http://www.cnr.it/ontology/cnr/individuo/prodotto/ID170580

Thiol/disulfide interconversion in bovine lens aldose reductase induced by intermediates of glutathione turnover. (Articolo in rivista)

Type

Prodotto della ricerca (Classe)
Articolo in rivista (Classe)

Label

Thiol/disulfide interconversion in bovine lens aldose reductase induced by intermediates of glutathione turnover. (Articolo in rivista) (literal)

Anno

2001-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

10.1021/bi0104975 (literal)

Alternative label

Vilardo PG, Scaloni A, Amodeo P, Barsotti C, Cecconi I, Cappiello M, Lopez Mendez B, Rullo R, Dal Monte M, Del Corso A, Mura U. (2001)
Thiol/disulfide interconversion in bovine lens aldose reductase induced by intermediates of glutathione turnover.
in Biochemistry (Easton); ACS, American chemical society, Washington, DC (Stati Uniti d'America)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Vilardo PG, Scaloni A, Amodeo P, Barsotti C, Cecconi I, Cappiello M, Lopez Mendez B, Rullo R, Dal Monte M, Del Corso A, Mura U. (literal)

Pagina inizio

11985 (literal)

Pagina fine

11994 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

http://pubs.acs.org/doi/abs/10.1021/bi0104975 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

40 (literal)

Rivista

Biochemistry (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

10 (literal)

Note

ISI Web of Science (WOS) (literal)
PubMe (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

Dipartimento di Fisiologia e Biochimica, Università di Pisa, Via S. Maria 55, 56100 Pisa, Italy, IABBAM, Mass Spectrometry Laboratory, Consiglio Nazionale delle Ricerche, 80147 Napoli, Italy, Istituto per la Chimica di Molecole di Interesse Biologico, CNR, 80072 Arco Felice, Napoli, Italy, Departamento de Química Orgánica, Universidad de Santiago de Compostela, E-15706 Santiago de Compostela, Spain (literal)

Titolo

Thiol/disulfide interconversion in bovine lens aldose reductase induced by intermediates of glutathione turnover. (literal)

Abstract

The effectiveness of cysteine and cysteinylglycine to act as protein thiolating agents was investigated using bovine lens aldose reductase (ALR2) as the protein target. Disulfides of both thiol compounds appear to be very effective as ALR2 thiolating agents. Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach. Both Cys-ALR2 and CysGly-ALR2 essentially retain the ability to reduce glyceraldehyde but lose the susceptibility to inhibition by Sorbinil and other ALR2 inhibitors. Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents. The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues. A rationale for the special susceptibility of Cys-ALR2 and CysGly-ALR2, as compared to GS-ALR2, to the thermally induced intramolecular rearrangement is given on the basis of a molecular dynamic and energy minimization approach. A pathway of thiol/disulfide interconversion for bovine lens ALR2 induced, in oxidative conditions, by physiological thiol compounds is proposed. (literal)

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