ArticleBiochemical and biophysical research communications2011
Serum amyloid A 2.2 refolds into a octameric oligomer that slowly converts to a more stable hexamer.
Article in Biochemical and biophysical research communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Serum amyloid A: multifaceted roles in inflammation and cellular interactions.Immunologic research · 2025Review
- Serum Amyloid A: A Double-Edged Sword in Health and Disease.International journal of molecular sciences · 2025Review
- Acute-serum amyloid A and A-SAA-derived peptides as formyl peptide receptor (FPR) 2 ligands.Frontiers in endocrinology · 2023Review
- Signal peptide stabilizes folding and inhibits misfolding of serum amyloid A.Protein science : a publication of the Protein Society · 2022Article
- Review
- Serum amyloid A is a soluble pattern recognition receptor that drives type 2 immunity.Nature immunology · 2020Article
- Soluble pattern recognition molecules: Guardians and regulators of homeostasis at airway mucosal surfaces.European journal of immunology · 2020Review
- Molecular basis for retinol binding by serum amyloid A during infection.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Interleukin-1β Induces Intracellular Serum Amyloid A1 Expression in Human Coronary Artery Endothelial Cells and Promotes its Intercellular Exchange.Inflammation · 2019Article
- Serum amyloid A - a review.Molecular medicine (Cambridge, Mass.) · 2018Review
- Structure of serum amyloid A suggests a mechanism for selective lipoprotein binding and functions: SAA as a hub in macromolecular interaction networks.FEBS letters · 2016Article
- Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid A.Biochimie · 2014Article
- Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection.eLife · 2014Article
- Structural mechanism of serum amyloid A-mediated inflammatory amyloidosis.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Pathogenic serum amyloid A 1.1 shows a long oligomer-rich fibrillation lag phase contrary to the highly amyloidogenic non-pathogenic SAA2.2.The Journal of biological chemistry · 2013Article
- Article
- Influence of the carboxy terminus of serum amyloid A on protein oligomerization, misfolding, and fibril formation.Biochemistry · 2012Article
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Authors and funding
6 authors.
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Abstract
Serum amyloid A (SAA) is an inflammatory protein predominantly bound to high-density lipoprotein in plasma and presumed to play various biological and pathological roles. We previously found that the murine isoform SAA2.2 exists in aqueous solution as a marginally stable hexamer at 4-20°C, but becomes an intrinsically disordered protein at 37°C. Here we show that when urea-denatured SAA2.2 is dialyzed into buffer (pH 8.0, 4°C), it refolds mostly into an octameric species. The octamer transitions to the hexameric structure upon incubation from days to weeks at 4°C, depending on the SAA2.2 concentration. Thermal denaturation of the octamer and hexamer monitored by circular dichroism showed that the octamer is ∼10°C less stable, with a denaturation mid point of ∼22°C. Thus, SAA2.2 becomes kinetically trapped by refolding into a less stable, but more kinetically accessible octameric species. 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.
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