NDLI: Low density lipoprotein receptor-related protein mediates uptake of cholesteryl esters derived from apoprotein E-enriched lipoproteins.

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Low density lipoprotein receptor-related protein mediates uptake of cholesteryl esters derived from apoprotein E-enriched lipoproteins.

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Low density lipoprotein receptor-related protein mediates uptake of cholesteryl esters derived from apoprotein E-enriched lipoproteins.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Herz, J. Esser, V. Brown, M. S. Kowal, R. C. Goldstein, J. L.
Description	Author Affiliation: Kowal RC ( Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.);
Abstract	Low density lipoprotein receptor-related protein (LRP) is a recently described cell-surface protein of 4544 amino acids that contains reiterated sequences found in the 839-amino acid receptor for low density lipoprotein (LDL). In the current studies, we purified LRP from rat liver, prepared polyclonal antibodies that recognize the extracellular domain, and demonstrated an immunoreactive protein of approximately 600 kDa in human fibroblasts. The function of this LRP was studied in mutant human fibroblasts that do not produce LDL receptors. The mutant cells were incubated with beta-migrating very low density lipoprotein (beta-VLDL) that was isolated from cholesterol-fed rabbits and artificially enriched with apoprotein (apo) E by incubation in vitro with human apo E produced in a bacterial expression system. The apo E-enriched beta-VLDL, but not unincubated beta-VLDL, stimulated incorporation of [14C]-oleate into cholesteryl [14C]oleate 20- to 40-fold in the mutant cells. This stimulation was blocked by chloroquine, suggesting that such stimulation resulted from receptor-mediated uptake and lysosomal hydrolysis of the cholesteryl esters in apo E-enriched beta-VLDL. Stimulation of cholesterol esterification was blocked by the antibody against LRP, but not by an antibody against the LDL receptor. Unlike the LDL receptor, the amount of LRP was not reduced when cells were incubated with oxygenated sterols. We conclude that LRP can mediate the cellular uptake and lysosomal hydrolysis of cholesteryl esters contained in lipoproteins that are enriched in apo E.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	86
Language	English
Publisher	National Academy of Sciences
Publisher Date	1989-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Apolipoproteins E Metabolism Cholesterol Esters Liver Receptors, Immunologic Receptors, LDL Animals Cells, Cultured Chloroquine Pharmacology Fibroblasts Drug Effects Lipoproteins, VLDL Low Density Lipoprotein Receptor-Related Protein-1 Molecular Weight Mutation Oleic Acid Oleic Acids Biosynthesis Isolation & Purification Skin Triglycerides Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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