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Journal of Lipid Research, Vol 36, 148-157, Copyright © 1995 by Lipid Research, Inc.
TM Forte, JK Bielicki, R Goth-Goldstein, J Selmek and MR McCall
Studies were carried out to determine whether apolipoprotein (apo) A- II,
like apoA-I, can recruit phospholipid and cholesterol from cell membranes,
thereby forming nascent apoA-II-specific HDL. ApoA-II and apoA-I were
purified from plasma and each was incubated with CHO cells at a
concentration of 10 micrograms/ml. Lipid-containing complexes were isolated
from the medium in both cases; the composition of the apoA-II- and
apoA-I-specific complexes were similar where percent protein, phospholipid,
and cholesterol were 35 +/- 3, 38 +/- 2, and 25 +/- 1 for apoA-II,
respectively, and 40 +/- 2, 35 +/- 1, and 24 +/- 2 for apoA-I,
respectively. On a per mole of apolipoprotein basis, apoA-I recruited
significantly more phospholipid and cholesterol than dimeric apoA-II
suggesting that apoA-I with its greater number of alpha helices binds more
lipid. By electron microscopy, nascent apoA-II- and apoA-I- specific
particles were predominantly discoidal in morphology. ApoA-II complexes
were unique in their nondenaturing polyacrylamide gradient gel size
distribution as six distinct populations of particles with diameters of
8.1, 9.3, 10.4, 11.8, 13.1, and 14.6 nm were routinely noted, compared with
apoA-I which formed only three major populations with diameters of 7.3,
9.2, and 11.0 nm. Nascent apoA-I complexes incubated with purified
lecithin:cholesterol acyltransferase (LCAT) were transformed into
predominantly 8.4 nm particles. The latter is similar in size to plasma
HDL3a, LpA-I particles, suggesting that extracellularly assembled
apoA-I-lipid complexes can directly give rise to a major plasma LpA-I
subpopulation upon interaction with LCAT. Unlike apoA-I, apoA-II-lipid
complexes could not serve as substrates for LCAT and did not undergo
transformation. This study also demonstrates, for the first time, that
apoA-II and apoA-I show a preference in phospholipid recruitment from
membranes. Although phosphatidylcholine is the major phospholipid removed
by both apolipoproteins, apoA-II preferentially recruits
phosphatidylethanolamine (PE) as its second most abundant phospholipid
while apoA-I recruits sphingomyelin. As PE is usually associated with the
inner leaflet of the membrane, it is likely that dimeric apoA-II, compared
with apoA-I, can penetrate farther into the membrane and extract PE. This
ability of apoA-II to insert more deeply into the lipid milieu may explain
the known ability of apoA-II to resist dissociation from the mature HDL
particle.
ARTICLES
Recruitment of cell phospholipids and cholesterol by apolipoproteins A- II and A-I: formation of nascent apolipoprotein-specific HDL that differ in size, phospholipid composition, and reactivity with LCAT
Life Sciences Division, Lawrence Berkeley Laboratory, University of California, Berkeley 94720.
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