IndraLab
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"Activation of the Akt pathway blocks the apoptotic pathway by negatively regulating the activity of BAD, a member of the Bcl2 family that binds to Bcl2 or Bcl-XL and inhibits their anti-apoptotic activity [XREF_BIBR], and the ASK1 and JNK mediated pro apoptotic pathway via phosphorylation of ASK1 at ser83 that inhibits ASK1 activity [XREF_BIBR]."
"Another function of reduced Trx is to bind and inhibit ASK1, whereas oxidized Trx dissociates from ASK1 [43,51,52]. We therefore examined Trx1/ASK1 association as another cellular indicator of the functional redox state of Trx1. In untreated cells in which >95% of Trx1 is reduced (Fig. 4), ASK1 is bound to Trx1 (Fig. 8)."
"Apoptosis signal-regulating kinase 1 (ASK1), a member of the mitogen-activated protein kinase kinase kinase family, plays pivotal roles in reactive oxygen species (ROS)-induced cellular responses. In resting cells, endogenous ASK1 constitutively forms a homo-oligomerized but still inactive high-molecular-mass complex including thioredoxin (Trx), which we designated the ASK1 signalosome. Upon ROS stimulation, the ASK1 signalosome unbinds from Trx and forms a fully activated higher-molecular-mass complex"
"Another function of reduced Trx is to bind and inhibit ASK1, whereas oxidized Trx dissociates from ASK1 [43,51,52]. We therefore examined Trx1/ASK1 association as another cellular indicator of the functional redox state of Trx1. In untreated cells in which >95% of Trx1 is reduced (Fig. 4), ASK1 is bound to Trx1 (Fig. 8)."
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"Since Trx2 bind to Apoptosis signal regulating kinase 1 (Ask1), a major mitogen activated protein kinase kinase kinase (MAPKKK) and inhibits Ask1 phosphorylation and activation, increased binding of Txnip to Trx2 reduces the interaction between Trx2 and Ask1 and induces Ask1 activation for apoptosis."
"we investigated the molecular interaction between human glutaminyl-tRNA synthetase (QRS) and ASK1 and found the Gln-dependent association of the two molecules. While their association was enhanced by the elevation of Gln concentration, they were dissociated by Fas ligation within 5 min. The association involved the catalytic domains of the two enzymes. The ASK1 activity was inhibited by the interaction with QRS as determined by in vitro kinase and transcription assays. Finally, we have shown that QRS inhibited the cell death induced by ASK1, and this antiapoptotic function of QRS was weakened by the deprivation of Gln"