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Your search keyword '"Vilardo, Pier Giuseppe"' showing total 17 results
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17 results on '"Vilardo, Pier Giuseppe"'

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

Author

Vilardo, Pier Giuseppe, Scaloni, Andrea, Amodeo, Pietro, Barsotti, Catia, Cecconi, Ilaria, Cappiello, Mario, Mendez, Blanca Lopez, Rullo, Rosario, Dal Monte, Massimo, Del Corso, Antonella, and Mura, Umberto

Subjects
Biochemistry -- Research, Thiols -- Physiological aspects, Sulfides -- Physiological aspects, Aldose reductase -- Physiological aspects, Glutathione -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on the ability of cysteine and cysteinyglycine to act as the protein thiolating agents. This ability has been investigated via the bovine lense aldose reductase used as a protein target and the results indicate that the disulfides of the thiol compounds are effective as the lense aldose reductase thiolating agents.

Published
2001

9. Insulin Control of Glycogen Metabolism in Knockout Mice Lacking the Muscle-Specific Protein Phosphatase PP1G/RGL

Author

Suzuki, Yoichi, primary, Lanner, Carita, additional, Kim, Jong-Hwa, additional, Vilardo, Pier Giuseppe, additional, Zhang, Hong, additional, Yang, Jie, additional, Cooper, Lori D., additional, Steele, Marcella, additional, Kennedy, Andrew, additional, Bock, Cheryl B., additional, Scrimgeour, Angus, additional, Lawrence, John C., additional, and DePaoli-Roach, Anna A., additional

Published
2001
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10. Oxidative Modification of Aldose Reductase Induced by Copper Ion. Factors and Conditions Affecting the Process

Author

Cecconi, Ilaria, primary, Moroni, Maria, additional, Vilardo, Pier Giuseppe, additional, Dal Monte, Massimo, additional, Borella, Paola, additional, Rastelli, Giulio, additional, Costantino, Luca, additional, Garland, Donita, additional, Carper, Deborah, additional, Petrash, J. Mark, additional, Del Corso, Antonella, additional, and Mura, Umberto, additional

Published
1998
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16. Determination of mammalian glycogen synthase phosphatase activity.

Author

DePaoli-Roach AA, Vilardo PG, Kim JH, Mavila N, Vemuri B, and Roach PJ

Subjects
Animals, Chromatography, DEAE-Cellulose methods, Glycogen-Synthase-D Phosphatase analysis, Glycogen-Synthase-D Phosphatase isolation & purification, Indicators and Reagents, Kinetics, Mammals, Rabbits, Glycogen-Synthase-D Phosphatase metabolism
Published
2003
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17. Physiological thiols as promoters of glutathione oxidation and modifying agents in protein S-thiolation.

Author

Del Corso A, Vilardo PG, Cappiello M, Cecconi I, Dal Monte M, Barsacchi D, and Mura U

Subjects
Cysteine chemistry, Cysteine metabolism, Dipeptides chemistry, Dipeptides metabolism, Glutathione chemistry, Models, Chemical, Oxidation-Reduction, Oxygen chemistry, Oxygen metabolism, Protein Processing, Post-Translational, Sulfhydryl Compounds chemistry, Aldehyde Reductase metabolism, Glutathione metabolism, Sulfhydryl Compounds metabolism
Abstract

Glutathione is one of the most relevant antioxidants present in cells. It exerts its scavenging action through the involvement of efficient and ubiquitous enzymes. GSH on the other hand, because of its chemical features, can scavenge reactive oxygen species without the involvement of enzymatic systems. The study deals with the mobilization of GSH pool in a nonenzymatic antioxidant system by other physiological thiols (i.e., cysteine and cysteinyl-glycine), which are far more sensitive than GSH to oxidative conditions. These thiol compounds, in the presence of iron/EDTA, can promote oxygen activation through their oxidation to disulfides. GSH, through trans-thiolation reactions, can regenerate Cys and CysGly, which can then recycle, thus inducing a massive GSH oxidation. In these conditions, making use of bovine lens aldose reductase as a protein model, evidence is given that Cys and CysGly promote specific protein S-thiolation reactions. The possibility that GSH may be recruited in controlling cellular oxygen tension is considered., ((c)2002 Elsevier Science.)

Published
2002
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