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(Arteriosclerosis, Thrombosis, and Vascular Biology. 1995;15:1755-1763.)
© 1995 American Heart Association, Inc.

Articles

Lipoproteins Containing Apolipoprotein A-IV but Not Apolipoprotein A-I Take Up and Esterify Cell-Derived Cholesterol in Plasma

Arnold von Eckardstein; Yadong Huang; Shili Wu; Ahmad Saadat Sarmadi; Sigrid Schwarz; Armin Steinmetz; Gerd Assmann

From the Institut für Klinische Chemie und Laboratoriumsmedizin, Zentrallaboratorium, Westfälische Wilhelms-Universität Münster (A.von E., A.S.S., G.A.), FRG; the Institut für Arterioskleroseforschung an der Universität Münster (Y.H., S.W., G.A.); and the Abteilung für Endokrinologie und Stoffwechsel, Zentrum Innere Medizin, Philipps-Universität Marburg (S.S., A.S.).

Correspondence to Arnold von Eckardstein, Institut für Klinische Chemie und Laboratoriumsmedizin, Zentrallaboratorium, Westfälische Wilhelms-Universität Münster, Albert-Schweitzer-Strasse 33, D-48129 Münster, FRG.

Abstract Two-dimensional nondenaturing polyacrylamide gradient gel electrophoresis (2D-PAGGE) identifies distinct apoA-I– or apoE-containing subclasses of high-density lipoproteins (HDLs), each of which plays a different role in reverse cholesterol transport. In this study we used 2D-PAGGE to investigate the role of apoA-IV–containing lipoproteins in reverse cholesterol transport in native plasma. Incubation of 2D electrophoretograms with anti–apoA-IV antibodies identified up to three subclasses of particles. The smaller particle subclasses, LpA-IV-1 and LpA-IV-2, were found in every plasma sample. The largest particle subclass, LpA-IV-3, was observed in fewer than 10% of the plasmas analyzed. 2D-PAGGE of apoA-I–deficient plasma and apoA-I–depleted plasma and anti–apoA-I immunosubtracting 2D-PAGGE of normal plasma revealed that LpA-IV-1 and LpA-IV-2 do not contain apoA-I. The importance of LpA-IV-1 and LpA-IV-2 for uptake and esterification of cell-derived cholesterol was investigated using pulse-chase incubations of plasma with [³H]cholesterol-labeled fibroblasts followed by anti–apoA-I immunosubtracting 2D-PAGGE. During 1-minute pulse incubation with cells, [³H]cholesterol was taken up by -LpE >LpA-IV-1 >pre-ß₁-LpA-I >LpA-IV-2 (">" denotes "more than"). During subsequent chase incubation without cells, proportionately less radioactivity disappeared from LpA-IV-1 and LpA-IV-2 than from pre-ß₁-LpA-I and -LpE. During 5-minute pulse incubations, radioactive cholesteryl esters were formed in pre-ß₃-LpA-I >-LpA-I >LpA-IV-1 >LpA-IV-2. The fractional esterification rate was highest in pre-ß₃-LpA-I and lowest in -LpA-I. Subsequent chase led to the disappearance of [³H]cholesteryl esters from pre-ß₃-LpA-I and, to a lesser extent, from LpA-IV-1 and LpA-IV-2 but to an increase of [³H]cholesteryl esters in -LpA-I and LDL. Similar pulse-chase experiments with apoA-I–deficient plasma revealed that LpA-IV-1 and LpA-IV-2 take up and esterify cell-derived cholesterol even more effectively than in normal plasma. We conclude that LpA-IV-1 and LpA-IV-2 are apoA-I–free lipoproteins that are important contributors to reverse cholesterol transport.

Key Words: lecithin:cholesterol acyltransferase • HDL subfractions • reverse cholesterol transport • cholesterol efflux • nondenaturing two-dimensional electrophoresis

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