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Journal of Lipid Research, Vol 37, 1733-1742, Copyright © 1996 by Lipid Research, Inc.
A Niemeier, M Gafvels, J Heeren, N Meyer, B Angelin and U Beisiegel
The VLDL receptor has been described as a new member of the LDL receptor
supergene family that specifically binds VLDL in vitro via apolipoprotein E
and lipoprotein lipase. Both apolipoprotein E and lipoprotein lipase are
constituents of chylomicron remnants, another triglyceride-rich lipoprotein
which has been proposed as a physiological ligand for the VLDL receptor. We
used human chylomicron remnants to study their uptake into LDL,
receptor-deficient Chinese hamster ovary cells overexpressing the human
VLDL receptor. The uptake into these cells was compared to that into cells
transfected with an empty transfection vector. Human chylomicron remnants
were produced in vitro by hydrolysis with lipoprotein lipase, and were
labeled with 125I. The uptake of these remnants into the cells
overexpressing the VLDL receptor was found to be about 3-fold higher than
the uptake into the control cells. The addition of a surplus of either
apolipoprotein E or inactivated lipoprotein lipase to the remnants led to
an increase in particle uptake. The chylomicron remnant uptake was
inhibited by addition of the 39 kDa receptor associated protein These in
vitro experiments strongly support the idea that the VLDL receptor is a
physiological receptor for chylomicron remnants. The increase of
receptor-mediated uptake induced by the addition of apoE or lipoprotein
lipase underlines the role of these two proteins in this process.
ARTICLES
VLDL receptor mediates the uptake of human chylomicron remnants in vitro
Medizinische Klinik, Universitatskrankenhaus Eppendorf, Hamburg, Germany.
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