Influence of lipoproteins on microglial degradation of Alzheimer's amyloid beta-protein
β Scribed by Greg M. Cole; March D. Ard
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 180 KB
- Volume
- 50
- Category
- Article
- ISSN
- 1059-910X
No coin nor oath required. For personal study only.
β¦ Synopsis
Amyloid β€-protein (Aβ€), the major component of plaques in Alzheimer's disease, is a small hydrophobic protein that is carried on apolipoprotein E (ApoE)-and ApoJ-containing lipoprotein particles in plasma and cerebrospinal fluid (CSF). Microglia, the scavenger cells of the CNS, take up and degrade Aβ€ via lipoprotein receptors including scavenger receptors A and B, and possibly via other receptors. Lipoproteins, ApoE, and ApoJ influence the uptake and degradation of Aβ€ in vitro and in vivo. Differences in ApoE-E4, -E3, and -E2 isoforms with respect to Aβ€ binding to lipoproteins and delivery to cells, including microglia, may contribute to the increased risk of Alzheimer's disease for people with an APOE4 genotype and to risk reduction with APOE2. Microsc.
π SIMILAR VOLUMES
## Abstract The Ξ²βamyloid protein (AΞ²) is derived by proteolytic processing of the amyloid protein precursor (APP). Cleavage of APP by Ξ²βsecretase generates a Cβterminal fragment (APPβCTFΞ²), which is subsequently cleaved by Ξ³βsecretase to produce AΞ². Our previous studies have shown that the proteas
## Abstract The precise function of APP (Alzheimer's amyloid precursor protein) remains to be fully elucidated, but various lines of evidence suggest that it may be involved in cell adhesion processes. Because APP is a transmembrane glycoprotein, variations in its expression level may have direct b