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Arteriosclerosis, Thrombosis, and Vascular Biology. 1995;15:1412-1418

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(Arteriosclerosis, Thrombosis, and Vascular Biology. 1995;15:1412-1418.)
© 1995 American Heart Association, Inc.


Articles

Cholesterol Efflux, Cholesterol Esterification, and Cholesteryl Ester Transfer by LpA-I and LpA-I/A-II in Native Plasma

Yadong Huang; Arnold von Eckardstein; Shili Wu; Gerd Assmann

From the Institut für Arterioskleroseforschung an der Universität Münster (Y.H., S.W., G.A.) and the Institut für Klinische Chemie und Laboratoriumsmedizin, Zentrallaboratorium, Westfälische Wilhelms-Universität Münster (A. von E., G.A.), Germany.

Correspondence to Yadong Huang, Institut für Arterioskleroseforschung an der Universität Münster, Domagkstr 3, D-48149 Münster, Federal Republic of Germany.

Abstract HDLs encompass structurally heterogeneous particles that fulfill specific functions in reverse cholesterol transport. Two-dimensional nondenaturing polyacrylamide gradient gel electrophoresis (2D-PAGGE) of normal plasma and subsequent immunoblotting with anti–apolipoprotein (apo) A-I antibodies differentiates an abundant particle with electrophoretic {alpha}-mobility and less abundant particles with electrophoretic pre-ß-mobility (preß1–LpA-I, preß2–LpA-I, preß3–LpA-I). Immunodetection with anti–apoA-II antibodies identifies a single particle with {alpha}-mobility. To differentiate {alpha}-migrating HDL without apo A-II ({alpha}–LpA-I) from those with apoA-II ({alpha}–LpA-I/A-II), we combined 2D-PAGGE with immunoadsorption of apoA-II. Incubation of plasma with [3H]cholesterol-labeled fibroblasts in combination with immunosubtracting 2D-PAGGE allowed us to analyze the role of {alpha}–LpA-I and {alpha}–LpA-I/A-II in the uptake and esterification of cell-derived cholesterol in native plasma. Depending on the duration of incubations with cells, {alpha}-LpA-I took up two to four times more [3H]cholesterol than {alpha}–LpA-I/A-II. Irrespective of the duration of incubation, two to three times more [3H]cholesteryl esters accumulated in {alpha}–LpA-I than in {alpha}–LpA-I/A-II. Subsequent incubations in the presence of an inhibitor of lecithin:cholesterol acyltransferase led to preferential accumulation of [3H]cholesteryl esters in {alpha}–LpA-I/A-II. In conclusion, our data indicate that {alpha}–LpA-I is more effective than {alpha}–LpA-I/A-II in both uptake and esterification of cell-derived cholesterol. Moreover, {alpha}–LpA-I/A-II appears to accumulate cholesteryl esters, at least partially, from {alpha}–LpA-I.


Key Words: apoA-II • HDL subclasses • reverse cholesterol transport • cholesterol efflux




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