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(Received for publication, October 6, 1995, and in revised form, March 21, 1996)
From the Division of Biopharmaceutics, Leiden-Amsterdam Center for
Drug Research, University of Leiden, Sylvius Laboratories, 2300 RA
Leiden, The Netherlands
Apolipoprotein E (apoE) is an important
determinant for the liver uptake of triglyceride-rich lipoproteins and
emulsions by the remnant receptor. In the current study, we assessed an
additional role of apoE as modulator of the metabolism of
triglyceride-rich lipoproteins in vitro and in
vivo. Glycerol tri[3H]oleate
[14C]cholesteryl oleate double-labeled triglyceride-rich
emulsions were injected into fasted rats. The serum half-life of
glycerol tri[3H]oleate was 3-fold faster (5.4 min) than
that of [14C]cholesteryl oleate (16.7 min), confirming
lipoprotein lipase (LPL)-mediated processing. To establish a specific
effect of apoE on emulsion lipolysis rather than liver uptake, rats
were functionally hepatectomized, and hypo(apo)lipoproteinemia was
induced by 17 The mechanism and specificity of the effect of apoE on emulsion
lipolysis by purified LPL was assessed in vitro. Addition
of apoE to glycerol tri[3H]oleate-labeled emulsions led
to a concentration-dependent inhibition of
[3H]oleate release (9.5% residual LPL activity at 60 µg/ml apoE), while apoA-I was ineffective. The inhibitory effect of
apoE was not abolished by reductive methylation of lysine residues,
whereas selective modification of arginine residues by
1,2-cyclohexadione completely cancelled the inhibitory effect of
apoE.
It is concluded that apoE can specifically inhibit the LPL-mediated
hydrolysis of emulsion triglycerides both in vitro and
in vivo, and that arginine residues in apoE are essential
for this effect. We suggest that in addition to its role in receptor
recognition, apoE also modulates the LPL-mediated processing of
triglyceride-rich lipoproteins.
Volume 271, Number 25,
Issue of June 21, 1996
pp. 14791-14799
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
-ethinyl estradiol treatment. An apoE
concentration-dependent inhibition of emulsion-triglyceride
hydrolysis was observed, reaching a 14.8-fold increased half-life of
glycerol tri[3H]oleate as compared with that in the
absence of exogenous apoE.
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