INT123530
From wiki-pain
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Sentences Mentioned In
Key: | Protein | Mutation | Event | Anatomy | Negation | Speculation | Pain term | Disease term |
We performed Western blot analysis of the total protein lysate from the tissues of mouse PIN lesions to measure the level of expression of androgen receptor, vascular endothelial growth factor, nuclear factor-kappaB p65, BclII, AKT (total and phosphorylated Ser473), p53, cyclin-dependent kinase inhibitor p21WAF1/CIP1, p27, BAX, and caspase-3 to demonstrate the COX-2-independent mechanism involved in the inhibition of PIN lesions of the dorsolateral prostate by both celecoxib and exisulind. | |||||||||||||||
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Oxidant scavengers and Bay 11-7085 [an inhibitor of nuclear factor kappaB (NF-kappaB) activation] prevented the FLX-induced cell death, increase in phosphorylated inhibitory kappaB-alpha and NF-kappaB p65 levels, and binding of NF-kappaB p65 to DNA. | |||||||||||||||
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phosphorylation and on p65 nuclear translocation. | |||||||||||||||
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phosphorylation and p65 nuclear migration | |||||||||||||||
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Here we demonstrate that activation of the mu-opioid receptor in human neuroblastoma SH-SY5Y cells led to the phosphorylations of IkappaB kinase (IKK) and p65, denoting the stimulation of the nuclear factor-kappaB (NFkappaB) transcription factor. | |||||||||||||||
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These data suggest that the mu-opioid receptor is capable of simulating NFkappaB signaling via the phosphorylation of IKK and p65 in human neuroblastoma SH-SY5Y cells. | |||||||||||||||
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B transcriptional activity through a p38 MAPK-dependent RelA phosphorylation pathway in the induction of pro-inflammatory gene expression [40]. | |||||||||||||||
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Exposure of Granta cells to 30 µM parthenolide for 3 hours resulted in a significant decrease in the phosphorylation state of p65 (Fig. 6B, lane 2) which was abrogated by pretreatment with 5 mM GSH for 2 hours (Fig. 6B, lane 4). | |||||||||||||||
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The now active PKAC subunit dissociates and phosphorylates the p65 subunit of NF-? | |||||||||||||||
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Resveratrol, like N-Ac-Leu-Leu-norleucinal (ALLN) suppressed IL-1beta-induced proteasome function and the degradation of IkappaBalpha (an inhibitor of NF-kappaB) without affecting IkappaBalpha kinase activation, IkappaBalpha-phosphorylation or IkappaBalpha-ubiquitination which suppressed nuclear translocation of the p65 subunit of NF-kappaB and its phosphorylation. | |||||||||||||||
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