共 80 条
Interactions between metals and α-synuclein -: function or artefact?
被引:44
作者:

Brown, David R.
论文数: 0 引用数: 0
h-index: 0
机构:
Univ Bath, Dept Biol & Biochem, Bath BA2 7AY, Avon, England Univ Bath, Dept Biol & Biochem, Bath BA2 7AY, Avon, England
机构:
[1] Univ Bath, Dept Biol & Biochem, Bath BA2 7AY, Avon, England
关键词:
amyloid;
copper;
Lewy body;
Parkinson's disease;
D O I:
10.1111/j.1742-4658.2007.05917.x
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
alpha-synuclein is one of a family of proteins whose function remains unknown. This protein has become linked to a number of neurodegenerative disease although its potential causative role in these diseases remains mysterious. In diseases such as Parkinson's disease and Lewy body dementias, alpha-synuclein becomes deposited in aggregates termed Lewy bodies. Also, some inherited forms of Parkinson's diseases are linked to mutations in the gene for alpha-synuclein. Studies have mostly focussed on what causes the aggregation of the protein but, like many amyloidogenic proteins associated with a neurodegenerative disorder, this protein has now been suggested to bind copper. This finding is currently controversial. This review examines the evidence that alpha-synuclein is a copper binding protein and discusses whether this has any significance in determining the function of the protein or whether copper binding is at all necessary for aggregation.
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页码:3766 / 3774
页数:9
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