Journal article
Serum Amyloid A Is an Exchangeable Apolipoprotein
Arteriosclerosis, thrombosis, and vascular biology, Vol.38(8), pp.1890-1900
08/2018
DOI: 10.1161/ATVBAHA.118.310979
PMCID: PMC6202200
PMID: 29976766
Abstract
Objective- SAA (serum amyloid A) is a family of acute-phase reactants that have proinflammatory and proatherogenic activities. SAA is more lipophilic than apoA-I (apolipoprotein A-I), and during an acute-phase response, <10% of plasma SAA is found lipid-free. In most reports, SAA is found exclusively associated with high-density lipoprotein; however, we and others have reported SAA on apoB (apolipoprotein B)-containing lipoproteins in both mice and humans. The goal of this study was to determine whether SAA is an exchangeable apolipoprotein. Approach and Results- Delipidated human SAA was incubated with SAA-free human lipoproteins; then, samples were reisolated by fast protein liquid chromatography, and SAA analyzed by ELISA and immunoblot. Both in vitro and in vivo, we show that SAA associates with any lipoprotein and does not remain in a lipid-free form. Although SAA is preferentially found on high-density lipoprotein, it can exchange between lipoproteins. In the presence of CETP (cholesterol ester transfer protein), there is greater exchange of SAA between lipoproteins. Subjects with diabetes mellitus, but not those with metabolic syndrome, showed altered SAA lipoprotein distribution postprandially. Proteoglycan-mediated lipoprotein retention is thought to be an underlying mechanism for atherosclerosis development. SAA has a proteoglycan-binding domain. Lipoproteins containing SAA had increased proteoglycan binding compared with SAA-free lipoproteins. Conclusions- Thus, SAA is an exchangeable apolipoprotein and increases apoB-containing lipoproteins' proteoglycan binding. We and others have previously reported the presence of SAA on low-density lipoprotein in individuals with obesity, diabetes mellitus, and metabolic syndrome. We propose that the presence of SAA on apoB-containing lipoproteins may contribute to cardiovascular disease development in these populations.
Details
- Title: Subtitle
- Serum Amyloid A Is an Exchangeable Apolipoprotein
- Creators
- Patricia G Wilson - Barnstable Brown Diabetes Center (P.G.W., J.C.T., P.S.,M.C.d.B., F.C.d.B., N.R.W., L.R.T.)Joel C Thompson - Barnstable Brown Diabetes Center (P.G.W., J.C.T., P.S.,M.C.d.B., F.C.d.B., N.R.W., L.R.T.)Preetha Shridas - Barnstable Brown Diabetes Center (P.G.W., J.C.T., P.S.,M.C.d.B., F.C.d.B., N.R.W., L.R.T.)Patrick J McNamara - College of Medicine and Department of Pharmaceutical Sciences (P.J.M.), College of Pharmacy, University of Kentucky, LexingtonMaria C de Beer - Barnstable Brown Diabetes Center (P.G.W., J.C.T., P.S.,M.C.d.B., F.C.d.B., N.R.W., L.R.T.)Frederick C de Beer - Barnstable Brown Diabetes Center (P.G.W., J.C.T., P.S.,M.C.d.B., F.C.d.B., N.R.W., L.R.T.)Nancy R Webb - Barnstable Brown Diabetes Center (P.G.W., J.C.T., P.S.,M.C.d.B., F.C.d.B., N.R.W., L.R.T.)Lisa R Tannock - Barnstable Brown Diabetes Center (P.G.W., J.C.T., P.S.,M.C.d.B., F.C.d.B., N.R.W., L.R.T.)
- Resource Type
- Journal article
- Publication Details
- Arteriosclerosis, thrombosis, and vascular biology, Vol.38(8), pp.1890-1900
- DOI
- 10.1161/ATVBAHA.118.310979
- PMID
- 29976766
- PMCID
- PMC6202200
- ISSN
- 1079-5642
- eISSN
- 1524-4636
- Grant note
- P30 GM127211 / NIGMS NIH HHS P20 GM103527 / NIGMS NIH HHS I01 CX000975 / CSRD VA R01 HL134731 / NHLBI NIH HHS I01 CX000773 / CSRD VA
- Language
- English
- Date published
- 08/2018
- Academic Unit
- Stead Family Department of Pediatrics; Neonatology; Internal Medicine
- Record Identifier
- 9984093478302771
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