Induced AA Amyloid in Hamster: On the Amyloid Enhancing Factor and Protein AA-Cross Reacting Components of Intermediate Molecular Weight

1988 ◽  
pp. 75-80 ◽  
Author(s):  
Th. A. Niewold ◽  
P. C. J. Tooten ◽  
A. C. J. van Andel ◽  
E. Gruys
Keyword(s):  
Molecular Weight ◽  
Enhancing Factor ◽  
Amyloid Enhancing Factor

Diffusible amyloid oligomers trigger systemic amyloidosis in mice

2008 ◽  
Vol 415 (2) ◽  
pp. 207-215 ◽  
Author(s):  
Sivanesan Senthilkumar ◽  
Edwin Chang ◽  
Rajadas Jayakumar
Keyword(s):  
Protein A ◽  
Mouse Tissue ◽  
Cytokine Induction ◽  
Amyloidogenic Proteins ◽  
Enhancing Factor ◽  
Amyloid Oligomers ◽  
Apparent Relationship ◽  
Amyloid Enhancing Factor ◽  
Local Accumulation

AA (amyloid protein A) amyloidosis in mice is markedly accelerated when the animals are given, in addition to an inflammatory stimulus, an intravenous injection of protein extracted from AA-laden mouse tissue. Previous findings affirm that AA fibrils can enhance the in vivo amyloidogenic process by a nucleation seeding mechanism. Accumulating evidence suggests that globular aggregates rather than fibrils are the toxic entities responsible for cell death. In the present study we report on structural and morphological features of AEF (amyloid-enhancing factor), a compound extracted and partially purified from amyloid-laden spleen. Surprisingly, the chief amyloidogenic material identified in the active AEF was diffusible globular oligomers. This partially purified active extract triggered amyloid deposition in vital organs when injected intravenously into mice. This implies that such a phenomenon could have been inflicted through the nucleation seeding potential of toxic oligomers in association with altered cytokine induction. In the present study we report an apparent relationship between altered cytokine expression and AA accumulation in systemically inflamed tissues. The prevalence of serum AA monomers and proteolytic oligomers in spleen AEF is consistent to suggest that extrahepatic serum AA processing might lead to local accumulation of amyloidogenic proteins at the serum AA production site.

scholarly journals Deposition, Clearance, and Reinduction of Amyloid A Amyloid in Interleukin 1 Receptor Antagonist Knockout Mice

2016 ◽  
Vol 54 (1) ◽  
pp. 99-110 ◽  
Author(s):  
K. Watanabe ◽  
K. Uchida ◽  
J. K. Chambers ◽  
N. Ushio ◽  
H. Nakayama
Keyword(s):  
Receptor Antagonist ◽  
Knockout Mice ◽  
Interleukin 1 ◽  
Recovery Process ◽  
Amyloid Deposition ◽  
Aa Amyloidosis ◽  
Amyloid A ◽  
Enhancing Factor ◽  
Amyloid Deposits ◽  
Amyloid Enhancing Factor

Amyloid A (AA) amyloidosis is characterized by the extracellular deposition of AA amyloid and results in the irreversible dysfunction of parenchymal organs. In experimental models, AA amyloid deposits are cleared following a decrease in circulating serum amyloid A (SAA) concentrations. Additional inflammatory stimuli during this recovery process may induce more severe amyloid redeposition. In the present study, we confirmed the deposition, clearance, and reinduction of AA amyloid deposits in interleukin 1 receptor antagonist knockout mice (IL-1raKO) and studied the SAA levels and amyloid-enhancing factor activity based on the time-dependent changes of amyloid deposition. Histopathologically, following initial (day 0) injection of amyloid-enhancing factor in combination with an inflammatory stimulus (silver nitrate [AgNO3]), amyloid deposition peaked by day 20, and its deposition gradually decreased after day 35. SAA concentrations in serum were precipitously elevated on day 1 but returned to normal levels by day 10, whereas the SAA dimer was detected in serum after day 45. An additional AgNO3 injection was administered to mice with amyloidosis on day 5, 10, 35, or 50, and all mice developed large amyloid deposits. Amyloid deposition was most severe in mice treated with AgNO3 on day 35. The inoculation of sera from mice with AA amyloidosis, combined with AgNO3, induced AA amyloidosis. Serum samples collected on days 35 and 50, which contained high concentrations of the SAA dimer, induced amyloidosis in a high proportion (83%) of mice. Therefore, increased SAA and/or its dimer in serum during the recovery process may markedly exacerbate the development of AA amyloidosis.

scholarly journals Amyloid enhancing factor activity is associated with ubiquitin

1992 ◽  
Vol 420 (2) ◽  
pp. 139-148 ◽  
Author(s):  
Kamel Alizadeh-Khiavi ◽  
Josée Normand ◽  
Soula Chronopoulos ◽  
Ambereen Ali ◽  
Zafer Ali-Khan
Keyword(s):  
Factor Activity ◽  
Enhancing Factor ◽  
Amyloid Enhancing Factor

New clothes for amyloid enhancing factor (AEF): Silk as AEF

Amyloid ◽  
1999 ◽  
Vol 6 (2) ◽  
pp. 98-106 ◽  
Author(s):  
Robert Kisilevsky ◽  
Laura Lernieux ◽  
Lee Boudreau ◽  
Yang Dun-Sheng ◽  
Paul Fraser
Keyword(s):  
Enhancing Factor ◽  
Amyloid Enhancing Factor

Evidence for increased amyloid enhancing factor activity in Alzheimer brain extract

1988 ◽  
Vol 77 (1) ◽  
pp. 82-90 ◽  
Author(s):  
Z. Ali-Khan ◽  
R. Quirion ◽  
Y. Robitaille ◽  
K. Alizadeh-Khiavi ◽  
T. Du
Keyword(s):  
Brain Extract ◽  
Factor Activity ◽  
Enhancing Factor ◽  
Alzheimer Brain ◽  
Amyloid Enhancing Factor

Inactivation of amyloid-enhancing factor (AEF): study on experimental murine AA amyloidosis

2007 ◽  
Vol 40 (2) ◽  
pp. 88-94 ◽  
Author(s):  
Masatoshi Omoto ◽  
Tadaaki Yokota ◽  
Dan Cui ◽  
Yoshinobu Hoshii ◽  
Hiroo Kawano ◽  
...  
Keyword(s):  
Aa Amyloidosis ◽  
Enhancing Factor ◽  
Amyloid Enhancing Factor
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