INT110178
From wiki-pain
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Sentences Mentioned In
Key: | Protein | Mutation | Event | Anatomy | Negation | Speculation | Pain term | Disease term |
Next, we investigated the effect of MKK3 or MKK6 knock down on the phosphorylation of p38-MAPK in response to stimulation with IL-1? | |||||||||||||||
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-induced phosphorylation of p38-MAPK was inhibited in chondrocytes pre-treated with PE (Figure 4a). | |||||||||||||||
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(10 ng/ml) for different time periods (5 to 120 minutes) phosphorylated the p38-MAPK protein (Figure 2a). | |||||||||||||||
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Human phosphorylated p38 MAP Kinase protein was detected with anti-phospho-p38 MAP Kinase antibody (Thr180/Tyr182) (Cell Signaling, Ozyme, Saint Quentin Yvelines, France) antibody at a 1/1000 dilution. | |||||||||||||||
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MKK3 selectively phosphorylates p38? | |||||||||||||||
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enhances the phosphorylation of the p38? | |||||||||||||||
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alone had higher level of p38-MAPK phosphorylation compared with unstimulated OA chondrocytes. | |||||||||||||||
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The phosphorylation of p38 MAPK and c-Jun NH2-terminal kinase (JNK) were detected after capsaicin stimulation. p38 MAPK is involved in capsaicin-induced IL-6 production, as shown by the use of specific inhibitors of this kinase. | |||||||||||||||
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Suppression of AP-1 was associated with altered phosphorylation of p38 mitogen-activated protein kinases. | |||||||||||||||
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M) greatly decreases the LPS induced phosphorylation of the p38 protein, resulting in a level that is near identical to the control. | |||||||||||||||
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Figure 2 confirms that the action of LPS on mature adipocytes results in p38 protein phosphorylation with a peak obtained 5 minutes after stimulation. | |||||||||||||||
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The quantity of phosphorylated p38 protein subsequently decreases and is no longer detectible 20 minutes after treatment with LPS. | |||||||||||||||
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AEA triggered phosphorylation of c-Jun NH(2)-terminal kinase (JNK) and p38 mitogen activated protein kinase. | |||||||||||||||
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ET-1 at 10 nM induced p38, Akt, p44/42, and SAP/JNK phosphorylation in a time-ordered manner. | |||||||||||||||
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As shown by western blot analysis of the cell extracts, incubation of cells for a short period of time with ET-1 results in the phosphorylation of p38 MAP, p44/42, SAP/JNK and Akt kinases. | |||||||||||||||
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Figure 3ad show the effects of ET-1 on the phosphorylation of p38, Akt, p44/42 and SAP/JNK kinases as detected by western blot of cell extracts. | |||||||||||||||
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Both aspirin-mediated permeability and phosphorylation of p38 MAPK were significantly attenuated by SB-203580 (a p38 MAPK inhibitor) but not by U-0126 (a MEK1 inhibitor) or SP-600125 (a JNK inhibitor). | |||||||||||||||
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Thrombin induced phosphorylation of ERK1/2 and p38 in MDMs. | |||||||||||||||
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The membranes were immersed overnight in the Super Block Blocking buffer (Pierce, Rockford, IL, USA), rinsed and incubated for 24 hours at 4°C with one of the mouse monoclonal primary antibodies (New England Biolabs, Mississauga, ON, Canada) specifically recognizing phosphorylated p38 or total p38 (dilution, 1/1000), phosphorylated p44/42 (dilution, 1/5000), phosphorylated Akt (dilution, 1/2000), phosphorylated stress-activated protein kinase/Jun-N-terminal kinase (SAP/JNK) (dilution, 1/1000), or actin C-terminal fragment (dilution, 1/5000). iNOS was detected with a rabbit polyclonal antibody (dilution, 1/1000; Santa Cruz Biotechnology Inc., Santa Cruz, CA, USA). | |||||||||||||||
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Additionally, inducible nitric oxide synthase (iNOS) and phosphorylated forms of p38 mitogen-activated protein kinase, p44/42, stress-activated protein kinase/Jun-N-terminal kinase and serine-threonine Akt kinase were determined by western blot. | |||||||||||||||
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General Comments
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