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

被引：13

作者：

Binger, Katrina J. ^{[1
]}

Griffin, Michael D. W. ^{[1
]}

Heinemann, Stefan H. ^{[2
]}

Howlett, Geoffrey J. ^{[1
]}

机构：

[1] Univ Melbourne, Dept Biochem & Mol Biol, Parkville, Vic 3052, Australia

[2] Univ Jena, Dept Biophys, Ctr Mol Biomed, Jena, Germany

来源：

BIOCHEMISTRY | 2010年 / 49卷 / 14期

基金：

澳大利亚国家健康与医学研究理事会;

关键词：

ALZHEIMERS-DISEASE; OXIDATION; PROTEIN; PEPTIDE; BRAIN; BETA; FIBRILLATION; OLIGOMERS;

D O I：

10.1021/bi902203m

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：

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.

引用

页码：2981 / 2983

页数：3

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