diamide and prolinedithiocarbamate

diamide has been researched along with prolinedithiocarbamate* in 2 studies

Other Studies

2 other study(ies) available for diamide and prolinedithiocarbamate

Article	Year
Inhibition of NF kappa B activity by oxidative processes in intact cells mechanism of action of pyrolidine dithiocarbamate and diamide. Biochemical Society transactions, 1996, Volume: 24, Issue:1 Topics: Amino Acid Sequence; Animals; Antioxidants; Binding Sites; Cell Line; Conserved Sequence; Diamide; Glutathione; Humans; Molecular Sequence Data; NF-kappa B; Oxidation-Reduction; Proline; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-rel; Sequence Homology, Amino Acid; Thiocarbamates; Tumor Cells, Cultured; Tumor Necrosis Factor-alpha	1996
2-mercaptoethanol restores the ability of nuclear factor kappa B (NF kappa B) to bind DNA in nuclear extracts from interleukin 1-treated cells incubated with pyrollidine dithiocarbamate (PDTC). Evidence for oxidation of glutathione in the mechanism of inh The Biochemical journal, 1996, Dec-15, Volume: 320 ( Pt 3) The metal chelator and anti-oxidant pyrollidine dithiocarbamate (PDTC) has been used extensively in studies implicating reactive oxygen intermediates in the activation of nuclear factor kappa B (NF kappa B). In agreement with other studies, we have shown that PDTC inhibits NF kappa B activation in response to the pro-inflammatory cytokines interleukin 1 (IL1) and tumour necrosis factor (TNF). However, we have found that the inhibition was reversed by treatment of inhibited nuclear extracts with the reducing agent 2-mercaptoethanol. This was observed in extracts prepared from IL1-treated EL4.NOB-1 thymoma cells and TNF-treated Jurkat E6.1 lymphoma cells. These results suggested that the inhibition was caused by oxidation of NF kappa B on a sensitive thiol, possibly on the p50 subunit (which was detected in NF kappa B complexes in both cell types), and not by inhibition of the activation pathway. The possibility that PDTC was acting as a pro-oxidant was therefore investigated. PDTC caused an increase in oxidized glutathione, suggesting that it acts as an oxidizing agent in the cells tested rather than as an anti-oxidant. Similar results were obtained with diamide, a compound designed to oxidize glutathione. Finally, an increase in the ratio of oxidized to reduced glutathione was shown to inhibit NF kappa B-DNA binding in vitro. On the basis of these results we suggest that, while NF kappa B activation is unaffected by PDTC, DNA binding is inhibited through a mechanism involving a shift towards oxidizing conditions, and that this is the mechanism of action of both PDTC and diamide in the cells tested here. Topics: Animals; Antioxidants; Diamide; DNA-Binding Proteins; Electrophoresis, Polyacrylamide Gel; Glutathione; Humans; Interleukin-1; Mercaptoethanol; Mice; NF-kappa B; Nuclear Proteins; Oxidation-Reduction; Proline; Protein Binding; Thiocarbamates; Thymoma; Tumor Cells, Cultured	1996

Article

Year

Inhibition of NF kappa B activity by oxidative processes in intact cells mechanism of action of pyrolidine dithiocarbamate and diamide.

Biochemical Society transactions, 1996, Volume: 24, Issue:1

Topics: Amino Acid Sequence; Animals; Antioxidants; Binding Sites; Cell Line; Conserved Sequence; Diamide; Glutathione; Humans; Molecular Sequence Data; NF-kappa B; Oxidation-Reduction; Proline; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-rel; Sequence Homology, Amino Acid; Thiocarbamates; Tumor Cells, Cultured; Tumor Necrosis Factor-alpha

1996

2-mercaptoethanol restores the ability of nuclear factor kappa B (NF kappa B) to bind DNA in nuclear extracts from interleukin 1-treated cells incubated with pyrollidine dithiocarbamate (PDTC). Evidence for oxidation of glutathione in the mechanism of inh

The Biochemical journal, 1996, Dec-15, Volume: 320 ( Pt 3)

The metal chelator and anti-oxidant pyrollidine dithiocarbamate (PDTC) has been used extensively in studies implicating reactive oxygen intermediates in the activation of nuclear factor kappa B (NF kappa B). In agreement with other studies, we have shown that PDTC inhibits NF kappa B activation in response to the pro-inflammatory cytokines interleukin 1 (IL1) and tumour necrosis factor (TNF). However, we have found that the inhibition was reversed by treatment of inhibited nuclear extracts with the reducing agent 2-mercaptoethanol. This was observed in extracts prepared from IL1-treated EL4.NOB-1 thymoma cells and TNF-treated Jurkat E6.1 lymphoma cells. These results suggested that the inhibition was caused by oxidation of NF kappa B on a sensitive thiol, possibly on the p50 subunit (which was detected in NF kappa B complexes in both cell types), and not by inhibition of the activation pathway. The possibility that PDTC was acting as a pro-oxidant was therefore investigated. PDTC caused an increase in oxidized glutathione, suggesting that it acts as an oxidizing agent in the cells tested rather than as an anti-oxidant. Similar results were obtained with diamide, a compound designed to oxidize glutathione. Finally, an increase in the ratio of oxidized to reduced glutathione was shown to inhibit NF kappa B-DNA binding in vitro. On the basis of these results we suggest that, while NF kappa B activation is unaffected by PDTC, DNA binding is inhibited through a mechanism involving a shift towards oxidizing conditions, and that this is the mechanism of action of both PDTC and diamide in the cells tested here.

Topics: Animals; Antioxidants; Diamide; DNA-Binding Proteins; Electrophoresis, Polyacrylamide Gel; Glutathione; Humans; Interleukin-1; Mercaptoethanol; Mice; NF-kappa B; Nuclear Proteins; Oxidation-Reduction; Proline; Protein Binding; Thiocarbamates; Thymoma; Tumor Cells, Cultured

1996