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Modulation of aldose reductase activity through S-thiolation by physiological thiols.
Cappiello, M; Amodeo, P; Mendez, B L; Scaloni, A; Vilardo, P G; Cecconi, I; Dal Monte, M; Banditelli, S; Talamo, F; Micheli, V; Giblin, F J; Del Corso, A; Mura, U.
Afiliación
  • Cappiello M; Dipartimento di Fisiologia e Biochimica, Università di Pisa, Via S. Maria, 55, 56126, Pisa, Italy.
Chem Biol Interact ; 130-132(1-3): 597-608, 2001 Jan 30.
Article en En | MEDLINE | ID: mdl-11306078
The glutathionyl-modified aldose reductase (GS-ALR2) is unique, among different S-thiolated enzyme forms, in that it displays a lower specific activity than the native enzyme (ALR2). Specific interactions of the bound glutathionyl moiety (GS) with the ALR2 active site, were predicted by a low perturbative molecular modelling approach. The outcoming GS allocation, involving interactions with residues relevant for catalysis and substrate allocation, explains the rationale behind the observed differences in the activity between GS-ALR2 and other thiol-modified enzyme forms. The reversible S-glutathionylation of ALR2 observed in cultured intact bovine lens undergoing an oxidative/non oxidative treatment cycle is discussed in terms of the potential of ALR2/GS-ALR2 inter-conversion as a response to oxidative stress conditions.
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Banco de datos: MEDLINE Asunto principal: Compuestos de Sulfhidrilo / Aldehído Reductasa Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Chem Biol Interact Año: 2001 Tipo del documento: Article País de afiliación: Italia
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Banco de datos: MEDLINE Asunto principal: Compuestos de Sulfhidrilo / Aldehído Reductasa Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Chem Biol Interact Año: 2001 Tipo del documento: Article País de afiliación: Italia