Abstract
The relationship between LCAT mediated HDL modification and the redistribution of lipoprotein-unassociated apoA-IV to HDL was investigatedin vitro. Immunoaffinity-isolated rat lipoprotein-unassociated apoA-IV was added to apoB-, apoE-, apoA-IV depleted, [3H]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 the3H label retained by an anti-apoA-IV immunoaffinity column. Lipoproteins retained by the anti-apoA-IV immunoaffinity column had experienced a greater conversion of [3H]cholesterol to [3H]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.
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Abbreviations
- HDL:
-
high density lipoproteins
- EDTA:
-
ethylene-diaminetetraacetic acid
- DTNB:
-
5,5′-dithiobis(2-nitrobenzoic acid); apo, apolipoprotein
- PBS:
-
phosphate buffered saline
- LCAT:
-
lecithin:cholesterol acyltransferase
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Lefevre, M., Goudey-Lefevre, J.C. & Roheim, P.S. Preferential redistribution of lipoprotein-unassociated apoA-IV to an HDL subpopulation with a high degree of LCAT modification. Lipids 24, 1035–1038 (1989). https://doi.org/10.1007/BF02544075
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DOI: https://doi.org/10.1007/BF02544075