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• W2149656912 endingPage "3448" @default.
• W2149656912 startingPage "3436" @default.
• W2149656912 abstract "During inflammatory diseases, serum amyloid A (SAA), an acute-phase apolipoprotein of HDL, can assemble into tissue deposits called AA amyloids. The mechanism and physiological factors promoting amyloidosis are largely unknown but likely involve heparan sulfate (HS), a glycosaminoglycan colocalized with all types of amyloids. In this study, we explored HDL-SAA:HS interactions using in vitro and cell culture assays to identify HS-binding domains that promote the conversion of native SAA into AA amyloid. HS causes the remodeling of HDL-SAA at mildly acidic pH, producing SAA-rich aggregates. A sequence motif in SAA responsible for this conversion was identified that contains a pH-sensitive heparin/HS-binding site, functions as a ligand for a cell surface receptor, and acts as a structural focal point for SAAaggregation. Synthetic peptides corresponding to this region promoted the deposition of AA amyloid in a monocyte culture model for AA amyloidogenesis. The effects were peptide sequence specific and reliant on the protonation of H36. We conclude that a highly conserved motif required for SAA binding to macrophages can, under acidic pH conditions and in an HS-dependent manner, also act as a molecular switch, directing SAA misfolding into AA amyloid. Similar histidine-dependent HS-binding sites are also found in other amyloidogenic polypeptides.—Elimova, E., Kisilevsky, R., Ancsin, J. B. Heparan sulfate promotes the aggregation of HDL-associated serum amyloid A: evidence for a proamyloidogenic histidine molecular switch. FASEB J. 23, 3436–3448 (2009). www.fasebj.org" @default.
• W2149656912 created "2016-06-24" @default.
• W2149656912 creator A5010034511 @default.
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• W2149656912 date "2009-06-23" @default.
• W2149656912 modified "2023-10-18" @default.
• W2149656912 title "Heparan sulfate promotes the aggregation of HDL‐associated serum amyloid A: evidence for a proamyloidogenic histidine molecular switch" @default.
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• W2149656912 doi "https://doi.org/10.1096/fj.09-134981" @default.
• W2149656912 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19549924" @default.
• W2149656912 hasPublicationYear "2009" @default.
• W2149656912 type Work @default.

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