- 作者: Yi-Hui Hsieh; Chi-Yuan Chou
- 作者服務機構: Department of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taiwan, R.O.C.
- 中文摘要: --
- 英文摘要:
Backgrounds: There are three apolipoprotein E (apoE) isoforms involved in human
lipid homeostasis. In the present study, truncated apoE2-, apoE3- and apoE4-(72-166)
peptides that are tailored to lack domain interactions are expressed and elucidated the
structural and functional consequences.
Methods & Results: Circular dichroism analyses indicated that their secondary
structure is still well organized. Analytical ultracentrifugation analyses demonstrated
that apoE-(72-166) produces more complicated species in PBS. All three isoforms
were significantly dissociated in the presence of dihexanoylphosphatidylcholine.
Dimyristoylphosphatidylcholine turbidity clearance assay showed that apoE4-(72-166)
maintains the highest lipid-binding capacity. Finally, only apoE4-(72-166) still
maintained significant LDL receptor binding ability.
Conclusions: Overall, apoE4-(72-166) peptides displayed a higher lipid-binding and
comparable receptor-binding ability as to full-length apoE. These findings provide the
explanation of diverged functionality of truncated apoE isoforms. - 中文關鍵字: --
- 英文關鍵字: --