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 Spontaneous, Experimentally Induced, and Transmissible AA Amyloidosis in Japanese Quail (Coturnix japonica)

2017 ◽  
Vol 54 (6) ◽  
pp. 912-921 ◽  
Author(s):  
Yumi Nakayama ◽  
Junichi Kamiie ◽  
Gen Watanabe ◽  
Kazuhiko Suzuki ◽  
Tomoaki Murakami
Keyword(s):  
Japanese Quail ◽  
Intestinal Tract ◽  
Amyloid Fibrils ◽  
Amyloid Deposition ◽  
Coturnix Japonica ◽  
Aa Amyloidosis ◽  
Amyloid A ◽  
Amyloid Deposits ◽  
Amyloid Enhancing Factor ◽  
Apparently Healthy

The authors describe a spontaneous case of amyloid A (AA) amyloidosis in an adult female Japanese quail ( Coturnix japonica). The bird developed AA amyloidosis secondary to chronic peritonitis caused by a Gram-negative bacillus infection. Mild amyloid deposition was also identified in the intestinal tract of apparently healthy adult individuals, suggesting that quail may develop intestinal amyloidosis with age. Based on these observations, it was hypothesized that quail can develop AA amyloidosis following inflammatory stimulation with lipopolysaccharide (LPS). Therefore, adult quail were repeatedly injected with LPS and the development of AA amyloidosis was confirmed. The amyloid deposition in this model increased when quail amyloid was intravenously injected as an amyloid-enhancing factor. The experiments were repeated with young quail, but amyloid deposits were not observed following LPS injections. However, AA amyloidosis did develop when quail amyloid was injected in addition to LPS. These results indicated that adult quail develop AA amyloidosis after inflammatory stimulation with LPS. Furthermore, quail AA amyloidosis was shown to have transmissibility regardless of age. Interestingly, the authors found that administration of chicken amyloid fibrils also induced AA amyloidosis in young quail. This is the first report of cross-species transmission of avian AA amyloidosis.

Generalized AA-amyloidosis in Siberian Tigers (Panthera tigris altaica) with Predominant Renal Medullary Amyloid Deposition

1998 ◽  
Vol 35 (1) ◽  
pp. 70-74 ◽  
Author(s):  
C. Schulze ◽  
M. Brügmann ◽  
M. Böer ◽  
H.-P. Brandt ◽  
J. Pohlenz ◽  
...  
Keyword(s):  
Congo Red ◽  
Kidney Diseases ◽  
Amyloid Deposition ◽  
Panthera Tigris ◽  
Aa Amyloidosis ◽  
Familial Predisposition ◽  
Amyloid A ◽  
Panthera Tigris Altaica ◽  
Amyloid Deposits ◽  
Congo Red Staining

Generalized amyloidosis with predominant renal medullary amyloid deposition was found in four closely related Siberian tigers ( Panthera tigris altaica) suffering from end stage kidney diseases. Only minimal to mild amounts of amyloid were deposited in various organs outside the kidneys with individually variable organ involvement. The Congo red staining affinity of amyloid deposits was sensitive to potassium permanganate oxidation. The deposits were further characterized as being of the amyloid-A (AA) type by immunohistochemistry using the mouse monoclonal antibody mc4 directed against a conserved region of the human AA-protein. A combination of immunohistochemistry and Congo red staining was much more sensitive for the diagnosis of amyloid deposits than Congo red staining alone. With this combination, even minimal amyloid deposits were detected that had been missed in the first reading using Congo-red-stained slides alone. Since no common primary cause was identified, the amyloidosis was classified as idiopathic generalized AA-amyloidosis with a potential familial predisposition.

scholarly journals Amyloid deposition in granuloma of tuberculosis patients: A pilot study

2021 ◽  
Author(s):  
Shreya Ghosh ◽  
Akansha Garg ◽  
Chayanika Kala ◽  
Ashwani Kumar Thakur
Keyword(s):  
Serum Amyloid A ◽  
Amyloid Deposition ◽  
Serum Amyloid ◽  
Secondary Amyloidosis ◽  
Amyloid Formation ◽  
Tuberculosis Patients ◽  
Amyloid A ◽  
Inflammatory Conditions ◽  
Amyloid Deposits ◽  
Serum Amyloid A Protein

AbstractThe formation of granuloma is one of the characteristic feature of tuberculosis. Besides, rise in the concentration of acute phase response proteins mainly serum amyloid A is the indicator for chronic inflammation associated with tuberculosis. Serum amyloid A drives secondary amyloidosis in tuberculosis and other chronic inflammatory conditions. The linkage between serum amyloid A (SAA) protein and amyloid deposition site is not well understood in tuberculosis and other chronic inflammatory conditions. We hypothesized that granuloma could be a potential site for amyloid deposition because of the presence of serum amyloid A protein and proteases that cleave SAA and trigger amyloid formation. Based on this hypothesis, for the first time we have shown the presence of amyloid deposits in the granuloma of tuberculosis patients using the gold standard, Congo red dye staining.

Effective Anti-TNF-α Therapy Can Induce Rapid Resolution and Sustained Decrease of Gastroduodenal Mucosal Amyloid Deposits in Reactive Amyloidosis Associated with Rheumatoid Arthritis

2009 ◽  
Vol 36 (11) ◽  
pp. 2409-2415 ◽  
Author(s):  
TAKESHI KURODA ◽  
YOKO WADA ◽  
DAISUKE KOBAYASHI ◽  
SHUICHI MURAKAMI ◽  
TAKEHITO SAKAI ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Aa Amyloidosis ◽  
Laboratory Findings ◽  
Protein Levels ◽  
Amyloid A ◽  
Biopsy Specimens ◽  
Amyloid Deposits ◽  
Reactive Amyloidosis ◽  
Serum Amyloid A Protein ◽  
Before And After

Objective.To examine the effect of anti-tumor necrosis factor-α (anti-TNF) therapy in patients with reactive AA amyloidosis associated with rheumatoid arthritis (RA).Methods.Fourteen patients with reactive AA amyloidosis associated with RA were prospectively evaluated. Four patients were treated with infliximab and 10 with etanercept. The mean period of anti-TNF therapy was 20.1 ± 13.8 months. Laboratory findings and renal function were examined before and after initiation of anti-TNF therapy. In 9 patients the area of amyloid deposits in serial gastroduodenal mucosal biopsy specimens was examined and image analysis was performed.Results.C-reactive protein and serum amyloid A protein levels were significantly reduced after initiation of anti-TNF therapy. Twenty-four hour creatinine clearance improved in 4 patients, did not change in 5, and deteriorated in 3. Twenty-four hour urinary protein excretion was significantly decreased in 3 patients, not exacerbated in 6, and increased in 3 after initiation of anti-TNF therapy. The biopsy specimens from the 9 patients who underwent serial gastroduodenal biopsies showed significant decreases in the area of amyloid deposits, from 8.8% ± 6.4% to 1.6% ± 0.6% (p = 0.003) after initiation of anti-TNF therapy. Four patients showed a sustained decrease in the areas of amyloid deposits in their third biopsy specimens, and amyloid deposits were not detectable in 2.Conclusion.Our results indicate a striking effect of anti-TNF therapy for rapid removal and sustained disappearance of amyloid deposits in gastric mucosal tissue with amelioration of renal functions in patients with reactive amyloidosis due to RA.

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

scholarly journals Colocalization of Apolipoprotein AI in Various Kinds of Systemic Amyloidosis

2005 ◽  
Vol 53 (2) ◽  
pp. 237-242 ◽  
Author(s):  
Naohiro Sakata ◽  
Yoshinobu Hoshii ◽  
Tomomi Nakamura ◽  
Makiko Kiyama ◽  
Hirofumi Arai ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Amyloid Fibrils ◽  
Senile Plaques ◽  
Systemic Amyloidosis ◽  
High Density Lipoproteins ◽  
Apolipoprotein Ai ◽  
Aa Amyloidosis ◽  
Amyloid A ◽  
Amyloid Deposits ◽  
A Minor

Apolipoprotein AI (apoAI), a major component of high-density lipoproteins, is one of the major amyloid fibril proteins and a minor constituent of the senile plaques observed in Alzheimer's disease. We examined colocalization of apoAI in various kinds of systemic amyloidosis in this study. Forty-three of 48 formalin-fixed paraffin-embedded heart specimens with various forms of systemic amyloidosis reacted immunohistochemically with anti-human apoAI antibody. ApoAI was also detected in water-extracted amyloid material by immunoblotting. In addition, we observed colocalization of apoAI and murine amyloid A (AA) amyloidosis in human apoAI transgenic mice. This is the first report of colocalization of apoAI with amyloid deposits in various forms of human systemic amyloidosis and murine AA amyloidosis in human apoAI transgenic mice. ApoAI may not always be a major component of amyloid fibrils, even when it is present in systemic amyloid deposits.

Antisense oligonucleotide suppression of serum amyloid A reduces amyloid deposition in mice with AA amyloidosis

Amyloid ◽  
2011 ◽  
Vol 18 (3) ◽  
pp. 136-146 ◽  
Author(s):  
Barbara Kluve-Beckerman ◽  
Joyce Hardwick ◽  
Lijing Du ◽  
Merrill D. Benson ◽  
Brett P. Monia ◽  
...  
Keyword(s):  
Antisense Oligonucleotide ◽  
Serum Amyloid A ◽  
Amyloid Deposition ◽  
Serum Amyloid ◽  
Aa Amyloidosis ◽  
Amyloid A
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