Abstract:
: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, [3H]cholesterol labelled rat plasma and incubated at 37 degrees 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 3H 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 LCAT-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.
journal_name
Lipidsjournal_title
Lipidsauthors
Lefevre M,Goudey-Lefevre JC,Roheim PSdoi
10.1007/BF02544075subject
Has Abstractpub_date
1989-12-01 00:00:00pages
1035-8issue
12eissn
0024-4201issn
1558-9307journal_volume
24pub_type
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