Methionine-Oxidized Amyloid Fibrils Are Poor Substrates for Human Methionine Sulfoxide Reductases A and B2

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• 作者：Katrina J. Binger ; Michael D. W. Griffin ; Stefan H. Heinemann ; Geoffrey J. Howlett
• 刊名：Biochemistry
• 出版年：2010
• 出版时间：April 13, 2010
• 年：2010
• 卷：49
• 期：14
• 页码：2981-2983
• 全文大小：661K
• 年卷期：v.49,no.14(April 13, 2010)
• ISSN：1520-4995

文摘

A common feature of many amyloid diseases is the appearance of oxidized, aggregated proteins. Methionine is one of the most readily oxidized amino acids, and its oxidative state is regulated in vivo by the methionine sulfoxide reductases (Msr). Here, we have explored the basis by which methionine oxidation is linked to amyloid disease by comparing the reduction of oxidized amyloid fibrils and monomer. We show that oxidized amyloid fibrils are not as effectively reduced by the Msr enzymes as the monomer. This work suggests a mechanism by which oxidized proteins and aggregates can accumulate as a part of degenerative disease.