Isoform-specific interactions of human apolipoprotein E to an intermediate conformation of human Alzheimer amyloid-beta peptide
| Autor: | Christine Castle, Bruce M. Taylor, Donald B. Carter, George W. Melchior, Nancy C. Stratman, Dennis E. Epps |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Apolipoprotein E
Gene isoform Apolipoprotein E2 Amyloid beta Apolipoprotein E4 Apolipoprotein E3 Enzyme-Linked Immunosorbent Assay Peptide Plasma protein binding Biochemistry Pathogenesis Apolipoproteins E Protein structure mental disorders Humans Protein Isoforms Molecular Biology chemistry.chemical_classification Amyloid beta-Peptides biology Chemistry Organic Chemistry Cell Biology Molecular biology Peptide Fragments Protein Structure Tertiary biology.protein lipids (amino acids peptides and proteins) Protein Binding |
| Zdroj: | Chemistry and Physics of Lipids. 137:52-61 |
| ISSN: | 0009-3084 |
| Popis: | Brain plaque deposits of amyloid-beta peptide (Abeta) is a pathological hallmark of Alzheimer's disease (AD) and apolipoprotein E (apoE) is thought to be involved in its deposition. One hypothesis for the role of apoE in the pathogenesis of AD is that apoE may be involved in deposition or clearance of Abeta by direct protein-to-protein interaction. Lipidated apoE4 bound preferentially to an intermediate aggregated form of Abeta and formed two- to three-fold more binding complexes than isoforms apoE2 or apoE3. The interaction was detected by a sandwich ELISA with capture antibodies specific for the N-terminus of apoE, whereas the interaction was not recognized with a C-terminal antibody. The observations indicate that the C-terminus of apoE4 interacts with the intermediate form of Abeta. The differential risk of AD related to apoE genotype may be the result of an enhanced capacity of apoE4 binding to an intermediate aggregated form of Abeta. |
| Databáze: | OpenAIRE |
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