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Cited by 240

Role of heparan sulfate proteoglycans in the binding and uptake of apolipoprotein E-enriched remnant lipoproteins by cultured cells

Ji, Z.S., Brecht, W.J., Miranda, R.D., Hussain, M.M., Innerarity, T.L., Mahley, R.W.·1993·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(18)82186-x
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Abstract

Addition of apolipoprotein (apo) E to rabbit beta-very low density lipoproteins (beta-VLDL) has been shown to result in a marked enhancement of their binding and uptake by various cell types. Apolipoprotein E binds to lipoprotein receptors and proteoglycans. To distinguish between apoE binding to these sites, cells were treated with heparinase. Heparinase treatment of receptor-negative familial hypercholesterolemic (FH) fibroblasts and human hepatoma cells (HepG2) released 30-40% of newly synthesized cell surface 35S-labeled proteoglycans and decreased the binding of beta-VLDL+apoE to FH and normal fibroblasts and HepG2 cells by more than 80%. Furthermore, heparinase treatment significantly decreased the uptake of fluorescently labeled beta-VLDL+apoE by HepG2 cells and decreased cholesteryl ester synthesis in FH fibroblasts by 75%. Likewise, canine chylomicron remnants enriched in apoE demonstrated enhanced binding that was 80% inhibited by heparinase treatment of HepG2 cells. Heparinase treatment did not affect beta-VLDL (without added apoE) or low density lipoprotein (LDL) binding to these cells or the binding activity of beta-VLDL+apoE to the LDL receptor-related protein (LRP) or to the LDL receptor on ligand blots. Chinese hamster ovary (CHO) mutant cells lacking the synthesis of either heparan sulfate (pgsD-677) or all proteoglycans (pgsA-745) did not display any enhanced binding of the beta-VLDL+apoE. By comparison, wild-type CHO cells demonstrated enhanced binding of b…

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  • LRP1 can form complexes with HSPGs, allowing ligands such as APOE to either bind directly to the LRP1-HSPG complex or initially interact with HSPGs before being transferred to LRP1 for endocytosis.

    “Research indicates that LRP1 can form complexes with HSPGs, allowing ligands such as APOE to either bind directly to the LRP1–HSPG complex or initially interact with HSPGs before being transferred to LRP1 for endocytosis. 45”

    From Protective mechanisms against Alzheimer's disease in APOE3‐Christchurch homozygous astrocytes (2025) · cites this paper as [45]

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Authors
Ji, Z. S., Brecht, W. J., Miranda, R. D., Hussain, M. M., Innerarity, T. L., & Mahley, R. W.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1993-05
Volume
268
Issue
14
Pages
10160-10167
ISSN
0021-9258
DOI
10.1016/s0021-9258(18)82186-x
Cited by
240
References
0
Language
en
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