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Journal of Lipid Research, Vol 37, 1802-1811, Copyright © 1996 by Lipid Research, Inc.
K Aalto-Setala, PH Weinstock, CL Bisgaier, L Wu, JD Smith and JL Breslow
We previously showed that human apoC-III expression in transgenic mice
causes hypertriglyceridemia due to the accumulation of enlarged very low
density lipoprotein (VLDL)-like particles, with increased triglycerides and
apoC-III and decreased apoE. In vivo turnover studies indicated the
metabolic basis was decreased particle fractional catabolic rate. The
presence of enlarged triglyceride-rich particles with prolonged residence
time in plasma implied defective lipolysis, but in vitro these particles
were good substrates for purified lipoprotein lipase (LPL). In the current
study we further characterize the metabolic properties of these particles.
We show that expression of a mouse apoC-III transgene can also cause
hypertriglyceridemia with a similar accumulation of a VLDL-like particle
with increased apoC-III and decreased apoE. A vitamin A fat tolerance test
was used to show that MoCIIITg and HuCIIITg mice had similarly delayed
clearance of triglyceride-rich postprandial particles. Thus, the previously
observed hypertriglyceridemia caused by human apoC-III transgene expression
was not due interspecies incompatibility but a property of apoC-III. In
further experiments we showed VLDL from apoC-III transgenic mice interacted
poorly with fibroblast lipoprotein receptors and this could be corrected by
adding exogenous apoE. In addition, control VLDL interaction could be
decreased by exogenous apoC-III. Moreover, the hypertriglyceridemia of
HuCIIITg mice could be normalized by crossbreeding with HuETg mice. Thus, a
functionally significant reciprocal relationship of apoC-III and apoE
exists, presumably due to competition for space on the surface of
triglyceride-rich lipoproteins. Finally, VLDL from HuCIITg and MoCIIITg
mice showed decreased binding to heparin-Sepharose. This suggests and
additional locus of the defect in these mice could potentially be in the
binding of triglyceride-rich lipoproteins to heparan sulfate proteoglycan
matrix on the surface of endothelial cells in which LPL is embedded. This
could explain the predicted functional lipase deficiency in apoC-III
transgenic mice based on the observation of a prolonged residence time of
enlarged triglyceride-rich lipoproteins.
ARTICLES
Further characterization of the metabolic properties of triglyceride- rich lipoproteins from human and mouse apoC-III transgenic mice
Laboratory of Biochemical Genetics and Metabolism, Rockefeller University, New York, NY 10021-6399, USA.
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