SAT0105 Inflammatory Markers in Rheumatoid Arthritis – What Is The Role of Serum Amyloid A Protein?

2016 ◽  
Vol 75 (Suppl 2) ◽  
pp. 703.2-703
Author(s):  
D.R. Gonçalves ◽  
R. Fonseca ◽  
F. Aguiar ◽  
T. Martins-Rocha ◽  
M. Bernardes ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Inflammatory Markers ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Serum Amyloid A Protein

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

2020 ◽  
Author(s):  
Syed Wali Peeran ◽  
Ahmed Elhassan ◽  
Mohammed Zameer ◽  
Syed Nahid Basheer ◽  
Mohammed Mustafa ◽  
...  
Keyword(s):  
Chronic Periodontitis ◽  
Serum Amyloid A ◽  
Inflammatory Diseases ◽  
Apical Periodontitis ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Serum Amyloid A Protein ◽  
Health And Disease ◽  
Periapical Inflammation

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.

SERUM AMYLOID A PROTEIN DURING THE TREATMENT OF RHEUMATOID ARTHRITIS WITH SECOND-LINE DRUGS

Rheumatology ◽  
1985 ◽  
Vol 24 (2) ◽  
pp. 158-163 ◽  
Author(s):  
K. A. GRINDULIS ◽  
D. L. SCOTT ◽  
M. W. ROBINSON ◽  
P. A. BACON ◽  
B. McCONKEY
Keyword(s):  
Rheumatoid Arthritis ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Second Line ◽  
Amyloid A ◽  
Serum Amyloid A Protein

scholarly journals Role of Serum Amyloid A Protein in the Early Detection of Late Onset Sepsis in Neonate

2020 ◽  
Vol 0 (0) ◽  
pp. 0-0
Author(s):  
Heba Abd Elkhalek ◽  
Neeven Abed ◽  
Omima Abdel Haie ◽  
Seham Goda
Keyword(s):  
Early Detection ◽  
Serum Amyloid A ◽  
Late Onset ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Late Onset Sepsis ◽  
Serum Amyloid A Protein

scholarly journals Cleavage, down-regulation and aggregation of serum amyloid A

2019 ◽  
Author(s):  
Wenhua Wang ◽  
Prabir Khatua ◽  
Ulrich H.E. Hansmann
Keyword(s):  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid Formation ◽  
Dynamic Simulations ◽  
Over Expression ◽  
Amyloid A ◽  
Serum Amyloid A Protein ◽  
Ph Increase ◽  
The One

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.

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