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The prevalence of the SAA2 polymorphisms (rs 2445174 and rs2468844) did not differ significantly between the groups of ankylosing spondylitis patients with and without amyloidosis.
Pathogenic serum amyloid A 1.1 shows a long oligomer-rich fibrillation lag phase contrary to the highly amyloidogenic non-pathogenic SAA2.2
successful quantification of SAA2 in crude serum by MRM, for the first time, shows that SAA2 can be a good biomarker for the detection of lung cancers.
Data show that both rs12218 of the SAA1 gene and rs2468844 of SAA2 gene are associated with carotid IMT in healthy Han Chinese subjects.
The glucocorticoid response element of the SAA2 promoter is dysfunctional compared to that of SAA1, hence glucocorticoids are unable to enhance the cytokine-driven transcriptional activity of SAA2.
saa2 is regulated by tumor necrosis factor-alpha, interleukin-6, and glucocorticoids in hepatic and epithelial cells.
SAA1a/a genotype is one genetic factor that confers a significant risk for amyloidosis in the Turkish FMF population but neither SAA1 nor SAA2 genotypes had a significant effect on SAA level.
Increased expression of SAA2 by adipocytes in obesity may play a critical role in local and systemic inflammation and free fatty acid production and could be a direct link between obesity and its comorbidities.
CRP and SAA strongly correlated up to the fifth day of observation but were not good predictors of mortality in septic shock.
polymorphisms in the SAA2 gene are associated with milk production traits in Chinese Holstein cows
SAA1/2 produced by macrophages promotes early lesion formation in the ascending aorta in LDLR knockout mice.
CE/J mice possess functional Saa1 and Saa2 genes with identical amino acid sequence.
Its gene hold broader diversity and greater complexity and these characteristics were likely attained through gene duplication and repeated gene conversion events in the Mus lineage.
The absence of endogenous SAA1.1 and 2.1 does not affect atherosclerotic lipid deposition in apolipoprotein E-deficient mice fed either normal or Western diets.
High level SAA expression induced amyloidosis in all mice after a short, slightly variable delay.
These results suggest that the carboxy terminus of SAA, which is highly conserved among SAA sequences in all vertebrates, might play important structural roles, including modulating the folding, oligomerization, misfolding, and fibrillation of SAA.(Saa2)
The nonpathogenic murine Saa2.2 spontaneously forms marginally stable amyloid fibrils at 37 degrees C that exhibit cross-beta structure, binding to thioflavin T, and fibrillation by a nucleation-dependent seeding mechanism.
The ability of SAA2.2 to form different oligomeric species in vitro along with its marginal stability, suggest that the structure of SAA might be modulated in vivo to form different biologically relevant species.
SAA does not impact High Density Lipoprotein levels, apoA-I clearance, or High Density Lipoprotein size
forms a hexamer containing a central channel in solution
Only liposomes containing intact SAA2.1 or its residues 1-20 or 74-103 promoted the efflux of cholesterol in vivo
SAA2.2 can form amyloid fibrils in vitro at physiological temperatures, which suggests that SAA2.2's inability to cause amyloidosis may be related to the stabilization of hexameric SAA2.2 and/or the slow kinetics of aberrant misfolding and self-assembly.
Many functional and pathological roles attributed to serum amyloid A may rely on its precarious structure, modulated by its interaction with ligands under homeostasis conditions and during the acute phase response.
Plasma A-SAA elevation was due to induction of Saa1 and Saa2 expression in liver but not in adipose tissue.
Major acute phase reactant. Apolipoprotein of the HDL complex.
serum amyloid A2
, serum amyloid A-2 protein
, serum amyloid A protein
, serum amyloid A 1
, LOW QUALITY PROTEIN: serum amyloid A-2 protein