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Journal of Lipid Research, Vol 29, 869-882, Copyright © 1988 by Lipid Research, Inc.
S Azhar, A Cooper, L Tsai, W Maffe and E Reaven
Recent findings from this laboratory have led to the suggestion that the
hormone-producing cells of the rat luteinized ovary in situ may obtain a
large share of low density lipoprotein (LDL) cholesterol without actually
internalizing the intact lipoprotein particles. We have shown that the
lipoproteins are trapped at the surface of the luteal cells in a rich
network of "microvillar channels" and have theorized that these channel
membranes, with their large surface area for interacting with lipoprotein
particles, may function in the cholesterol transfer process. In the current
study, we try to establish what proportion of the human (h)LDL-cholesterol
transfer in the in situ perfused tissue occurs by a classical apoB, E
receptor-mediated process versus a surface extraction process. We examine
the tissue for the presence of apoB, E receptors, and characterize the
structural/functional interaction of hLDL with the apoB, E receptor
utilizing a variety of modified hLDL particles as probes. Then, using
nonmetabolizable radiolabels for both the protein and cholesteryl ester
moieties of these LDL probes, we attempt to quantify the extent to which
apoB, E receptors in the ovary contribute to the uptake of hLDL-
cholesterol during steroidogenesis. Our experiments show that although the
luteinized ovary contains apoB, E receptor protein, hLDL interacts with the
tissue atypically. That is, despite modifications of LDL amino acid
residues to prevent interaction with the apoB, E receptor, the modified
ligands continue to contribute cholesterol for luteal cell internalization
and/or steroidogenesis. We conclude, therefore, that in this tissue much of
the LDL-cholesterol is not delivered by the apoB, E receptor pathway.
ARTICLES
Characterization of apoB, E receptor function in the luteinized ovary
Department of Medicine, Stanford University School of Medicine, Palo Alto, CA 94305.
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