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Journal of Lipid Research, Vol 36, 1557-1566, Copyright © 1995 by Lipid Research, Inc.
F Karpe and M Hultin
The rat liver secretes very low density lipoproteins (VLDL) containing
either apoB-100 or apoB-48. After oral fat intake, chylomicrons containing
apoB-48 and endogenously synthesized VLDL are mixed in the blood and the
triglyceride clearance from these triglyceride-rich lipoprotein species
compete for the same lipolytic pathway, i.e., lipoprotein lipase. A
situation mimicking alimentary lipemia was induced by a short-term
intravenous primed infusion of a chylomicron- like triglyceride emulsion to
fed and fasted rats. The plasma concentration of apoB-100 and apoB-48 was
monitored in triglyceride- rich lipoprotein subfractions after separation
with density gradient ultracentrifugation by analytical SDS-PAGE. The net
liver secretory output of VLDL was quantified by lipolytic blockade induced
by Triton WR 1339. The chylomicron-like triglyceride emulsion induced a
linear increase of large VLDL (Sf 60-400 subfraction containing both
apoB-100 and apoB-48), almost to the same extent as that induced by Triton.
The clearance of postprandial triglyceride-rich lipoproteins and both
lipolysis and clearance of intravenously injected labeled rat chylomicrons
was efficiently inhibited by the emulsion but not so complete as for
fasting VLDL. The linearity of the VLDL increase and the very early
response in the Intralipid-treated rats suggest that enhanced synthesis of
VLDL is not a major cause for the accumulation. Rather, the present data
indicate that a high plasma concentration of a chylomicron-like
triglyceride emulsion competes efficiently with liver- derived VLDL for the
same lipolytic pathway, which leads to accumulation in plasma of endogenous
VLDL in the postprandial state.
ARTICLES
Endogenous triglyceride-rich lipoproteins accumulate in rat plasma when competing with a chylomicron-like triglyceride emulsion for a common lipolytic pathway
Atherosclerosis Research Unit, King Gustaf V Research Institute, Stockholm, Sweden.
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