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J. Biol. Chem., Vol. 258, Issue 15, 9086-9092, 08, 1983
P Lindqvist, AM Ostlund-Lindqvist, JL Witztum, D Steinberg and JA Little
We have previously shown that cultured macrophages secrete lipoprotein
lipase (LPL) into the culture medium. The purpose of these experiments was
to determine the role of LPL in the uptake of very low density lipoproteins
(VLDL). Both J774 cells and mouse peritoneal macrophages took up and
degraded normotriglyceridemic VLDL in a saturable manner. Uptake of VLDL
was effectively competed for by rabbit beta-VLDL, human VLDL, but not by
native LDL or acetyl LDL. LPL activity accelerated saturable uptake of VLDL
but was not a prerequisite for it. This was most clearly seen in
experiments with apo-C-II-deficient VLDL. Although no hydrolysis of VLDL
triglyceride occurred, saturable uptake and degradation of the
C-II-deficient lipoprotein occurred. However, addition of apo-C-II enhanced
saturable uptake. Normal VLDL also promoted cellular accumulation of both
triglycerides and cholesteryl esters. Accumulation of triglyceride occurred
by uptake of intact VLDL particles, by uptake of a triglyceride-depleted
particle produced by the action of LPL, and by the direct uptake of free
fatty acids generated by the activity of LPL. In turn, the latter process
was influenced by the amount of albumin in the medium capable of being an
acceptor for free fatty acids. Finally, we have shown that when albumin is
present in the medium, the macrophage is capable of mobilizing most of its
stored triglyceride over 24 h, even as its cholesteryl ester content
remains constant. These studies may be relevant to the ability of VLDL to
promote macrophage accumulation of cholesteryl ester, even as triglyceride
accumulation is minimized.
The role of lipoprotein lipase in the metabolism of triglyceride-rich lipoproteins by macrophages
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