽  
Author(s):  
Agata Rekas ◽  
Lucy Jankova ◽  
David C. Thorn ◽  
Roberto Cappai ◽  
John A. Carver
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

scholarly journals Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners

2021 ◽  
Vol 296 ◽  
pp. 100510
Author(s):  
Keiichi Yamaguchi ◽  
Masatomo So ◽  
César Aguirre ◽  
Kensuke Ikenaka ◽  
Hideki Mochizuki ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

scholarly journals Investigation of a Peptide Responsible for Amyloid Fibril Formation of β2-Microglobulin byAchromobacterProtease I

2001 ◽  
Vol 277 (2) ◽  
pp. 1310-1315 ◽  
Author(s):  
Gennady V. Kozhukh ◽  
Yoshihisa Hagihara ◽  
Toru Kawakami ◽  
Kazuhiro Hasegawa ◽  
Hironobu Naiki ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Β2 Microglobulin ◽  
Amyloid Fibril Formation

scholarly journals 2P071 Direct observation of burst of amyloid fibril formation by calorimetry(01C. Protein: Property)

2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S170
Author(s):  
Tatsuya Ikenoue ◽  
Young-Ho Lee ◽  
Jozef Kardos ◽  
Yuji Goto
Keyword(s):  
Direct Observation ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Protein Property
Sign in / Sign up

Export Citation Format

Share Document