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National Cholesterol Awareness Month |
From the Graduate Center for Nutritional Science (M.C.d.B., N.R.W., N.L.W., J.M.W., A.J., D.R.v.d.W., F.C.d.B.), the Cardiovascular Research Center (M.C.d.B., N.R.W., N.L.W., J.M.W., A.J., D.R.v.d.W., F.C.d.B.), and the Departments of Physiology (M.C.d.B.) and Internal Medicine (N.R.W., N.L.W., J.M.W., A.J., D.R.v.d.W., F.C.d.B.), University of Kentucky Medical Center, Lexington; and the Department of Veterans Affairs Medical Center (F.C.d.B.), Lexington, Ky.
Correspondence to Maria C. de Beer, PhD, Room 527 CT Wethington Bldg, 900 S Limestone Street, Lexington, KY 40536. E-mail mdebeer{at}uky.edu
Abstract
Objective— The purpose of this study was to investigate the interaction of SAA and SR-BI in remodeling of acute phase HDL (AP HDL).
Methods and Results— We used SAA and SR-BI adenoviral vector expression models to study the interaction between these entities. SR-BI processing of mouse AP HDL generated progressively smaller discreet HDL particles with distinct apolipoprotein compositions. SR-BI actions segregated apolipoproteins with the smallest particles containing only apoA-I. Larger remnants contained apoA-I, apoA-II, and SAA. Small apoA-I only particles failed to associate with preformed HDL, whereas larger remnants readily did. The presence of SAA on SR-BI-processed HDL particles propelled apoA-I to a small lipid-poor form and accelerated apoA-I catabolism.
Conclusions— Data indicate that after core and surface HDL lipid perturbation by SR-BI, SAA propels apoA-I to a small lipid-poor form while accelerating HDL metabolism.
SR-BI processing of AP HDL segregates apolipoprotein metabolism. A small apoA-I only remnant is generated. It fails to associate with preformed HDL. SAA displaces apoA-I from SR-BI remnants.
Key Words: SAA HDL inflammation SR-BI metabolism
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