Site-specific inactivation of aldose reductase by 4-hydroxynonenal.
Arch Biochem Biophys
; 350(2): 245-8, 1998 Feb 15.
Article
em En
| MEDLINE
| ID: mdl-9473298
ABSTRACT
Bovine lens aldose reductase (ALR2), which catalyzes the NADPH-dependent reduction of 4-hydroxy-2-nonenal (HNE), is readily inactivated by its own substrate in a time- and concentration-dependent manner. Both DTT and NADP+ can prevent enzyme inactivation but neither extensive dialysis nor thiol-reducing treatment were able to restore enzyme activity once inactivation had occurred. Unlike the native enzyme, S-glutathionyl-modified ALR2 is unaffected by HNE, and can be easily reverted to the native form under thiol-reducing conditions. Evidence is presented of the involvement of Cys298 in the inactivation process. Zofenoprilat, an antioxidant thiol compound, mimics the effect of GSH. The possibility is raised that enzyme thiolation may function as a protection mechanism against the irreversible modification of ALR2.
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Coleções:
01-internacional
Temas:
Geral
Base de dados:
MEDLINE
Assunto principal:
Aldeído Redutase
/
Aldeídos
Limite:
Animals
Idioma:
En
Revista:
Arch Biochem Biophys
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Itália