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Journal of Lipid Research, Vol 26, 11-25, Copyright © 1985 by Lipid Research, Inc.
CL Bisgaier, OP Sachdev, L Megna and RM Glickman
Human apoA-IV was purified from delipidated urinary chylomicrons.
Monospecific antibodies were raised in rabbits and used to develop a double
antibody radioimmunoassay (RIA). Displacement of 125I-labeled apoA-IV by
plasma or purified chylomicron apoA-IV resulted in parallel displacement
curves, indicating that apoA-IV from both sources share common antigenic
determinants. The apoA-IV level in plasma from normal healthy fasting male
subjects (n = 5) was 37.4 +/- 4.0 mg/dl, while fat- feeding increased the
level to 49.1 +/- 7.9 mg/dl (P less than 0.05) at 4 hr. The apoA-IV level
in plasma from abetalipoproteinemic fasting subjects was 13.7 +/- 3.1 mg/dl
(n = 5). Plasma from a single fasting Tangier subject showed a reduced
apoA-IV level of 21.1 mg/dl. The distribution of apoA-IV in fasting and
postprandial plasma was determined by 6% agarose gel chromatography.
Fifteen to 25% of plasma apoA-IV eluted in the region of plasma high
density lipoprotein (HDL), with the remainder eluting in subsequent column
fractions. In abetalipoproteinemic plasma this HDL fraction is reduced and
lacks apoA- IV, suggesting that at least some of the apoA-IV on these
particles is normally derived from triglyceride-rich lipoproteins. Lipemic
plasma from a fat-fed subject showed a small rise (3%) in chylomicron-
associated apoA-IV. Gel-filtered HDL and subsequent apoA-IV-containing
fractions were subjected to 4-30% polyacrylamide gradient gel
electrophoresis (4/30 GGE), and apoA-IV was identified by
immunolocalization following transfer of proteins to nitrocellulose paper.
In normal plasma apoA-IV was localized throughout all HDL fractions. In
addition, normal plasma contained apoA-IV localized in a small particle
(diameter 7.8-8.0 nm). This particle also contained apoA- I and lipid. A
markedly elevated saturated to unsaturated cholesteryl ester ratio was
present in gel-filtered plasma fractions containing small HDL, suggesting
an intracellular origin of these particles. In abetalipoproteinemic plasma
apoA-IV was absent from all HDL fractions except for the small HDL
particles, suggesting that they are not derived from the surface of
triglyceride-rich particles. All plasmas contained free apoA-IV. In
contrast to gel-filtered plasma, lipoprotein subfractions of fasted normal
plasma prepared in the ultracentrifuge primarily contained apoA-IV in the d
greater than 1.26 g/ml fraction, suggesting an artifactual redistribution
of the apolipoprotein during centrifugation. Overall, these data suggest
that apoA-IV secretion into plasma is increased with fat feeding, and that
apoA-IV normally exists as both a free apolipoprotein and in association
with HDL particles.
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Distribution of apolipoprotein A-IV in human plasma
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