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Cu ~ (2) effects of β - amyloid protein neurotoxicity and aggregation state in vitro studies

Author: DaiXueLing
Tutor: JiangZhaoFeng
School: Capital Normal University
Course: Biochemistry and Molecular Biology
Keywords: Alzheimer 's disease (AD) β- amyloid (Aβ) Oxidative Stress Cytotoxicity Aβ deposition Secondary structure
CLC: R749.16
Type: Master's thesis
Year: 2007
Downloads: 153
Quote: 0
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Abstract


Alzheimer's disease (Alzheimer's disease, AD) is a neurodegenerative disorder, a serious hazard to human health is one of the most common form of senile dementia. The prevalence of AD risk rose sharply with age, has yet to find an effective treatment method. Considerable evidence that beta-amyloid protein (β-amyloid peptide, Aβ) in the brain of AD patients produce aggregation and deposition and formation of senile plaques (Senile The tumor drug can be used for the heart disease in the SP), played a key in the occurrence and development process of AD role. Aβ enzymatic degradation products of β-amyloid precursor protein (Amyloid precursor protein, APP), usually consists of 39-42 amino acids, to Aβ 1-40 and Aβ 1-42 is the most common. Senile plaques in abnormally high concentration of CH 2 , prompted Cu 2 may be involved in the pathogenesis of AD. Cu 2 and AB may lead to two abnormal consequences: redox reaction H 2 O 2 caused the number of apoptotic neurons and promote the formation of Aβ deposition. The study shows that an important role of oxidative stress in the pathogenesis of AD, a large area within the AD brain tissue lipid peroxidation injury, brain accumulation of large DNA and protein oxidation products. In cell culture will antioxidants VC, the VE with Aβ or Aβ / Cu 2 complex joint action on neurons, the results show that the VC, VE can significantly reduce the Aβ cytotoxicity, but not completely clear, prompt Aβ-induced injury may exist other mechanisms of oxidative stress. Cu 2 and Aβ related evidence, but the the precise covalent binding geometry and participation Cu 2 combination of amino acid sites are still in dispute. Results of this experiment suggest that His6 - His13, His14 locus Aβ on Cu 2 binding sites for the phenolic hydroxyl group of Tyr10 whether Aβ and Cu 2 combination provides the O atom is still I do not know. Cytological experiments prompted Met35 the the Aβ neurotoxicity key sites, but Aβ with Cu 2 combination of process does not involve Met35. This article by circular dichroism spectroscopy, fluorescence spectroscopy, and optical density experimental analysis of the structure and state of aggregation of Aβ added Cu 2 , results suggest that regardless of whether to join Cu 2 the structure of the wild-type Aβ were lower, the content of β-deposition of soluble Aβ oligomers may be further polymerized to form the amorphous deposition. Summary Aβ fibrous deposition of Aβ-induced oxidative damage and neurotoxicity negatively correlated soluble Aβ oligomers may be the source of the cause of a large number of neuronal apoptosis in AD brain tissue.

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