scholarly journals Alzheimer Amyloid-β Peptide Forms Denaturant-Resistant Complex with Type ε3 but Not Type ε4 Isoform of Native Apolipoprotein E

1996 ◽  
Vol 2 (2) ◽  
pp. 175-180 ◽  
Author(s):  
Zhongmin Zhou ◽  
Jonathan D. Smith ◽  
Paul Greengard ◽  
Sam Gandy
Keyword(s):  
Apolipoprotein E ◽  
Amyloid Β ◽  
Amyloid Β Peptide

Apolipoprotein E includes a binding site which is recognized by several amyloidogenic polypeptides

2000 ◽  
Vol 349 (1) ◽  
pp. 77-84 ◽  
Author(s):  
Marc H. BAUMANN ◽  
Jukka KALLIJÄRVI ◽  
Hilkka LANKINEN ◽  
Claudio SOTO ◽  
Matti HALTIA
Keyword(s):  
Apolipoprotein E ◽  
Binding Site ◽  
Late Onset ◽  
Specific Binding ◽  
Prion Diseases ◽  
Amyloid Β ◽  
Structural Motif ◽  
Amyloid Β Peptide ◽  
High Avidity ◽  
Amyloidogenic Protein

Inheritance of the apolipoprotein E (apoE) ϵ4 allele is a risk factor for late-onset Alzheimer's disease (AD). Biochemically apoE is present in AD plaques and neurofibrillary tangles of the AD brain. There is a high avidity and specific binding of apoE and the amyloid β-peptide (Aβ). In addition to AD apoE is also present in many other cerebral and systemic amyloidoses, Down's syndrome and prion diseases but the pathophysiological basis for its presence is still unknown. In the present study we have compared the interaction of apoE with Aβ, the gelsolin-derived amyloid fragment AGel183-210 and the amyloidogenic prion fragments PrP109-122 and PrP109-141. We show that, similar to Aβ, also AGel and PrP fragments can form a complex with apoE, and that the interaction between apoE and the amyloidogenic protein fragments is mediated through the same binding site on apoE. We also show that apoE increases the thioflavin-T fluorescence of PrP and AGel and that apoE influences the content of β-sheet conformation of these amyloidogenic fragments. Our results indicate that amyloids and amyloidogenic prion fragments share a similar structural motif, which is recognized by apoE, possibly through a single binding site, and that this motif is also responsible for the amyloidogenicity of these fragments.

Chemical Cross-Linking/Mass Spectrometry Maps the Amyloid β Peptide Binding Region on Both Apolipoprotein E Domains

2015 ◽  
Vol 10 (4) ◽  
pp. 1010-1016 ◽  
Author(s):  
Stéphanie Deroo ◽  
Florian Stengel ◽  
Azadeh Mohammadi ◽  
Nicolas Henry ◽  
Ellen Hubin ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Apolipoprotein E ◽  
Peptide Binding ◽  
Amyloid Β ◽  
Cross Linking ◽  
Amyloid Β Peptide ◽  
Binding Region ◽  
Peptide Binding Region ◽  
Chemical Cross Linking

scholarly journals Role of ABCG1 and ABCA1 in Regulation of Neuronal Cholesterol Efflux to Apolipoprotein E Discs and Suppression of Amyloid-β Peptide Generation

2006 ◽  
Vol 282 (5) ◽  
pp. 2851-2861 ◽  
Author(s):  
Woojin Scott Kim ◽  
Aldwin Suryo Rahmanto ◽  
Alvin Kamili ◽  
Kerry-Anne Rye ◽  
Gilles J. Guillemin ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Cholesterol Efflux ◽  
Amyloid Β ◽  
Amyloid Β Peptide

scholarly journals Apolipoprotein E Interferes with IAPP Aggregation and Protects Pericytes from IAPP-Induced Toxicity

Biomolecules ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 134 ◽  
Author(s):  
Anna L. Gharibyan ◽  
Tohidul Islam ◽  
Nina Pettersson ◽  
Solmaz A. Golchin ◽  
Johanna Lundgren ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Amyloid Formation ◽  
Loss Of Function ◽  
Islet Amyloid ◽  
Amyloid Deposits ◽  
Primary Focus ◽  
The Impact

Apolipoprotein E (ApoE) has become a primary focus of research after the discovery of its strong linkage to Alzheimer’s disease (AD), where the ApoE4 variant is the highest genetic risk factor for this disease. ApoE is commonly found in amyloid deposits of different origins, and its interaction with amyloid-β peptide (Aβ), the hallmark of AD, is well known. However, studies on the interaction of ApoEs with other amyloid-forming proteins are limited. Islet amyloid polypeptide (IAPP) is an amyloid-forming peptide linked to the development of type-2 diabetes and has also been shown to be involved in AD pathology and vascular dementia. Here we studied the impact of ApoE on IAPP aggregation and IAPP-induced toxicity on blood vessel pericytes. Using both in vitro and cell-based assays, we show that ApoE efficiently inhibits the amyloid formation of IAPP at highly substoichiometric ratios and that it interferes with both nucleation and elongation. We also show that ApoE protects the pericytes against IAPP-induced toxicity, however, the ApoE4 variant displays the weakest protective potential. Taken together, our results suggest that ApoE has a generic amyloid-interfering property and can be protective against amyloid-induced cytotoxicity, but there is a loss of function for the ApoE4 variant.

scholarly journals Characterization of stable complexes involving apolipoprotein E and the amyloid β peptide in Alzheimer's disease brain

Neuron ◽  
1995 ◽  
Vol 15 (1) ◽  
pp. 219-228 ◽  
Author(s):  
Jan Näslund ◽  
Johan Thyberg ◽  
Lars O. Tjernberg ◽  
Christer Wernstedt ◽  
Anders R. Karlström ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Apolipoprotein E ◽  
Amyloid Β ◽  
Amyloid Β Peptide

Amyloid β-Peptide Effects on Synaptosomes from Apolipoprotein E-Deficient Mice

2002 ◽  
Vol 74 (4) ◽  
pp. 1579-1586 ◽  
Author(s):  
Jeffrey N. Keller ◽  
Christopher M. Lauderback ◽  
D. Allan Butterfield ◽  
Mark S. Kindy ◽  
Jin Yu ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Deficient Mice

Interaction with Amyloid β Peptide Compromises the Lipid Binding Function of Apolipoprotein E†

Biochemistry ◽  
2008 ◽  
Vol 47 (18) ◽  
pp. 5225-5234 ◽  
Author(s):  
Shiori Tamamizu-Kato ◽  
Jenny K. Cohen ◽  
Carolyn B. Drake ◽  
Malathi G. Kosaraju ◽  
Jessica Drury ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Amyloid Β ◽  
Lipid Binding ◽  
Amyloid Β Peptide ◽  
Binding Function
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