Methionine-oxidized amyloid fibrils are poor substrates for human methionine sulfoxide reductases A and B2.
Biochemistry
; 49(14): 2981-3, 2010 Apr 13.
Article
em En
| MEDLINE
| ID: mdl-20218727
ABSTRACT
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxirredutases
/
Fatores de Transcrição
/
Metionina Sulfóxido Redutases
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Apolipoproteína C-II
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Amiloide
/
Metionina
Limite:
Humans
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article