IndraLab

Statements

Kinase-active EGFR activates MAPK1. 20 / 20
12 8 |
bel
"The treatment of NCI-N87 cells with EGF resulted in increases in phosphorylation of Erk1/2, Akt, and P38. Blockade of the Erk, phosphatidylinositol-3 kinase/Akt, or P38 pathways in this cell line"
12618892
bel
"GRP induced rapid activation of p44/42 MAPK in lung cancer cells through EGFR."
15967120
bel
"activation of ERK depended on EGFR, Src tyrosine kinase and calcium calmodulin in PC12 cells (31), while requiring ras/Raf-1/MEK activation in human neutrophils (58)."
19273391
bel
"As previously reported, expression of Dok-R in EGF-stimulated cells resulted in a dramatic decrease in the induction of Erk-2 activation as well as a delay in the activation kinetics (Fig. 1), while Dok-R {Delta}PRR completely lost this Erk-2 attenuating capacity, which demonstrates that the key residues for mediating this attenuation are found within the PRR."
15831486
bel
"In addition, we were able to show in both BEAS-2B and 16HBE140- cells the involvement of the MAPK pathway and specifically of the EGFR-dependent MAPK/ERK1/2 pathway in mediating CSC-induced TJ alterations."
bel
"Studies to date suggest that, in these cancers, several (if not all) of the critical downstream signaling pathways, including the phosphoinositide 3-kinase (PI3K)/Akt, signal transducers and activators of transcription, and extracellular signal-regulated kinase 1 and 2 pathways, are solely controlled by EGFR. Thus, when the tumors are exposed to EGFR inhibitors, these intracellular pathways are turned off and the cancer cells undergo apoptosis (21, 22, 24, 25)."
18483355
bel
"An important finding is that intact BRCA1 also prevents EGF and IGF-I signaling through ERK to cell proliferation. EGF and IGF-1 are strongly implicated in the biology of human breast cancer, where they signal through this member of the MAP kinase family to cell growth (27, 52)."
15199145
bel
"Expression of wild-type (wt) Cbp remarkably suppressed EGF-induced activation of Src, ERK1/2, and Akt-1 enzymes, and NIH3T3 cell transformation, as well as colony formation of a breast cancer cell line (MDA-MB-468) in soft agar."
16636672
bel
"Mig-6 overexpression results in reduced activation of the mitogenactivated protein kinase ERK2 in response to EGF,"
11843178
bel
"Expression of wild-type (wt) Cbp remarkably suppressed EGF-induced activation of Src, ERK1/2, and Akt-1 enzymes, and NIH3T3 cell transformation, as well as colony formation of a breast cancer cell line (MDA-MB-468) in soft agar."
16636672
bel
"Mig-6 overexpression results in reduced activation of the mitogenactivated protein kinase ERK2 in response to EGF,"
11843178
bel
"As previously reported, expression of Dok-R in EGF-stimulated cells resulted in a dramatic decrease in the induction of Erk-2 activation as well as a delay in the activation kinetics (Fig. 1), while Dok-R {Delta}PRR completely lost this Erk-2 attenuating capacity, which demonstrates that the key residues for mediating this attenuation are found within the PRR."
15831486
bel
"PK1 induced a time-dependent increase in expression of IL-8 and COX-2, which was significantly reduced by inhibitors of Gq, cSrc, epidermal growth factor receptor (EGFR), and MAPK kinase. Treatment of third-trimester placenta with 40 nm PK1 induced a rapid phosphorylation of cSrc, EGFR, and ERK1/2. Phosphorylation of ERK1/2 in response to PK1 was dependent on sequential phosphorylation of cSrc and EGFR."
18372330
bel
"addition of AG1478 also suppressed ATP-mediated phosphorylation of ERK1/2 and I-?B? (Fig. 4A), indicating the involvement of EGFR activation in these signaling events."
19386603
bel
"PK1 induced a time-dependent increase in expression of IL-8 and COX-2, which was significantly reduced by inhibitors of Gq, cSrc, epidermal growth factor receptor (EGFR), and MAPK kinase. Treatment of third-trimester placenta with 40 nm PK1 induced a rapid phosphorylation of cSrc, EGFR, and ERK1/2. Phosphorylation of ERK1/2 in response to PK1 was dependent on sequential phosphorylation of cSrc and EGFR."
18372330
bel
"Studies to date suggest that, in these cancers, several (if not all) of the critical downstream signaling pathways, including the phosphoinositide 3-kinase (PI3K)/Akt, signal transducers and activators of transcription, and extracellular signal-regulated kinase 1 and 2 pathways, are solely controlled by EGFR. Thus, when the tumors are exposed to EGFR inhibitors, these intracellular pathways are turned off and the cancer cells undergo apoptosis (21, 22, 24, 25)."
18483355
bel
"The treatment of NCI-N87 cells with EGF resulted in increases in phosphorylation of Erk1/2, Akt, and P38. Blockade of the Erk, phosphatidylinositol-3 kinase/Akt, or P38 pathways in this cell line"
12618892
bel
"\"Dependence of peroxisome proliferator-activated receptor ligand-induced mitogen-activated protein kinase signaling on epidermal growth factor receptor transactivation.\" In the current study, we demonstrate that various PPARalpha (nafenopin) and gamma (ciglitazone and troglitazone) agonists rapidly induced extracellular signal-regulated kinase (Erk) and/or p38 phosphorylation in rat liver epithelial cells (GN4). The selective epidermal growth factor receptor (EGFR) kinase inhibitors, PD153035 and ZD1839 (Iressa), abolished PPARalpha and gamma agonist-dependent Erk activation."
12966092
bel
"GRP induced rapid activation of p44/42 MAPK in lung cancer cells through EGFR."
15967120
bel
"An important finding is that intact BRCA1 also prevents EGF and IGF-I signaling through ERK to cell proliferation. EGF and IGF-1 are strongly implicated in the biology of human breast cancer, where they signal through this member of the MAP kinase family to cell growth (27, 52)."
15199145