Serum Amyloid A as a Marker of Persistent Inflammation and an Indicator of Cardiovascular and Renal Involvement in Patients with Rheumatoid Arthritis

Targońska-Stępniak, Bożena; Majdan, Maria

doi:10.1155/2014/793628

Cited by 72 publications

(64 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Individuals with benign tumors did not have significantly higher serum SAA levels than healthy persons [61], but SAA levels increased significantly as cancer progressed [56, 61, 90, 101, 104, 106]. The same effect was seen in patients with RA or osteoarthritis, whose serum SAA concentrations increased with the severity of the disease [83, 102, 107, 108]. Marhaug and Dowton [93] concluded that the serum SAA concentration is a very sensitive, but non-specific marker both in diagnosis, prognosis and monitoring of inflammatory and infectious diseases, just as in cancer [56, 61, 90, 105, 106].…”

Section: Production Of Human Saa Variantsmentioning

confidence: 99%

Structure and Expression of Different Serum Amyloid A (SAA) Variants and their Concentration-Dependent Functions During Host Insults

Buck¹,

Gouwy²,

Wang³

et al. 2016

CMC

197

220

View full text Add to dashboard Cite

Serum amyloid A (SAA) is, like C-reactive protein (CRP), an acute phase protein and can be used as a diagnostic, prognostic or therapy follow-up marker for many diseases. Increases in serum levels of SAA are triggered by physical insults to the host, including infection, trauma, inflammatory reactions and cancer. The order of magnitude of increase in SAA levels varies considerably, from a 10- to 100-fold during limited inflammatory events to a 1000-fold increase during severe bacterial infections and acute exacerbations of chronic inflammatory diseases. This broad response range is reflected by SAA gene duplications resulting in a cluster encoding several SAA variants and by multiple biological functions of SAA. SAA variants are single-domain proteins with simple structures and few post-translational modifications. SAA1 and SAA2 are inducible by inflammatory cytokines, whereas SAA4 is constitutively produced. We review here the regulated expression of SAA in normal and transformed cells and compare its serum levels in various disease states. At low concentrations (10-100 ng/ml), early in an inflammatory response, SAA induces chemokines or matrix degrading enzymes via Toll-like receptors and functions as an activator and chemoattractant through a G protein-coupled receptor. When an infectious or inflammatory stimulus persists, the liver continues to produce more SAA (> 1000 ng/ml) to become an antimicrobial agent by functioning as a direct opsonin of bacteria or by interference with virus infection of host cells. Thus, SAA regulates innate and adaptive immunity and this information may help to design better drugs to treat specific diseases.

show abstract

Section: Production Of Human Saa Variantsmentioning

confidence: 99%

Structure and Expression of Different Serum Amyloid A (SAA) Variants and their Concentration-Dependent Functions During Host Insults

Buck¹,

Gouwy²,

Wang³

et al. 2016

CMC

197

220

View full text Add to dashboard Cite

show abstract

“…SAA may play an important, pathogenic role in the proinflammatory process of RA (Connolly et al, 2012). Moreover, studies have indicated increased serum levels of SAA in RA and found it to be strongly associated with disease activity (Targonska-Stepniak and Majdan, 2014). In the current study, increased levels of serum SAA were demonstrated in the CP group.…”

Section: Oral Diseasesmentioning

confidence: 99%

Fetuin‐A, serum amyloid A and tumor necrosis factor alpha levels in periodontal health and disease

2017

View full text Add to dashboard Cite

show abstract

“…This circumstance holds true for RA, with elevated levels of both pro-inflammatory [e.g. C-reactive protein (CRP) (7)(8)(9)(10)(11), Tumor necrosis factor alpha (TNFα) (7,9,11), Interleukin-6 (IL-6) (7-12), IL-1β (7) and Serum Amyloid A (SAA) (10,13,14)] and prothrombotic markers [e.g. D-dimer (8,9,11,15,16), Fibrinogen (10,11,16,17), Tissue Factor (TF) (15), and von Willebrand factor (vWF) (8,16,18)], which is associated with one another (7,19) and with the risk of future cardiovascular complications (20)(21)(22)(23).…”

Section: Introductionmentioning

confidence: 99%

The Atypical Fibrin Fibre Network in Rheumatoid Arthritis and its Relation to Autoimmunity, Inflammation and Thrombosis

Bezuidenhout

Venter

Roberts

et al. 2020

Preprint

View full text Add to dashboard Cite

Objective. The risk of cardiovascular events in patients with RA is disproportionately heightened as a result of systemic inflammation. The relative effect of autoimmuneassociated citrullination on the structure and thrombotic potential of fibrin(ogen) remains unknown. We therefore compared indices of vascular function, inflammation, coagulation and fibrin clot composition in RA patients with healthy controls and evaluated inter-parameter relationships. Methods. Blood samples were collected from 30 RA patients and 25 age-and gender-matched healthy volunteers.Levels of SAA, CRP, ICAM-1 and VCAM-1 was measured using a sandwich immunoassay. Whole blood coagulation was assessed using Thromboelastography. Fibrin clot networks and fiber structure was investigated using Scanning Electron Microscopy. The detection and quantification of citrullination in formed fibrin clots were performed using a fluorescently labeled Citrulline monoclonal antibody with Confocal Microscopy. Results. Concentrations of SAA, CRP and ICAM-1 were significantly elevated in RA patients compared to controls. TEG parameters relating to coagulation initiation (R and K), rate of fibrin cross-linking (α-Angle), and time to reach maximum thrombus generation (TMRTG) were attenuated in RA patients. Parameters relating to clot strength (MA, MRTG, TGG) did not statistically differ between RA and controls. Logistic regression modelling revealed stronger association between acute phase reactants (CRP, SAA) with TEG parameters than endothelial function markers. Microscopic analysis revealed denser networks of thicker fibrin fibers in RA patients compared to controls [median (interquartile range) 214 (170-285) vs 120 (100-144) nm respectively, p<0.0001, Odds ratio=22.7). Detection of multiple citrullinated regions within fibrin clot structures in RA patients, which was less prevalent in control samples (p<0.05, OR=2.2). Conclusion.Patients with active RA display a coagulation profile that is dissimilar to general findings associated with other inflammatory conditions. The alteration of protein structures by autoimmune linked citrullination could play a role in determining the structure of fibrin and the potential of conferring a heightened thrombotic risk in RA patients.

show abstract

Serum Amyloid A as a Marker of Persistent Inflammation and an Indicator of Cardiovascular and Renal Involvement in Patients with Rheumatoid Arthritis

Cited by 72 publications

References 43 publications

Structure and Expression of Different Serum Amyloid A (SAA) Variants and their Concentration-Dependent Functions During Host Insults

Structure and Expression of Different Serum Amyloid A (SAA) Variants and their Concentration-Dependent Functions During Host Insults

Fetuin‐A, serum amyloid A and tumor necrosis factor alpha levels in periodontal health and disease

The Atypical Fibrin Fibre Network in Rheumatoid Arthritis and its Relation to Autoimmunity, Inflammation and Thrombosis

Contact Info

Product

Resources

About