Glycosylation of Human Apolipoprotein E
Open accessAbstract
The glycosylation of human apolipoprotein (apo) E was examined with purified plasma apoE and apoE produced by transfected cell lines. The carbohydrate attachment site of plasma apoE was localized to a single tryptic peptide (residues 192-206). Sequence analysis and amino sugar analysis of this peptide derived from asialo-, monosialo-, or disialo-apoE indicated that the carbohydrate moiety is attached only to Thr194 in monosialo- and disialo-apoE and that asialo-apoE is not glycosylated. Mammalian cells that normally do not express apoE were transfected with human apoE plasmid expression vectors to test the utilization of potential carbohydrate attachment sites and the role of apoE glycosylation in secretion. Site-specific mutants of apoE, designed to eliminate or alter glycosylation sites, were expressed in HeLa cells by acute transfection. Apolipoprotein E(Thr194----Ala) was secreted exclusively as the asialo isoform, confirming that Thr194 is the site of carbohydrate attachment in these cells and indicating that glycosylation of apoE is not essential for secretion. Apolipoprotein E(Thr194----Asn,Gly196----Ser), which introduces a potential site for N-glycosylation at position 194, was secreted with a higher apparent molecular weight than native, O-glycosylated apoE. Studies with tunicamycin indicated that this apoE was N-glycosylated at Asn194. Stably transfected cell lines expressing human apoE were prepared from wild-type Chinese hamster ovary (CHO) cells and from CHO ldl…
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The underglycosylation of apoE Leiden probably is due to a change in accessibility of the glycosylation site to the cell's glycosylation machinery.
“since the only glycosylation site in apoE is at threonine 194 (16), the underglycosylation of apoE Leiden probably is due to a change in accessibility of the glycosylation site to the cell's glycosylation machinery.”
From Preferential association of apolipoprotein E Leiden with very low density lipoproteins of human plasma. (1993) · cites this paper as [16]
Glycosylation is not necessary for proper intracellular processing and secretion of apoE.
“glycosylation is not necessary for proper intracellular processing and secretion of the protein (16)”
From Preferential association of apolipoprotein E Leiden with very low density lipoproteins of human plasma. (1993) · cites this paper as [16]
The only glycosylation site in apoE is at threonine 194.
“since the only glycosylation site in apoE is at threonine 194 (16)”
From Preferential association of apolipoprotein E Leiden with very low density lipoproteins of human plasma. (1993) · cites this paper as [16]
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Apolipoprotein E: Far More Than a Lipid Transport Protein
Mahley, R. W., & Rall, S. C. (2000) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.1.1.507 · Cited by 1,836 · see citing works
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Implications of Glycosylation in Alzheimer’s Disease
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Extracellular Proteolysis of Apolipoprotein E (apoE) by Secreted Serine Neuronal Protease
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- Authors
- Wernette-Hammond, M. E., Lauer, S. J., Corsini, A., Walker, D., Taylor, J. M., & Rall, S. C.
- Affiliations
- Gladstone Institutes (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1989-05
- Volume
- 264
- Issue
- 15
- Pages
- 9094-9101
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1585967257
- Cited by
- 149
- References
- 4
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 4 · 2023: 10 · 2022: 11 · 2021: 6 · 2020: 4 · 2019: 6 · 2018: 2 · 2017: 2 · 2016: 6 · 2015: 1 · 2014: 5 · 2013: 1 · 2012: 4
- FWCI
- 2.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- apolipoprotein E, glycosylation, N-glycosylation, O-glycosylation, sialic acid, carbohydrate attachment sites, site-directed mutagenesis, protein secretion, tunicamycin
- MeSH terms
- Animals, Apolipoproteins E, Cell Line, Genetic Vectors, Glycosylation, HeLa Cells, Humans, Models, Molecular, Plasmids, Protein Conformation, Threonine, Transfection, Restriction Mapping
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