Full metadata record
DC Field | Value | Language |
---|---|---|
dc.creator | Lopez-Sanchez, L.M. (Laura M.) | - |
dc.creator | Corrales, F.J. (Fernando José) | - |
dc.creator | Lopez-Pedrera, C. (Chary) | - |
dc.creator | Aranda, E. (E.) | - |
dc.creator | Rodriguez-Ariza, A. (Antonio) | - |
dc.date.accessioned | 2012-04-02T07:48:58Z | - |
dc.date.available | 2012-04-02T07:48:58Z | - |
dc.date.issued | 2010 | - |
dc.identifier.citation | Lopez-Sanchez LM, Corrales FJ, Lopez-Pedrera C, Aranda E, Rodriguez-Ariza A. Pharmacological impairment of s-nitrosoglutathione or thioredoxin reductases augments protein S-Nitrosation in human hepatocarcinoma cells. Anticancer Res 2010 Feb;30(2):415-421. | es_ES |
dc.identifier.issn | 1791-7530 | - |
dc.identifier.uri | https://hdl.handle.net/10171/21474 | - |
dc.description.abstract | BACKGROUND/AIM: S-Nitrosoglutathione reductase (GSNOR) and thioredoxin enzyme systems participate in cellular defence against nitrosative stress. Pharmacological interventions against these enzyme systems might represent valuable strategies to impair S-nitrosothiol (SNO) homeostasis in tumour cells. MATERIALS AND METHODS: Human HepG2 cells were pre-treated with mithramycin A or auranofin and exposed to S-nitroso-L-cysteine. GSNOR mRNA levels were analyzed by quantitative real-time reverse transcriptase-polymerase chain reaction and S-nitrosated proteins were detected and purified using the biotin-switch approach. Proteins were identified using electrospray ionization tandem mass spectrometry. RESULTS: Mithramycin interfered with GSNOR induction resulting in an increased cellular sensitivity to protein S-nitrosation. Moreover, the thioredoxin reductase inhibitor auranofin also increased cellular susceptibility to S-nitrosoprotein formation. The impairment of these two cellular defense systems against nitrosative stress resulted in different sets of S-nitrosated proteins, as revealed by the proteomics approach. CONCLUSION: Our results suggest that pharmacological intervention with mithramycin or auranofin may constitute promising tools for altering SNO homeostasis in tumour cells. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | International Institute of Anticancer Research | es_ES |
dc.rights | info:eu-repo/semantics/closedAccess | - |
dc.subject | Auranofin/pharmacology | es_ES |
dc.subject | Plicamycin/analogs & derivatives | es_ES |
dc.subject | Proteins/metabolism | es_ES |
dc.subject | S-Nitrosoglutathione/metabolism | es_ES |
dc.subject | Thioredoxin-Disulfide Reductase/antagonists & inhibitors | es_ES |
dc.subject | Thioredoxin-Disulfide Reductase/metabolism | es_ES |
dc.title | Pharmacological impairment of s-nitrosoglutathione or thioredoxin reductases augments protein S-Nitrosation in human hepatocarcinoma cells | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.relation.publisherversion | http://ar.iiarjournals.org/content/30/2/415 | es_ES |
dc.type.driver | info:eu-repo/semantics/article | es_ES |
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