Stereoselective Determination of Amino Acids in β-Amyloid Peptides and Senile Plaques

2001 ◽  
Vol 73 (11) ◽  
pp. 2625-2631 ◽  
Author(s):  
Gunnar Thorsén ◽  
Jonas Bergquist ◽  
Anita Westlind-Danielsson ◽  
Björn Josefsson
1997 ◽  
Vol 751 (2) ◽  
pp. 315-322 ◽  
Author(s):  
Wolfgang Härtig ◽  
Gert Brückner ◽  
Christina Schmidt ◽  
Kurt Brauer ◽  
Geert Bodewitz ◽  
...  

2003 ◽  
Vol 56 (5) ◽  
pp. 349 ◽  
Author(s):  
Tong-Lay Lau ◽  
Kevin J. Barnham ◽  
Cyril C. Curtain ◽  
Colin L. Masters ◽  
Frances Separovic

The deposition of senile plaques is a characteristic event in the progression of Alzheimer's disease (AD). Associated with the progression of the disease, the main component of the deposited material, the β-amyloid peptide (Aβ), undergoes a structural transition and a toxic gain of function. For this reason, extensive structural studies of Aβ and Aβ fragments have been carried out in order to determine the relationship between neurotoxicity and conformational changes of the peptide that lead to fibril formation. NMR studies in aqueous solution and in membrane-mimicking environments are reviewed, and include the effects of temperature, pH, and metal ions on Aβ structure. In addition, electron paramagnetic resonance (EPR) studies of Aβ in model membranes and the effect of metals of Aβ are discussed and demonstrate the pleiomorphic nature of the peptide. The contradictory results obtained from the various experiments are a result of studying different fragments of Aβ and illustrate the importance of studying the full-length peptide.


2001 ◽  
Vol 29 (4) ◽  
pp. 617-623 ◽  
Author(s):  
W. E. Müller ◽  
C. Kirsch ◽  
G. P. Eckert

β-Amyloid (Aβ) protein is the major constituent of senile plaques and cerebrovascular deposits characteristic of Alzheimer's disease (AD). The causal relationship between Aβ and AD-specific lesions like neurodegeneration and atrophy is still not known. The present article summarizes our studies indicating that rather low concentrations of Aβ significantly alter the fluidity of cell membranes and subcellular fractions from different tissues and different species including humans, as a possible initial step of its biological effects. Using different fluorescent probes our data show clearly that Aβ peptides specifically disturb the acylchain layer of cell membranes in a very distinct fashion. By contrast, membrane properties at the level of the polar heads of the phospholipid bilayer at the interface with membrane proteins are much less affected.


2008 ◽  
Vol 116 (8) ◽  
pp. 953-974 ◽  
Author(s):  
L. F. Agnati ◽  
G. Leo ◽  
S. Genedani ◽  
L. Piron ◽  
A. Rivera ◽  
...  

2021 ◽  
Vol 13 ◽  
Author(s):  
Mohammad Samadian ◽  
Mahdi Gholipour ◽  
Mohammadreza Hajiesmaeili ◽  
Mohammad Taheri ◽  
Soudeh Ghafouri-Fard

Alzheimer's disease (AD) is an irrevocable neurodegenerative condition characterized by the presence of senile plaques comprising amassed β-amyloid peptides (Aβ) and neurofibrillary tangles mainly comprising extremely phosphorylated Tau proteins. Recent studies have emphasized the role of microRNAs (miRNAs) in the development of AD. A number of miRNAs, namely, miR-200a-3p, miR-195, miR-338-5p, miR-34a-5p, miR-125b-5p, miR-132, miR-384, miR-339-5p, miR-135b, miR-425-5p, and miR-339-5p, have been shown to participate in the development of AD through interacting with BACE1. Other miRNAs might affect the inflammatory responses in the course of AD. Aberrant expression of several miRNAs in the plasma samples of AD subjects has been shown to have the aptitude for differentiation of AD subjects from healthy subjects. Finally, a number of AD-modifying agents affect miRNA profile in cell cultures or animal models. We have performed a comprehensive search and summarized the obtained data about the function of miRNAs in AD in the current review article.


2020 ◽  
Vol 20 (9) ◽  
pp. 770-781 ◽  
Author(s):  
Poornima Sharma ◽  
Anjali Sharma ◽  
Faizana Fayaz ◽  
Sharad Wakode ◽  
Faheem H. Pottoo

Alzheimer’s disease (AD) is the most prevalent and severe neurodegenerative disease affecting more than 0.024 billion people globally, more common in women as compared to men. Senile plaques and amyloid deposition are among the main causes of AD. Amyloid deposition is considered as a central event which induces the link between the production of β amyloid and vascular changes. Presence of numerous biomarkers such as cerebral amyloid angiopathy, microvascular changes, senile plaques, changes in white matter, granulovascular degeneration specifies the manifestation of AD while an aggregation of tau protein is considered as a primary marker of AD. Likewise, microvascular changes, activation of microglia (immune defense system of CNS), amyloid-beta aggregation, senile plaque and many more biomarkers are nearly found in all Alzheimer’s patients. It was seen that 70% of Alzheimer’s cases occur due to genetic factors. It has been reported in various studies that apolipoprotein E(APOE) mainly APOE4 is one of the major risk factors for the later onset of AD. Several pathological changes also occur in the white matter which include dilation of the perivascular space, loss of axons, reactive astrocytosis, oligodendrocytes and failure to drain interstitial fluid. In this review, we aim to highlight the various biological signatures associated with the AD which may further help in discovering multitargeting drug therapy.


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