Amyloid ? protein is internalized selectively by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein

1998 ◽  
Vol 397 (1) ◽  
pp. 139-147 ◽  
Author(s):  
Ben A. Bahr ◽  
Keith B. Hoffman ◽  
Austin J. Yang ◽  
Ursula S. Hess ◽  
Charles G. Glabe ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Amyloid Protein ◽  
Hippocampal Field ◽  
Field Ca1

scholarly journals β- and γ-Secretases and Lipid Rafts

2010 ◽  
Vol 3 (1) ◽  
pp. 16-20 ◽  
Author(s):  
Wataru Araki
Keyword(s):  
Alzheimer’S Disease ◽  
Amyloid Precursor Protein ◽  
Lipid Rafts ◽  
Molecular Pathology ◽  
Precursor Protein ◽  
Membrane Microdomains ◽  
Amyloid Protein ◽  
Amyloidogenic Processing ◽  
Β Amyloid ◽  
Shed Light

The cerebral accumulation of β-amyloid protein (Aβ) is thought to play a key role in the molecular pathology of Alzheimer’s disease (AD). Recent evidence indicates that both β-secretase and γ-secretase, the membrane-associated proteases directly involved in the generation of Aβ from its precursor, amyloid precursor protein (APP), are localized to cholesterol-rich membrane microdomains termed lipid rafts. This underscores the significance of lipid rafts in the amyloidogenic processing of APP. In the present mini-review, I summarize recent research developments that shed light on the association of β-secretase and γ-secretase with lipid rafts, and discuss their implications for the pathology and therapeutics of AD.

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