Apolipoprotein E5 (Glu212–>Lys): increased binding to cell surface proteoglycans but decreased uptake and lysosomal degradation in cultured fibroblasts.

Feussner, G; Scharnagl, H; Scherbaum, C; Acar, J; Dobmeyer, J; Lohrmann, J; Wieland, H; März, W

doi:10.1016/s0022-2275(20)39106-9

Cited by 21Lipid metabolism and disordersLipoproteins and Cardiovascular HealthCholesterol and Lipid Metabolism

Apolipoprotein E5 (Glu212–>Lys): increased binding to cell surface proteoglycans but decreased uptake and lysosomal degradation in cultured fibroblasts.

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Feussner, G, Scharnagl, H, Scherbaum, C, Acar, J, Dobmeyer, J, Lohrmann, J, Wieland, H, März, W·1996·Journal of Lipid Research

DOI 10.1016/s0022-2275(20)39106-9

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Abstract

A new apolipoprotein (apo) E variant, apoE5 (Glu212-->Lys) was identified in a Turkish family. The variant was due to a point mutation (CAG-->AAG) at the first nucleotide position of the codon encoding amino acid residue 212 of the mature apoE. The 23-year-old index patient was heterozygous for the mutation. Examination of the proband's kindred revealed six heterozygous and two homozygous mutation carriers. Compared to non-carriers, carriers of the mutation had slightly higher triglycerides (1.25 versus 1.11 g/l) and lower HDL cholesterol (0.36 versus 0.41 g/l). Very low density lipoproteins (VLDL) from an apoE5 (Glu212-->Lys) homozygote displayed enhanced binding (+17%, P < 0.05), but decreased uptake (-35%, P < 0.0001) and degradation (-51%, P < 0.0001) in cultured fibroblasts, compared to E3/3-VLDL. The region of the apoE molecule surrounding residue 212 contains a heparin binding domain. Consistently, the enhanced cell surface binding of E5/5-VLDL was observed in "wild-type" Chinese hamster ovary cells (+19%, P < 0.05), but not in proteoglycan-deficient cells. The binding of E5/5-VLDL to heparin was increased (+22%, P < 0.05). As the endocytosis of apoE-containing particles involves the transfer of proteoglycan-bound ligands to lipoprotein receptors, the stronger binding of apoE5 (Glu212-->Lys) to proteoglycans could reduce the rate at which the mutant is finally delivered to endocytotic pathways. These data may provide evidence for a functionally important heparin binding site around amino acid residue 212 of the apoE molecule in vivo.

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APOE5 (Glu212Lys) was identified in a Turkish family.
“Elsewhere, APOE5 (Glu212Lys) was identified in a Turkish family124).”
From Impact of Apolipoprotein E Variants: A Review of Naturally Occurring Variants and Clinical Features (2025) · cites this paper as [124]
Examination of the proband's kindred revealed six heterozygous and two homozygous variant carriers of APOE5 (Glu212Lys).
“Examination of the proband’s kindred revealed six heterozygous and two homozygous variant carriers.”
From Impact of Apolipoprotein E Variants: A Review of Naturally Occurring Variants and Clinical Features (2025) · cites this paper as [124]
Compared with non-carriers, carriers of APOE5 (Glu212Lys) had slightly higher triglyceride levels (110.7 versus 98.3 mg/L).
“Compared with the non-carriers, carriers of the variant had slightly higher triglyceride levels (110.7 versus 98.3 mg/L).”
From Impact of Apolipoprotein E Variants: A Review of Naturally Occurring Variants and Clinical Features (2025) · cites this paper as [124]
Individuals with apoE5 develop type II HLP and vulnerability to atherosclerosis due to hypercholesterolemia.
“individuals with apoE5 develop type II HLP [8] and vulnerability to atherosclerosis due to hypercholesterolemia [9].”
From A case of lipoprotein glomerulopathy with a rare apolipoprotein E isoform combined with neurofibromatosis type I (2018) · cites this paper as [9]

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Authors: Feussner, G., Scharnagl, H., Scherbaum, C., Acar, J., Dobmeyer, J., Lohrmann, J., Wieland, H., & März, W.
Affiliations: University Hospital Heidelberg (DE)
ORCID: Scharnagl, H
März, W
Venue: Journal of Lipid Research
Publisher: Elsevier BV
Published: 1996-01
Volume: 37
Issue: 8
Pages: 1632-1645
ISSN: 0022-2275 (ISSN-L)
DOI: 10.1016/s0022-2275(20)39106-9
OpenAlex: W2346307077
Cited by: 21
References: 46
Citations by year: 2025: 1 · 2024: 1 · 2022: 1 · 2021: 1 · 2018: 1 · 2015: 1 · 2014: 1 · 2013: 1
FWCI: 1.19
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 9033 d)
Locations: Journal of Lipid Research (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Topics: Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
Health Sciences › Medicine › Surgery › Lipoproteins and Cardiovascular Health
Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
Keywords: heparin-binding domain, proteoglycan binding, lysosomal degradation, endocytosis, lipoprotein receptors, triglycerides, HDL cholesterol, familial hypertriglyceridemia, fibroblasts
MeSH terms: Adolescent, Adult, Animals, Apolipoproteins E, Binding, Competitive, Cells, Cultured, Child, Child, Preschool, Endocytosis, Exons, Female, Fibroblasts, Cricetinae, Heparin, Humans, Hyperlipidemia, Familial Combined, Interpersonal Relations, Lipoproteins, VLDL, Male, Middle Aged, Pedigree, Phenotype, Proteoglycans, CHO Cells, Point Mutation

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Apolipoprotein E5 (Glu212–>Lys): increased binding to cell surface proteoglycans but decreased uptake and lysosomal degradation in cultured fibroblasts.

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