2002
DOI: 10.1074/jbc.m206826200
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Role of Glutaredoxin in Metabolic Oxidative Stress

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Cited by 235 publications
(76 citation statements)
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References 48 publications
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“…This complex in turn triggers the caspase cascade, the activation of specific kinases such as the I B kinase (IKK) complex and mitogen-activated protein kinases (MAPKs), and the transcription of various genes mediated by nuclear factor-B (NF-B) and activator protein-1 (AP-1) (6 -10). Many TNF-␣ signaling pathways are activated by ROS (7,(11)(12)(13)(14)(15)(16) and attenuated by Trx overexpression (17)(18)(19)(20)(21)(22)(23)(24)(25).…”
mentioning
confidence: 99%
“…This complex in turn triggers the caspase cascade, the activation of specific kinases such as the I B kinase (IKK) complex and mitogen-activated protein kinases (MAPKs), and the transcription of various genes mediated by nuclear factor-B (NF-B) and activator protein-1 (AP-1) (6 -10). Many TNF-␣ signaling pathways are activated by ROS (7,(11)(12)(13)(14)(15)(16) and attenuated by Trx overexpression (17)(18)(19)(20)(21)(22)(23)(24)(25).…”
mentioning
confidence: 99%
“…ASK1 activity appears to be enhanced by its binding to a number of important regulatory proteins, such as TRAFs Liu et al, 2000), Daxx (Chang et al, 1998), and JSAP1/JIP3 (Matsuura et al, 2002). On the other hand, ASK1 activity is suppressed in cells via its interaction with several prosurvival regulatory proteins, including thioredoxin (Gotoh and Cooper, 1998;Saitoh et al, 1998), glutaradoxin (Song et al, 2002), HSP72 (Park et al, 2002), Raf-1 (Chen et al, 2001), and 14-3-3 (Zhang et al, 1999). Interestingly, the binding of 14-3-3 proteins to ASK1 is phosphorylation-dependent.…”
mentioning
confidence: 99%
“…It is possible that hD53L1 may act as a competitive inhibitor of 14-3-3 or Grx proteins that bind to the C-terminal portion of ASK1 and suppress its activation (16,17,44), resulting in prevention of 14-3-3 proteins or Grx from binding to ASK1 in a concentrationdependent manner. This possible role of hD53L1 as an inhibitor of ASK1-inhibiting proteins may explain why the kinase activity of ASK1 is not induced significantly.…”
Section: Discussionmentioning
confidence: 99%
“…This stronger effect by H 2 O 2 may be mainly due to multiple roles of H 2 O 2 for regulation of ASK1. There are two identified pathways for activation of ASK1 by H 2 O 2 : glutathione-dependent Grx-ASK1 and glutathione-independent Trx-ASK1 pathways (14,16,44). Those two H 2 O 2 -sensing proteins, Trx and Grx, bind and inhibit ASK1 under reduced conditions.…”
Section: Discussionmentioning
confidence: 99%
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