Premium
Preferential redistribution of lipoprotein‐unassociated apoA‐IV to an HDL subpopulation with a high degree of LCAT modification
Author(s) -
Lefevre Michael,
GoudeyLefevre Jo C.,
Roheim Paul S.
Publication year - 1989
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02544075
Subject(s) - cholesterol , chemistry , lipoprotein , apolipoprotein b , clinical chemistry , redistribution (election) , chromatography , biochemistry , high density lipoprotein , apolipoprotein e , reverse cholesterol transport , lipoprotein particle , lipidology , intermediate density lipoprotein , in vitro , very low density lipoprotein , medicine , disease , politics , political science , law
The relationship between LCAT mediated HDL modification and the redistribution of lipoprotein‐unassociated apoA‐IV to HDL was investigated in vitro . Immunoaffinity‐isolated rat lipoprotein‐unassociated apoA‐IV was added to apoB‐, apoE‐, apoA‐IV depleted, [ 3 H]cholesterol labelled rat plasma and incubated at 37°C. The addition of lipoprotein‐unassociated apoA‐IV resulted in a modest (10%) but significant reduction in the rate of cholesterol esterification. Incubations conducted in the presence of active LCAT led to a time‐dependent increase in the amount of the 3 H label retained by an anti‐apoA‐IV immunoaffinity column. Lipoproteins retained by the anti‐apoA‐IV immunoaffinity column had experienced a greater conversion of [ 3 H]cholesterol to [ 3 H]cholesteryl esters (48% esterification at 30 min) than the unretained lipoproteins (19% esterification at 30 min). These data suggest that during the course of LACT‐induced cholesterol esterification, lipoprotein‐unassociated apoA‐IV transfers to a subpopulation of HDL which has been modified by LCAT to a greater extent than the remaining HDL. Further analysis of the data demonstrates that 48% cholesterol esterification is sufficient to allow apoA‐IV to be accommodated on the surface of an HDL particle.