INT158416
From wiki-pain
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Sentences Mentioned In
Key: | Protein | Mutation | Event | Anatomy | Negation | Speculation | Pain term | Disease term |
In addition to different types of noxious stimuli, high intensity electrical stimulation of C-fibers also activates ERK in the spinal cord dorsal horn, suggesting that C-fiber recruitment is crucial for release of transmitters that activate ERK centrally in the spinal cord [6,10]. | |||||||||||||||
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evidence was published on the combined use of ERK cascade inhibition and PPAR? | |||||||||||||||
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The activation of ERK pathway and subsequent translocation of NF-kappaB was possibly necessary for the up-regulation TRPC6 induced by Ang II. | |||||||||||||||
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Considering the importance of ERK in regulating gene expression, the ERK activation may be required for L-LTP. | |||||||||||||||
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The signalling pathways were pharmacologically investigated with the pre-administration of adenylyl cyclase (AC), cAMP-dependent protein kinase (PKA), protein kinase Cepsilon (PKCepsilon), and the extracellular signal-related kinase (ERK) inhibitors. | |||||||||||||||
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The signalling pathways were pharmacologically investigated with the pre-administration of adenylyl cyclase (AC), cAMP-dependent protein kinase (PKA), protein kinase Cepsilon (PKCepsilon), and the extracellular signal-related kinase (ERK) inhibitors. | |||||||||||||||
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In normal noncancerous tissue from radical prostatectomy specimens, immunohistochemistry localizes ERK to the cytoplasm of most cells of the prostate including the epithelial, basal, and stromal cells [1,2]. | |||||||||||||||
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Our observation that active ERK was localized to angiogenic buds and neovascular outgrowths indicates that altered MKK signaling also may be a factor in retinal neovascularization. | |||||||||||||||
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The signal by which nerve injury or disease may lead to microglial activation is unclear, but may relate to acute release of ERK, an enzyme that plays a critical role in intracellular signal transduction and neuronal plasticity. | |||||||||||||||
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Immunoblot analyses for angiotensin II, AT1R, synaptophysin, and phosphorylated forms of ERK, Akt, and STAT3. | |||||||||||||||
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ZnR activation induced intracellular release of Ca(2+), as well as phosphorylation of extracellular-regulated kinase and Ca(2+)/calmodulin kinase II. | |||||||||||||||
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and c-Jun (a phosphorylation target of ERK and JNK). | |||||||||||||||
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Normalization of p-ERK and t-ERK were also conducted against beta-actin, then p-ERK data were quantified as relative intensity of band divided by intensity of t-ERK. | |||||||||||||||
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Normalization of p-ERK and t-ERK were also conducted against beta-actin, then p-ERK data were quantified as relative intensity of band divided by intensity of t-ERK. | |||||||||||||||
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We have now demonstrated that expression of c-Myc requires phosphorylation and nuclear translocation of ERK, which results in phosphorylation of c-Fos and formation of a specific activator protein (AP)-1 complex. | |||||||||||||||
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-induced elevation in COX-2 Luciferase (Fig. 5C) and mRNA expression (Fig. 5D) was significantly inhibited by co-treatment of cells with the FP receptor antagonist (AL8810), and chemical inhibitors of PLC (U73122), PKA (4C3MQ), EGFR kinase (AG1478) and ERK1/2 kinase (PD98059), but not the EP2 receptor antagonist (AH6809), EP4 receptor antagonist (ONOAE2227) or PKC inhibitor (GF109203x; Fig. 5C and D, P < 0.05).
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The PGE2-induced elevation in COX-2 Luciferase (Fig. 5A) and mRNA expression (Fig. 5B) was significantly reduced by treatment of FPS cells with the FP receptor antagonist (AL8810), EP2 receptor antagonist (AH6809), EP4 receptor antagonist (ONOAE2227), and chemical inhibitors of PLC (U73122), PKA (4C3MQ), EGFR kinase (AG1478) and ERK1/2 kinase (PD98059), but not the PKC inhibitor (GF109203x; P < 0.05). | |||||||||||||||
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Activated MEK subsequently phosphorylates ERK, which translocates to the nucleus where it activates multiple transcription factors. | |||||||||||||||
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Additional antibodies included rabbit Erk 1/2 (Cell Signaling Technologies) and anti-phospho ERK1/2 purchased from Promega Corporation (Madison, WI). | |||||||||||||||
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