Serum amyloid A protein classification: A preliminary report of a subcommittee of the International Society of Amyloidosis

Amyloid ◽  
1995 ◽  
Vol 2 (1) ◽  
pp. 69-70 ◽  
Author(s):  
Jean D. Sipe
2021 ◽  
Vol 22 (3) ◽  
pp. 1036
Author(s):  
Xuguang Lin ◽  
Kenichi Watanabe ◽  
Masahiro Kuragano ◽  
Kiyotaka Tokuraku

Amyloid A (AA) amyloidosis is a condition in which amyloid fibrils characterized by a linear morphology and a cross-β structure accumulate and are deposited extracellularly in organs, resulting in chronic inflammatory diseases and infections. The incidence of AA amyloidosis is high in humans and several animal species. Serum amyloid A (SAA) is one of the most important precursor amyloid proteins and plays a vital step in AA amyloidosis. Amyloid enhancing factor (AEF) serves as a seed for fibril formation and shortens the onset of AA amyloidosis sharply. In this study, we examined whether AEFs extracted and purified from five animal species (camel, cat, cattle, goat, and mouse) could promote mouse SAA (mSAA) protein aggregation in vitro using quantum-dot (QD) nanoprobes to visualize the aggregation. The results showed that AEFs shortened and promoted mSAA aggregation. In addition, mouse and cat AEFs showed higher mSAA aggregation-promoting activity than the camel, cattle, and goat AEFs. Interestingly, homology analysis of SAA in these five animal species revealed a more similar amino acid sequence homology between mouse and cat than between other animal species. Furthermore, a detailed comparison of amino acid sequences suggested that it was important to mSAA aggregation-promoting activity that the 48th amino acid was a basic residue (Lys) and the 125th amino acid was an acidic residue (Asp or Glu). These data imply that AA amyloidosis exhibits higher transmission activity among animals carrying genetically homologous SAA gene, and may provide a new understanding of the pathogenesis of amyloidosis.


1994 ◽  
Vol 331 (7) ◽  
pp. 417-424 ◽  
Author(s):  
Giovanna Liuzzo ◽  
Luigi M. Biasucci ◽  
J. Ruth Gallimore ◽  
Rita L. Grillo ◽  
Antonio G. Rebuzzi ◽  
...  

2009 ◽  
Vol 1 (1) ◽  
pp. 53
Author(s):  
Marita Kaniawati ◽  
Andi Wijaya ◽  
Anwar Susanto

BACKGROUND: Low-HDL cholesterol is a risk factor of CAD. Although levels of HDLC are within normal limit in some patients, they suffer CAD. These normal HDL-C levels might become pro-inflammatoric. This study is to measure the correlations between myeloperoxidase (MPO), serum amyloid-A (SAA) protein, and secretoryphospholipase-A2 (sPLA2) with inflammatory status of HDL-C.METHODS: This was a cross-sectional study recruited 49 subjects with high HDL-C (> 40 mg/dL) and 31 subjects with low HDL-C (< 40 mg/dL). HDL-C was determined into antiinflammatory and proinflammatory based on levels of Apo A-1 and hs-CRP. Concentrations of MPO, SAA and s-PLA2 were measured by ELISA method. Levels of Apo A-1 was determined by immunoturbidimetric method. Multiple logistic regression analysis was done using inflammatory status of HDL-C as dependent variables and levels of MPO, SAA, sPLA2, ages, total cholesterol and triglycerides as independent variables.RESULTS: Patient’s age was 43.4 + 8.3 year, HDL-C was 43.1 + 9.5 mg/dL, Apo A-1 was 128.3 + 21.5 mg/dL, hs-CRP was 1.92 + 3.0 mg/dL. Concentrations of MPO, SAA and sPLA2 successively were 63.2 + 16.9 ng/mL, 7015.6 + 5021.1 ng/mL and 1340.2 + 406.3 pg/mL. Multiple logistic regression analysis showed that SAA is an independent predictor of pro-inflammatory status of HDL-C in high HDL-C group with prevalence ratio of 11.74 (95% CI : 2.51 – 54.84; P = 0.002). In contrast, MPO and sPLA2 were not independent predictor with PR of 1.26 (95% CI : 0.30 – 5.23; P = 0.75) and of 0.94 (95% CI : 0.23 – 3.91; P = 0.93).CONCLUSIONS: SAA is an independent predictor of pro-inflammatory HDL-C even in subjects with high HDL-C.KEYWORDS: Atherosclerosis, Apo A-I, serum amyloid A protein, secretory phospholipase A2, myeloperoxidase


2021 ◽  
Author(s):  
Shreya Ghosh ◽  
Akansha Garg ◽  
Chayanika Kala ◽  
Ashwani Kumar Thakur

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.


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