scholarly journals Role of Serum Amyloid A Protein in Various Diseases with Special Reference to Periodontal and Periapical Inflammation- A Review

Author(s):  
Syed Wali Peeran ◽  
Ahmed Elhassan ◽  
Mohammed Zameer ◽  
Syed Nahid Basheer ◽  
Mohammed Mustafa ◽  
...  

Serum Amyloid A (SAA) is an Acute-Phase Protein (APP) produced as an innate nonspecific response to any tissue damage. Hence, it plays a significant role in chronic inflammatory diseases. In particular, SAA levels increase dramatically in chronic periodontitis and chronic apical periodontitis. Recent studies suggest this role of SAA in the pathogenesis of various diseases, including chronic periodontitis and chronic apical periodontitis. Thus, the focus of this review is to sum up the current understanding of the role of SAA in health and disease and to elaborate on possible mechanisms by which SAA could play a role in the pathogenesis of chronic periodontitis and chronic apical periodontitis.

Cells ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 585
Author(s):  
Els Beijer ◽  
Claudia Roodenburg-Benschop ◽  
Milou C. Schimmelpennink ◽  
Jan C. Grutters ◽  
Bob Meek ◽  
...  

Elevated Serum Amyloid A (SAA) levels have been found in several inflammatory diseases, including sarcoidosis. SAA is suggested to be involved in sarcoidosis pathogenesis by involvement in granuloma formation and maintenance. We hypothesized that SAA serum levels would be higher in sarcoidosis compared to other non-infectious granulomatous and non-granulomatous diseases. SAA levels were measured in serum from sarcoidosis, Hypersensitivity pneumonitis (HP), and (eosinophilic) granulomatosis with polyangiitis ((E)GPA) patients. Idiopathic pulmonary fibrosis (IPF) patients were included as non-granulomatous disease group. SAA levels of patients with sarcoidosis (31.0 µg/mL), HP (23.4 µg/mL), (E)GPA (36.9 µg/mL), and IPF (22.1 µg/mL) were all higher than SAA levels of healthy controls (10.1 µg/mL). SAA levels did not differ between the diagnostic groups. When SAA serum levels were analyzed in sarcoidosis subgroups, fibrotic sarcoidosis patients showed higher SAA levels than sarcoidosis patients without fibrosis (47.8 µg/mL vs. 29.4 µg/mL, p = 0.005). To conclude, the observation that fibrotic sarcoidosis patients have higher SAA levels, together with our finding that SAA levels were also increased in IPF patients, suggests that SAA may next to granulomatous processes also reflect the process of fibrogenesis. Further studies should clarify the exact role of SAA in fibrosis and the underlying mechanisms involved.


2016 ◽  
Vol 75 (Suppl 2) ◽  
pp. 703.2-703
Author(s):  
D.R. Gonçalves ◽  
R. Fonseca ◽  
F. Aguiar ◽  
T. Martins-Rocha ◽  
M. Bernardes ◽  
...  

2020 ◽  
Vol 0 (0) ◽  
pp. 0-0
Author(s):  
Heba Abd Elkhalek ◽  
Neeven Abed ◽  
Omima Abdel Haie ◽  
Seham Goda

2019 ◽  
Author(s):  
Wenhua Wang ◽  
Prabir Khatua ◽  
Ulrich H.E. Hansmann

AbstractVarious diseases cause over-expression of the serum amyloid A protein (SAA), which leads in some, but not all, cases to amyloidosis as a secondary disease. The response to the over-expression involves dissociation of SAA hexamer and subsequent cleavage of the released monomers, most commonly yielding fragments SAA1−76 of the full-sized SAA1−104. We report results from molecular dynamic simulations that probe the role of this cleavage for down-regulating activity and the concentration of SAA. We propose a mechanism that relies on two elements. First, the probability to assemble into hexamers is lower for the fragments than it is for the full-sized protein. Second, unlike other fragments SAA1−76 can switch between two distinct configurations. The first kind is easy to proteolyze (allowing a fast reduction of SAA concentration) but prone to aggregation, while the situation is opposite for the second kind. If the time scale for amyloid formation is longer than the one for proteolysis, the aggregation-prone species dominates. However, if environmental conditions such as low pH increase the risk of amyloid formation, the ensemble shifts toward the more protected form. We speculate that SAA amyloidosis is a failure of the switching mechanism leading to accumulation of the aggregation-prone species and subsequent amyloid formation.


1992 ◽  
Vol 20 (2-3) ◽  
pp. 101-109 ◽  
Author(s):  
Yukio IKEDA ◽  
Yoshitaka KUMON ◽  
Kenzo YOSHIDA ◽  
Tadashi SUEHIRO ◽  
Fumitoshi OHNO

The Lancet ◽  
1982 ◽  
Vol 320 (8292) ◽  
pp. 231-234 ◽  
Author(s):  
F.C De Beer ◽  
ElizabethA Fagan ◽  
G.R.V Hughes ◽  
R.K Mallya ◽  
J.G Lanham ◽  
...  

2021 ◽  
Vol 80 (Suppl 1) ◽  
pp. 1066.2-1066
Author(s):  
K. Sakharova ◽  
M. Cherkasova ◽  
S. Erdes

Background:Serum amyloid A protein (SAA) likely has a critical role in control and possibly propagation of the primordial acute phase response and is the precursor of AA amyloid fibrils. Prolonged elevations in SAA are the major inciting factor for AA amyloidosis developing in chronic inflammatory diseases. In Russia 2-4% of patients with ankylosing spondylitis (AS) have secondary (AA) amyloidosis.Objectives:To study the level of SAA in AS its relationship with indicators of disease activity.Methods:124 patients with AS (according to mNYC 1984) 70 men, 54 women, of whom HLA B 27 positive 91.1% mean age 38.1 (± 12.9), age at the onset of the disease 23.5 (± 9.9) consecutively admitted to the clinic of the Research Institute rheumatology from February to November 2020. In addition to the standard examination (the median CRP 6.7 mg/l [1.4; 24.9], ESR 13 mm/h [7; 27], SAA was studied in all patients by the nephelometric method.Results:The median SAA in 124 patients was 12.5 mg/l [4;71.6]. Among them, 31% had normal SAA level (<5 mg/l), and 69 % - more than 5 mg/l. In 21 (17.5 %) cases, the level of SAA was increased at normal CRP levels, and only in 2 cases an increase in the level of CRP at normal SAA levels; 50 patients (40.3 %) with normal ESR had elevated SAA levels, and 7 (5.6%) - ESR exceeded the upper limits of the norm with normal SAA levels. Comparison of the average values of the levels of SAA, CRP, ESR in men and women did not reveal significant differences between them. The SAA level was weakly correlated with ESR (r = 0.2; p=0.002) and BASDAI (r=0.3; p=0.002), moderately with ASDAS-CRP (r=0.5; r<0.0001), but showed a strong association with CRP (r = 0.80; p<0.00001). Patients with elevated SAA levels (>5 mg/l) had a shorter disease duration (10 and 12 year; p<0.0004), higher ASDAS-CRP (2.9 and 2.4; p<0.003), blood CRP level (14.6 and 1.3; p<0.00001), and significantly more peripheral arthritis (60% and 39%; p<0.05) than patients with normal indicators.Conclusion:The level of SAA correlates well with indicators of AS activity, especially with the level of CRP, and can be used as an alternative indicator of disease activity.Disclosure of Interests:None declared


2021 ◽  
pp. 100080
Author(s):  
Martyna Maszota-Zieleniak ◽  
Annemarie Danielsson ◽  
Sergey A. Samsonov

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.


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