Structural highlights
Disease
SAA2_MOUSE Reactive, secondary amyloidosis is characterized by the extracellular accumulation in various tissues of the SAA protein. These deposits are highly insoluble and resistant to proteolysis; they disrupt tissue structure and compromise function.
Function
SAA2_MOUSE Major acute phase reactant. Apolipoprotein of the HDL complex.
Publication Abstract from PubMed
The co-deposition of amyloid fibrils from different precursor proteins is a topic of increasing relevance for protein misfolding diseases. Using cryo-electron microscopy (cryo-EM), we here determined the structures of two serum amyloid A (SAA) protein-derived amyloid fibril morphologies that were extracted from a mouse strain that is primarily known to be associated with apolipoprotein A-II-derived amyloid fibrils. The two fibril morphologies show the same protomer conformation as in previously reported ex vivo amyloid fibrils from SAA protein but a different relative arrangement of fibril protein stacks. These data establish that serum amyloid A-derived amyloid fibrils share the same fibril protein fold in different mouse strains and disease contexts.
Cryo-EM Observation of AA Amyloid Fibrils in Mouse Model of Systemic AApoAII Amyloidosis.,Andreotti G, Higuchi K, Schmidt M, Fandrich M J Mol Biol. 2025 Sep 11;437(24):169438. doi: 10.1016/j.jmb.2025.169438. PMID:40945578[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Andreotti G, Higuchi K, Schmidt M, Fändrich M. Cryo-EM Observation of AA Amyloid Fibrils in Mouse Model of Systemic AApoAII Amyloidosis. J Mol Biol. 2025 Sep 11;437(24):169438. PMID:40945578 doi:10.1016/j.jmb.2025.169438
