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| 1. |
Terstegen, L., Gatsios, P., Bode, J.G., Schaper, F., Heinrich, P.C., and Graeve, L.
(2000)
The inhibition of interleukin-6-dependent STAT activation by mitogen-activated protein kinases depends on tyrosine 759 in the cytoplasmic tail of glycoprotein 130.
J. Biol. Chem.
275
,
18810-18817
.
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Notes:
The effect of suppressor of cytokine signaling (SOCS) expression on the Jak/STAT, MAPK, JNK, and p38 signaling pathways was examined in HepG2, Cos-7, and NIH 3T3 cells. Both PMA and bFGF (Promega) resulted in a rapid upregulation of SOCS-3 expression. MAPK, JNK, and p38 activation was monitored by Western blot analysis using the Anti-ACTIVE® MAPK Anti-ACTIVE® JNK pAb, and the Anti-ACTIVE® p38 pAb. Total levels of active and inactive MAPK protein was determined using the Anti-ERK 1/2 pAb, Rabbit.
(0002380) |
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Products: Anti-ACTIVE® JNK pAb, Rabbit, (pTPpY) | Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY) | Anti-ACTIVE® p38 pAb, Rabbit, (pTGpY) |
| 2. |
Kim, Y.-N., Wiepz, G.J., Guadarrama, A.G., Bertics, P.J.
(2000)
Epidermal growth factor-stimulated tyrosine phosphorylation of caveolin-1: Enhanced caveolin-1 tyrosine phosphorylation following aberrant epidermal growth factor receptor status.
J. Biol. Chem.
275
,
7481-7491
.
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Notes:
Murine 82L fibroblasts were transfected with truncated EGF receptor. In these cells, EGF, PDGF and PMA greatly increased activation of Erk 1 and 2 as judged by Western blotting with the Anti-ACTIVE® p38 pAb, Rabbit, (pTGpY). The treatments also caused the protein caveolin-1 to be phosphorylated as judged by gel shifting and recognition by an anti-tyrosine antibody after immunoprecipitation. The immunoreactivity was reduced when the immunoprecipitates were treated with Calf Intestinal Alkaline Phosphatase. The mobility shift could be reduced by preincubating the cells with either 10 or 50nM of MEK Inhibitor U0126 for 20 minutes prior to a 5-minute treatment with EGF. There was a concomitant reduction in ERK 1/2 phosphorylation as judged by the Anti-ACTIVE® p38 pAb, Rabbit, (pTGpY).
(0000902) |
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Products: Anti-ACTIVE® p38 pAb, Rabbit, (pTGpY) |
| 3. |
Paine, E., Palmantier, R., Akiyama, S.K., Olden, K., and Roberts, J.D.
(2000)
Arachidonic acid activates mitogen-activated protein (MAP) kinase-activated protein kinase 2 and mediates adhesion of a human breast carcinoma cell line to collagen type IV through a p38 MAP kinase-dependent pathway.
J. Biol. Chem.
275
,
11284-90
.
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Notes:
The signaling pathways involved in arachidonic acid-stimulated cell adhesion of human breast carcinoma cells to collagen type IV were examined. MAPK and JNK did not appear to play a role in mediating adhesion but p38 activation appears to be necessary. Levels of activated p38 was determined in MDA-MB-435 cell extracts by Western blot using the Anti-ACTIVE® p38 pAb. Whole cell lysates were subjected to SDS-PAGE, transferred to PVDF membranes, and incubated with the Anti-ACTIVE® p38 (1:1000 dilution).
(0002405) |
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Products: Anti-ACTIVE® p38 pAb, Rabbit, (pTGpY) |