Article
Apolipoprotein E isoforms and rare mutations: parallel reduction in binding to cells and to heparin reflects severity of associated type III hyperlipoproteinemia.
Journal of lipid research - 1 Mar 1995
Mann W A, Meyer N, Weber W, Meyer S, Greten H, Beisiegel U
Abstract excerpt
The LDL receptor-independent binding of human apolipoprotein E isoforms and rare apoE mutations were studied on LDL receptor-deficient human fibroblasts using chemical cross-linking and cell binding studies. The cross-linking experiments demonstrated that all apoE variants bind to the low density lipoprotein receptor-related protein, a potential receptor for remnant lipoproteins. In cell binding studies, the...
Topics
- Animals
- Apolipoproteins E
- Cells, Cultured
- Fibroblasts
- Genetic Variation
- Heparin
- Humans
- Hyperlipoproteinemia Type III
- In Vitro Techniques
- Lipoproteins, VLDL
- Low Density Lipoprotein Receptor-Related Protein-1