Presence of soluble amyloid β–peptide precedes amyloid plaque formation in Down's syndrome

1996 ◽  
Vol 2 (1) ◽  
pp. 93-95 ◽  
Author(s):  
Jan K. Teller ◽  
Claudio Russo ◽  
Laura M. Debusk ◽  
Giovanna Angelini ◽  
Damiano Zaccheo ◽  
...  
Keyword(s):  
Down's Syndrome ◽  
Amyloid Β ◽  
Down’S Syndrome ◽  
Amyloid Plaque ◽  
Plaque Formation ◽  
Amyloid Β Peptide

scholarly journals Heterogeneity of water-soluble amyloid β-peptide in Alzheimer's disease and Down's syndrome brains

FEBS Letters ◽  
1997 ◽  
Vol 409 (3) ◽  
pp. 411-416 ◽  
Author(s):  
Claudio Russo ◽  
Takaomi C. Saido ◽  
Laura M. DeBusk ◽  
Massimo Tabaton ◽  
Pierluigi Gambetti ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Down's Syndrome ◽  
Amyloid Β ◽  
Down’S Syndrome ◽  
Water Soluble ◽  
Amyloid Β Peptide

The p3 Peptide, a Naturally Occurring Fragment of the Amyloid-β Peptide (Aβ)Found in Alzheimer's Disease, Has a Greater Aggregation Propensity In Vitro Than Full-Length Aβ, But Does Not Bind Cu2+.

2000 ◽  
Vol 53 (4) ◽  
pp. 321 ◽  
Author(s):  
Feda Ali ◽  
Andrew J. Thompson ◽  
Colin J. Barrow
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Down's Syndrome ◽  
Amyloid Β ◽  
Down’S Syndrome ◽  
Full Length ◽  
Amyloid Β Peptide ◽  
Sheet Structure ◽  
Β Sheet

Cerebellar preamyloid from both Down’s syndrome and Alzheimer’s disease contains the p3 fragment (Aβ 17–40/42) as a major amyloid-β peptide (Aβ) component. The p3 peptide was previously shown to form amyloid in vitro, but less readily than full-length Aβ. Here we show that the p3 peptide has a greater β-sheet-forming propensity than full-length Aβ. Using circular dichroism spectroscopy we determined that in aqueous solutions the p3 peptide forms β-sheet structure more readily than full-length Aβ. The p3 peptide also has a lower α-helical propensity than full-length Aβ in the structure-forming solvent trifluoroethanol. These results indicate that the lower amyloidogenicity of the p3 peptide is not related to an inability to form β-sheet structure. In this study we also show that, unlike full-length Aβ, the p3 peptide does not bind Cu2+ ions. This inability to bind copper ions may explain why the p3 peptide appears to play a lesser role in Down’s syndrome and Alzheimer’s disease related neurodegeneration than does full-length Aβ.

scholarly journals Interactions between Amyloid-β and Hemoglobin: Implications for Amyloid Plaque Formation in Alzheimer's Disease

PLoS ONE ◽  
2012 ◽  
Vol 7 (3) ◽  
pp. e33120 ◽  
Author(s):  
Jia-Ying Chuang ◽  
Chu-Wan Lee ◽  
Yao-Hsiang Shih ◽  
Tingting Yang ◽  
Lung Yu ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Β ◽  
Amyloid Plaque ◽  
Plaque Formation

scholarly journals The molecular biology of Alzheimer's disease

1991 ◽  
Vol 15 (9) ◽  
pp. 564-565
Author(s):  
L. J. Whalley
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amino Acids ◽  
Gene Dosage ◽  
Down's Syndrome ◽  
Amyloid Β ◽  
Down’S Syndrome ◽  
Mental Illnesses ◽  
Amyloid Β Protein ◽  
Β Protein

For some years, the pace of progress in clinical neuroscience has progressively quickened but none more so than with molecular biological techniques. Clinical psychiatrists have been promised (some say forewarned) that the systematic application of these techniques will swiftly cut through the multifactorial aetiologies of many mental illnesses and revolutionise diagnosis, treatment and, possibly prevention. Not surprisingly, given the fact that Down's syndrome and Alzheimer's neuropathological changes (senile plaques and neurofibrillary tangles) are so tightly linked, understanding of Alzheimer's disease (AD) was the first mental illness to benefit from these new methods. Once the amyloid β protein component of the senile plaque had been isolated and its 39–43 constituent amino acids sequenced, then it became almost a routine matter to locate the gene and describe comprehensively the much larger (approximately 710 amino acids) amyloid β protein precursor (APP). Almost simultaneously, the gene responsible for familial pre-senile Alzheimer's disease (FAD) was located, like the APP gene, on chromosome 21 (Tanzi et al, 1989). Soon, a claim was made that these (FAD and APP) were the same gene, and, in a manner akin to the presumed causal gene dosage effects in Down's syndrome, Alzheimer's disease was attributed to excess production of amyloid (by way of APP). However, this was quickly refuted and data to support a gene dosage effect in AD were not confirmed. The trail then seemed to go cold. Several studies indicated that FAD was genetically heterogeneous and distinct from senile AD (St George-Hyslop et al, 1990), and the problems of prion disease in animals and man secured more attention (Westaway et al, 1989).

Endogenous Murine Amyloid-β Peptide Assembles into Aggregates in the Aged C57BL/6J Mouse Suggesting These Animals as a Model to Study Pathogenesis of Amyloid-β Plaque Formation

2018 ◽  
Vol 61 (4) ◽  
pp. 1425-1450 ◽  
Author(s):  
Barbara Ahlemeyer ◽  
Sascha Halupczok ◽  
Elke Rodenberg-Frank ◽  
Klaus-Peter Valerius ◽  
Eveline Baumgart-Vogt
Keyword(s):  
Amyloid Β ◽  
Plaque Formation ◽  
Amyloid Β Peptide

scholarly journals The Neuronal Adaptor Protein X11β Reduces Amyloid β-Protein Levels and Amyloid Plaque Formation in the Brains of Transgenic Mice

2004 ◽  
Vol 279 (47) ◽  
pp. 49099-49104 ◽  
Author(s):  
Ju-Hyun Lee ◽  
Kwok-Fai Lau ◽  
Michael S. Perkinton ◽  
Claire L. Standen ◽  
Boris Rogelj ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Amyloid Β ◽  
Adaptor Protein ◽  
Amyloid Plaque ◽  
Plaque Formation ◽  
Amyloid Β Protein ◽  
Protein Levels ◽  
Β Protein
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