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Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
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Serum Amyloid A Is an Exchangeable Apolipoprotein
Patricia G Wilson1,2,3, Joel C Thompson1,2,3, Preetha Shridas4,2,3
1From the Department of Veterans Affairs, Lexington, KY (P.G.W., J.C.T., N.R.W., L.R.T.).
Arteriosclerosis, Thrombosis, and Vascular Biology
|July 7, 2018
Summary
Serum amyloid A (SAA) is an exchangeable apolipoprotein that binds to various lipoproteins. This association increases proteoglycan binding, potentially contributing to cardiovascular disease in specific populations.
Area of Science:
- Biochemistry
- Cardiovascular Science
- Lipid Metabolism
Background:
- Serum amyloid A (SAA) is an acute-phase reactant with pro-inflammatory and pro-atherogenic properties.
- SAA is typically found associated with high-density lipoprotein (HDL), but can also be present on apolipoprotein B (apoB)-containing lipoproteins.
- The exchangeability of SAA between different lipoprotein particles is not well understood.
Purpose of the Study:
- To investigate whether serum amyloid A (SAA) functions as an exchangeable apolipoprotein.
- To determine the association patterns of SAA with various human lipoproteins.
- To assess the impact of SAA on lipoprotein-proteoglycan interactions.
Main Methods:
- In vitro incubation of delipidated human SAA with SAA-free human lipoproteins.
- Analysis of SAA association with lipoproteins using fast protein liquid chromatography (FPLC), ELISA, and immunoblotting.
- Investigation of SAA lipoprotein distribution in subjects with diabetes mellitus and metabolic syndrome, including postprandial analysis.
Main Results:
- SAA demonstrated association with all tested lipoproteins, not remaining in a lipid-free state.
- SAA showed preferential association with HDL but was found to be exchangeable between different lipoprotein classes.
- The presence of cholesterol ester transfer protein (CETP) enhanced SAA exchange between lipoproteins.
- Lipoproteins containing SAA exhibited increased proteoglycan binding compared to SAA-free lipoproteins.
- Altered SAA lipoprotein distribution was observed postprandially in subjects with diabetes mellitus.
Conclusions:
- Serum amyloid A (SAA) is an exchangeable apolipoprotein.
- SAA enhances the proteoglycan binding of apoB-containing lipoproteins.
- The presence of SAA on apoB lipoproteins may play a role in cardiovascular disease development, particularly in individuals with diabetes mellitus and metabolic syndrome.
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