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EGF activates ERK. 1000 / 2279
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"These data indicate that EGF stimulates active ERK in a time- and concentration dependent manner in freshly isolated pGCs and that this experimental approach represents an effective manner with which to evaluate the role of EGF and the ERK signal transduction pathway in freshly harvested pGC."
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"In Panc-1 cells, FTS at a concentration of 25-100 microM reduced the amount of Ras in a dose dependent manner and interfered with serum dependent and epidermal growth factor stimulated ERK activation, thus inhibiting both anchorage dependent and anchorage independent growth of Panc-1 cells in vitro."
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"These findings were formalized mathematically [XREF_BIBR, XREF_BIBR] and have now also been validated experimentally by Hornberg et al. [XREF_BIBR], by measuring the time-course of extracellular signal related kinase (ERK) phosphorylation in fibroblast (NRK) cells treated with EGF in the presence or absence of inhibitors of the upstream MAP kinase kinase (MEK) or an inactivating MAP kinase phosphatase (PTP)."
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"Initial insight into this specificity dilemma came from observations that PC-12 cells proliferated after a transient ERK activation by epidermal growth factor (EGF), but differentiated after a sustained ERK activation by nerve growth factor (NGF), showing that the duration of ERK signaling is critical for cell fate decisions ( xref )."
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"It has been reported that transient overexpression of IQGAP1 in MCF-7 breast cancer cells significantly reduced activation of ERK1 and ERK2 by EGF, namely phospho-ERK1/2 was decreased. xref , xref Roy et al xref have reported that maximal activation of MEK and ERK by EGF was observed only when cellular IQGAP1 concentrations were close to normal levels."
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"Compounds 1 and 4 displayed strong cytotoxicity against three human tumor cell lines with GI50 values in the submicromolar range, whereas 2 showed subnanomolar activity as an inhibitor of EGFR-MAPK-AP1-mediated mitogenic signaling, causing inhibition of EGF mediated AP1 trans-activation and EGF mediated ERK activation and slight inhibition of EGF mediated JNK activation."
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"In contrast to IGF-1, AICAR did not block epidermal growth factor (EGF)-dependent Raf-1 and Erk activation, but our results demonstrated that multiple Raf-1 upstream pathways induced by EGF were differentially affected by AICAR: inhibition of Ras activation and simultaneous induction of Ras-independent Raf activation."
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"In previous studies, we compared human and rat goblet cells, and found that they were similar in their stimulation of proliferation by EGF, activation of ERK1/2 by EGF and cholinergic agonists, and the signaling pathways activated by EGF to stimulate proliferation ( xref , xref )."
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"In addition, in D283 cells, a cell line derived from medulloblastoma metastasis in the peritoneum, ouabain did not inhibit EGF-induced activation of Erk1/2 but reduced EGF-induced Akt activation (Fig. S2A) and almost completely abolished EGF-induced EGFR phosphorylation (Fig. S2B)."
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"We therefore constructed a new model of the EGF activated ERK pathway by taking the original Brown EGF model and expanding it to include receptor production and degradation as well as the C3G/Rap1/B-Raf pathway, which we believed were important processes in both normal EGF and cancerous signalling."
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"RCE in passage number 12-20 are a physiologically relevant model for studies on growth factor receptor mediated control of cell cycle progression and differentiation in its parent tissue as each of these phenomena were conserved : 1) EGF induced EGF receptor activation; 2) EGF activated ERK signaling; 3) expression of cornea specific differentiation markers; 4) karyotype profile; and 5) cell cycle control and progression."
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"To further investigate the bifurcation in EGF mediated activation of ERK1/2 versus STAT3 signaling upon subcellular compartmentalization of gefitinib, MDA-MB-468 cells were exposed to Gef-NArg, Gef-SV40-NArg, or gefitinib in a two-fold series of concentrations up to 1 muM for gefitinib or 5 muM for each peptoid conjugate (XREF_FIG)."
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"CMECs after being cultured for 2-3 days were randomly allocated to the following groups : control, control + the ROS donor XO/HX (con + XO/HX), control + the ERK1/2 activator EGF (con + EGF), control + the JNK and p38 activator ANISO (con + ANISO), H/R, H/R + the ROS scavenger NAC (H/R + NAC), H/R + the ROS scavenger EDA (H/R + EDA), H/R + ERK1/2 inhibitor U0126 (H/R + U0126), H/R + JNK inhibitor SP600125 (H/R + SP600125), H/R + p38 inhibitor SB203580 (H/R + SB203580), H/R + different doses of F 2, H/R + F 2 + XO/HX, H/R + F 2 + EGF, and H/R + F 2 + ANISO."
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"Overexpression of EGFR in MCF-7 cells confers estrogen independent growth, and studies using an MCF-7 cell line model of hormone resistance showed that EGF dependent activation of heterodimers of EGFR and HER1 and HER2 resulted in activation of the ERK pathway and increased cell proliferation."
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"While quantitative and systems-level analyses of EGF stimulated ERK activity have been performed, these studies have focused on acute re-stimulation of cells with growth factors following a period of withdrawal, which induces ERK signaling within minutes, followed by proliferation many hours later."
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"In mouse neuroblastoma N1E-115 cells, stimulation of AT2R inhibited EGF-induced ERK1/2 activation and cellular proliferation, and interestingly, not only was this effect blocked by PD123319, but it was also significantly inhibited by ATBP50 siRNA, indicating a functional modulatory interaction between ATBP50 and AT2R-mediated anti-mitogenic signalling (Wruck et al., 2005)."
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"Thus, pharmacologic blunting of basal and EGF induced ERK activity in C14 cells augmented early EGF induced EGFR activation; however, the overall 1068 Y phosphorylation signal at later EGF stimulation time points in PD98059 pretreated cells was not enhanced, likely in part because EGFR abundance was lessened at these later points in the inhibitor pretreated cells."
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"Pretreatment with the EGF receptor kinase inhibitor AG1478 had, remarkably, no significant effect on Erk1/2 activation induced by any of these adrenergic agonists (although it fully abolished EGF induced Erk1/2 activation), demonstrating absence of EGF receptor mediated transactivation."
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"Our results showed that EGF stimulated both MAPK and ERK and mTORC1 pathways, but had no effect on the PI3K and AKT pathway, suggesting that mTORC1 stimulation in EGF treated cells was regulated primarily by the MAPK (ERK1/2) signaling cascade and was independent of the PI3K and AKT pathway."
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"In a study by Impagnatiello et al. [ xref ] indicating an anti-proliferative effects of the overexpressed Spry1 and Spry2 on endothelial cells in the presence of FGF, VEGF, and EGF, while FGF- and VEGF-induced activation of ERK were repressed by Sprouty, EGF-activated ERK was left unaffected."
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"To verify the hypothesis that miR-543 regulate the progression of breast cancer via MAPK signal pathway, the gene expression and protein level of related factors including ERK2 and its phosphorylation site p-ERK1/2 were detected, as well as the pathway downstream factors such as RSK2, MSK1, p-RSK2 and p-MSK1 in the group of miR-543 mimics and MAPK and ERK activated group (miR-543 mimics treated with EGF)."
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"Thus, although PTHRP-induced mitogenesis may occur through an ERK-independent mechanism, the ability of PTHRP to potentiate the activation of ERK by EGF and IGF-1, together with the ability of cells to respond to autocrine PTHRP, could provide one explanation for the increased mitogenic responsiveness and reduced doubling times of MCF-7 cells overexpressing the PTHRP-R."
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"Further investigation revealed that both stimuli activated the same protein kinase, the extracellular signal regulated kinase (ERK), with a distinct temporal feature -- i.e., EGF induces a transient ERK activation -- whereas NGF triggers a sustained ERK activation [XREF_BIBR, XREF_BIBR, XREF_BIBR]."
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"Because Gab1’s association with Shp2 is critical for ERK1/2 activation by EGF and IGF-1 [ xref , xref , xref ], and because Grb2’s association with FRS2 is critical for this activation by bFGF [ xref , xref ], we determined if G i α proteins are important for these associations."
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"A sos1 (-/-) cell line, which expressed readily detectable levels of the closely related Sos2 protein, formed complexes between Sos2, epidermal growth factor receptor (EGFR) and Shc efficiently, gave normal Ras.GTP and ERK responses when treated with EGF for < or = 10 min and was transformed readily by activated Ras."
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"Notably, 11a-1 efficaciously attenuates cell viability and blocks EGF induced ERK1/2 activation in H1975 lung cancer cells; abrogates ERK1/2 and AKT activation in SKBR3 breast cancer cells and suppresses cell growth in a 3D Matrigel environment; and inhibits oncogenic KITD814V induced constitutive cell growth."
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"This sequence illustrates how non uniform EGF stimulation, which is visualized in the top row of images, can trigger a traveling wave of activated RAS that spreads over the plasma membrane (XREF_SUPPLEMENTARY) and that produces a transient gradient of ERK activity within the cell, which is visualized in the bottom row of images."
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"One important insight enabled by our study is that EGF solely leads to adaptive ERK activation (in the absence of continuous signaling input), while NGF can generate both adaptive and bistable outputs depending on growth factor input strength and duration and on population signaling heterogeneity."
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"XREF_BIBR These observations are in agreement with previous reports conducted both invivo and invitro that have indicated that BMP-4 inhibits EGF stimulated ERK activation in isolated parietal cells XREF_BIBR and that prolonged overexpression of growth factors in the stomach of mice alters the normal architecture of the gastric mucosa, leading to increased ERK activation, loss of parietal cells, and foveolar hyperplasia."
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"Overcoming this shortfall, we established a quantitative automated microscopy (QuAM) for a defined and multiparametric analysis of adherent heterogeneous primary neurons on a single cell base.The growth factors NGF, GDNF and EGF activate the MAP-kinase Erk1/2 via receptor tyrosine kinase signalling."
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"Here, we report that two structurally distinct PI3K inhibitors, wortmannin and LY294002, inhibited insulin-induced activation of ERK1/2 but had no effect on EGF-induced activation of ERK1/2 in hepatocellular carcinoma BEL-7402 and SMMC-7721 cells, breast cancer MCF-7 cells, and prostate cancer LNCaP cells."
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"Although the binding of EGF to the epidermal growth factor receptor (EGFR) was decreased in GnT-III transfectants to a level of about 60% of control cells, the EGF induced activation of extracellular signal regulated kinase (ERK) in GnT-III transfectants was enhanced to approximately 1.4-fold that of the control cells."
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"The loss of epidermal growth factor-induced activation and phosphorylation of ERK1/2 but not of their direct activator MEK1 in HeLa cells transfected with the p38alpha activator MKK6(E) indicated that activated p38alpha may sequester ERK1/2 and sterically block their phosphorylation by MEK1."
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"Positive rate of ER-alpha36 was increased in high-stage (P =.03) and high-grade (P =.224) endometrial cancer; expression of ER-alpha36 and EGFR exhibited a significant positive correlation (r = 0.334, P =.025) and they showed substantial colocalization on the plasma membrane of glandular cells; phospho-extracellular signal regulated kinase positive rate in ER-alpha36 positive group and EGFR positive group was higher than that of ER-alpha36 negative group (P =.014) and EGFR negative group (P =.016); finally, ER-alpha36 mediated epidermal growth factor stimulated extracellular signal regulated kinase activation in Hec1A cells."
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"MLK1-4 activated the MEK and ERK pathway in the presence of the RAF inhibitor but not the MEK inhibitor, indicating MLKs directly phosphorylate MEK (XREF_FIG and XREF_SUPPLEMENTARY in H157 cells; note both L779450 and U0126 blocked EGF stimulated ERK activation in cells, XREF_SUPPLEMENTARY)."
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"Sustained ERK activation by epidermal growth factor in PC12 cells overexpressing the epidermal growth factor receptor resulted in cell differentiation rather than proliferation, indicating that alteration of ERK activity can induce reversible changes in cell fate progression xref ."
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"These findings revealed that the expression of CCL3 in BMMs was regulated by ERK/CREB pathway.Recent one study indicated the EGF can be efficiently produced in MC-38 cells and EGF could activate the ERK pathway [15,16], thus we next explored whether MC-38-derived EGF contributed to the overexpression of CCL3 through ERK pathway."
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"Because glutamine is required for EGF stimulated proliferation and stimulates ERKs in intestinal cell culture, we hypothesized that glutamine and the EGF related peptide transforming growth factor-alpha (TGF-alpha) would synergistically enhance repair associated with stimulation of ERKs."
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"Overexpression of EGFR1 or HER2 as well as mutations that undermine the negative feedback regulation of the EGFR-ERK signaling pathway may transform the transient mode of the EGF induced ERK signaling to the sustained mode, and uncontrollably drive cells past the R-point [XREF_BIBR]."
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"53 It has been demonstrated that the PI3K and Akt and Erk1/2 signaling pathways are activated by EGF and p38 mitogen activated protein kinase (MAPK) by enhanced oxidative stress, all of which induce migration and invasion mediated by the up-regulation of Snail, Slug, ZEB1, and beta-catenin in association with GSK3beta inhibition in various cancers."
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"Since 2-APB did not block EGF activation of the ERK pathway, the PLCgamma-IP 3 R mediated increase in intracellular calcium is a previously undescribed independent regulator of EGF induced gene expression that works together with ERK activation to regulate immediate early gene expression."
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"In the presence of a NADH and NADPH oxidase inhibitor, diphenyleneiodonium (DPI) or an antioxidant, alpha-tocopherol, Ang II induced protein tyrosine phosphorylation of two major proteins (p120, p70) and ERK activation were markedly reduced, whereas ERK activation by epidermal growth factor was unaffected."
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"Binding of the epidermal growth factor (EGF) ligand to EGFR induces homo- or hetrodimerization of the receptor and activation of the kinase domain, ultimately leading to intracellular signaling events, including activation of protein kinase B (AKT), extracellular signal regulated kinase (ERK), and p38 mitogen activated protein kinase (MAPK)."
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"Importantly, SUMO1 modification at K 590 of hShp2 increased Shp2 binding to the Gab1, although having no effect on its catalytic activity, promoting EGF stimulated ERK activation and increasing HCC cell anchorage independent growth and xenograft tumor growth, which reveals a new mechanism for the regulation of Shp2 function in Ras and ERK signaling pathway."
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"Long-term, EGF induced ERK signaling is mainly controlled by ERK receptor feedback (XREF_FIG) and ligand induced degradation (XREF_FIG), short- and long-term HRG induced signaling is mainly controlled by RasGAP phosphorylation (XREF_FIG) and to a lesser extent the ERK-SOS feedback (XREF_FIG) and ERK-Gab feedback (XREF_FIG)."
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"The motogenic effect of TFF2 was previously demonstrated to depend on ERK1/2 and protein kinase C activation; whereas the EGF triggered motogenic response was completely independent of ERK1/2 activation but sensitive to the inhibition of phosphoinositide 3-kinase, p38, protein kinase C, or nuclear factor kappaB."
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"The overexpression or reduction of IQGAP1 expression by siRNA both caused the activation of Erk2 by EGF or IGF-1 in MCF-7 cells to be reduced, probably due to an optimal level of intracellular IQGAP1 being necessary for maximal level of activation of Erk by EGF or IGF-1 [ xref ]."
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"Finally, we observed that ERK inhibitor pretreatment alone enhanced EGF-dependent EGFR downregulation [ xref ], strongly suggesting that ERK-mediated EGFR threonine phosphorylation, whether accomplished by PRL or GH before EGF stimulation or resulting from EGF-induced ERK activation, can modulate EGF-induced EGFR downregulation."
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"A well-known example of a FRET based activity reporter is the extracellular signal regulated kinase activity reporter (EKAR) [XREF_BIBR], which has been used to study oscillatory EGF mediated ERK activation and relationships between ERK activity and nucleocytoplasmic shuttling [XREF_BIBR, XREF_BIBR]."
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"Since the initial observation that activation of ERK and PI3K by EGF is dependent on clathrin-dependent endocytosis [ xref ], endocytosis-dependent activation of ERK has been demonstrated in multiple receptor systems such as the insulin receptor [ xref ], the 5-HT receptor [ xref ], the m1 muscarinic receptor [ xref ] and the μ and δ opioid receptors [ xref , xref ]."
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"Consistently, AT2R inhibition of epidermal growth factor-activated extracellular signal-regulated kinase 1/2 was significantly reduced by the Rab1 mutants, indicating that endogenous Rab1 modulates the cell surface targeting and signaling of AT2R. It is of interest to note that Rab1 augmented the overall expression of AT2R and its mRNA, whereas the Rab1 mutants attenuated the total AT2R expression and enhanced ubiquitin-dependent AT2R degradation."
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"Furthermore, activation of ERK1/2 through EpEX-Fc and EGF in FaDu, Cal27, and Kyse30 cells was entirely blocked by an inhibitor of the upstream kinase MEK1 (AZD6244), whereas tyrosine kinase inhibitor (TKI) AG1478 entirely (Cal27) or partially (FaDu, Kyse30) blocked ERK1/2 activation by EpEX-Fc and EGF ( xref )."
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"Niacin showed a selected additive effect on chemoattractant-induced activation of ERK1/2, JNK and PI3K pathways, but only the MEK inhibitor UO126 reduced niacin-mediated inhibition of macrophage chemotaxis, while activation of ERK1/2 by EGF alone did not inhibit fMLF-mediated migration of HEK293T cells co-expressing HCA2 and fMLF receptor FPR1."
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"In a study by Edwin et al. [ xref ], where Spry2 unexpectedly inhibited EGF activation of AKT and exhibited no significant effect on EGF activation of EGFR and ERK, they observed that Spry2 increases the amount and activity of PTEN that was found necessary for Sprouty to attenuate EGF-activated AKT and to inhibit cell proliferation."
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"EGF exposure resulted in a transient, significant induction of PKC (81kDa) and ERK (43kDa) activation, with maximal ~ 2-fold (p < = 0.001) and ~ 1.6-fold (p < = 0.001) increases seen at 15 and 30min, respectively (XREF_FIG); activation of the other PKC and ERK proteins remained unaffected (XREF_FIG)."
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"Though many of the same pathways are activated by the inflammatory stimuli IL-1α and TNFα, and the mitogenic stimulus EGF, these stimuli differ strongly in their magnitude of activation: IL-1α and TNFα more strongly activate the NFκB, JNK, and p38 pathways, while EGF more strongly activates the MEK/ERK pathway (Fig. 6A)."
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"Whilst a complete mechanistic picture is lacking, studies in mammalian cell lines have revealed that Scrib depletion in EGF stimulated epithelial cells elevates ERK as well as JNK signalling [XREF_BIBR], and cell polarity perturbation leads to Hippo pathway impairment [XREF_BIBR, XREF_BIBR]."
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"In a study by Impagnatiello et al. [XREF_BIBR] indicating an anti-proliferative effects of the overexpressed Spry1 and Spry2 on endothelial cells in the presence of FGF, VEGF, and EGF, while FGF- and VEGF induced activation of ERK were repressed by Sprouty, EGF activated ERK was left unaffected."
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"To systematically analyze the effect of ERK signal duration on mRNA expression dynamics and its relationship with cell fate determination, we first aimed to modify the EGF triggered ERK signal duration by changing EGFR activation dynamics via impairment of ubiquitination and hence the receptor degradation process."
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"Widely expressed with highest levels in bone marrow, spleen, brain, testes, and embryonic brain, Abi1 may negatively regulate cell growth and transformation by interacting with the nonreceptor tyrosine kinases ABL1 and/or ABL2, thus regulating EGF induced Erk pathway activation and EGFR signaling."
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"We found that in HaCaT cells ADAM17 depletion reduces ERK1/2 phosphorylation, independent from the treatment with PsVs.To solidify the hypothesis that ADAM17 acts via the ERK signaling pathway in HPV16 infection and entry platform formation, we restored ERK activation by the addition of recombinant soluble form of the epidermal growth factor (EGF) which is one of the EGFR-activating ligands."
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"Metformin pretreatment also inhibited EGF stimulated ERK kinase activation, as evidenced by decreased phosphorylation of ERK at Thr201 and Tyr204 (XREF_FIG), consistent with the notion that metformin inhibits PDX-1 expression through a mechanism involving inhibition of EGF- stimulated ERK signaling (XREF_FIG)."
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"Whereas inhibition of EGF signaling clearly reduced the levels of active (phosphorylated) ERK in all three organoid types (i.e. P18T, NF1 and RASA1 KOs) after 1 hour of afatinib treatment, a substantial reactivation of ERK was observed in alive NF1 knock out organoids after 72 hours of afatinib treatment."
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"beta (2) AR dependent signaling to ERK1/2, like direct EGF stimulation of ERK1/2 activity, is sensitive to inhibitors of clathrin mediated endocytosis, suggesting that signaling downstream of both the EGF activated and the GPCR transactivated EGFRs requires a productive engagement of the complex with the cellular endocytic machinery."
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"While several studies have suggested that Erk activation can be regulated through the PI-3-kinase pathway [XREF_BIBR, XREF_BIBR] our data demonstrated that EGF stimulation of Erk activation in HC11 mammary epithelial cells was not altered by blocking PI-3-kinase signaling with LY294002."
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"Introduction of a SAICAR-insensitive or a non phosphorylatable PKM2 mutant inhibited the EGF stimulated ERK activation and consequent cancer cell proliferation, suggesting SAICAR induced PKM2 protein kinase activity is required for EGF mediated cancer cell proliferation [XREF_BIBR]."
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"Due to the lack of appropiate techniques it has not been analyzed in nociceptive neurons if there are differences in the kinetics of Erk1/2 in response to NGF versus EGF.Therefore‚ we investigated if nociceptive neurons express the EGF-receptor and if EGF results in activation of Erk1/2 similar to the growth factors NGF and GDNF."
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"Moreover, treatment of cells with epidermal growth factor (EGF) that activates MEK and ERK, as well as genetic ERK activation ( xref ) by a constitutively active MEK (MEK CA ) ( xref ), increased T562 phosphorylation levels; pharmacological or genetic MEK inhibition using the selective U0126 inhibitor or by expressing a dominant negative MEK mutant (MEK DN ); and reduced T562 phosphorylation; finally, in Mfn1 −/− cells re-expressing the MFN1 T562A mutant, phosphorylation was undetectable even in the presence of EGF ( xref G)."
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"On the other hand, epidermal growth factor causes a prolonged activation of Raf-1 kinase and ERK activity and a smaller, more transient activation of JNK, whereas the phorbol ester phorbol 12-myristate 13-acetate causes a small stimulation of Raf-1 kinase and a pronounced stimulation of ERK activity."
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"The combined data indicate that 1) EGF, TPA, and carbachol activate overlapping as well as distinct intracellular signaling pathways in gastric parietal cells, 2) EGF activates ERKs and enhances parietal cell acid secretory related functions via receptors with similar affinities, and 3) in contrast to some cell types, the parietal cell ERK signaling cascade does not appear to be directly modulated by the PtdIns 3-kinase pathway or by elevated intracellular free Ca2+ or adenosine 3 ',5 '-cyclic monophosphate concentrations."
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"Since the results presented here indicate that ERK mediates positive regulation of PDX-1 expression by EGF and metformin has recently been shown to inhibit ERK activation in PDAC cells [XREF_BIBR, XREF_BIBR, XREF_BIBR], we hypothesized that the metformin inhibits PDX-1 expression by abrogating EGF induced ERK activation."
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"In a two-hybrid screen, the catalytic domain of PMCA4b was found to interact with RASSF1 (via amino acids 144-193 of RASSF1A or amino acids 74-123 of RASSF1C), with co-expression in cells causing inhibition of the epidermal growth factor (EGF)-dependent activation of the Erk pathway (Erk is a downstream target of the Ras-Raf-MEK signalling cascade that activates cellular proliferation, see XREF_FIG) XREF_BIBR."
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"However, in breast cancer cells, abolishing PRMT5 mediated EGFR Arg1175 methylation increased EGF induced extracellular signal regulated kinase (ERK) activation by preventing the recruitment of Src homology 2 domain containing protein tyrosine phosphatase (SHP) 1 to EGFR, leading to enhanced cell proliferation, migration, and invasion of EGFR overexpressing tumor cells [XREF_BIBR]."
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"Experiments involving the expression of the dominant-negative mutants of Ras and Rap1 signaling (RasN17 or Rap1N17) indicate that both GTPases Ras and Rap1 are recruited for the ERK activation by VIP and PACAP38, whereas Rap1 is poorly involved in TRH or EGF-induced ERK activation."
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"The role played by Cdc42 in regulating the timing of EGF receptor-Cbl interactions is underscored by the fact that constitutively active Cdc42 (F28L), by persistently blocking the binding of Cbl to these receptors, leads to their aberrant accumulation and sustained EGF stimulated ERK activation, thus resulting in cellular transformation."
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"While GHR knockout is associated with diminished expression of the EGFR and a concomitant decrease in EGF signaling, GH overexpression results in EGFR overexpression with different effects depending on the signaling pathway analyzed : AKT and ERK1/2 pathways are induced by EGF, while STAT3 and STAT5 activation is heterologously desensitized."
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"An alternative pathway of PIP 3 -dependent ERK activation involves phosphoinositide dependent kinase-1 (PDK1), a target of PI3K, which can activate MEK directly and ERK indirectly through the activation of certain PKC isoforms, although it has been reported that PKCs are not involved in EGF induced ERK activation."
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"The results demonstrated that CHAG treatment efficiently blocked the phosphorylation and activation of EGFR, integrin and VEGFR, inhibited the EGF induced signaling of MAPK and ERK, PI3K and Akt and Rac1 mediated pathways, and diminished the EGF induced expression of proliferation and migration related proteins."
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"Firstly, RNAi studies by others XREF_BIBR, XREF_BIBR and our experiments (XREF_FIG and XREF_FIG) demonstrated that Shoc2 has significant role in EGF induced ERK1/2 activation only when mammalian cultured cells, such as HeLa, HEK293 and Cos1, are stimulated with low, physiological concentrations of EGF (< 1 ng/ml)."
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"Previous work with PC12 cells showed that epidermal growth factor (EGF) induces transient activation of extracellular signal regulated kinase (ERK) and results in cell proliferation, while sustained ERK activation triggered by nerve growth factor (NGF) leads to cell differentiation [XREF_BIBR, XREF_BIBR]."
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"For instance, epidermal growth factor-induced transient ERK activation via the Raf-MEK-ERK axis induces proliferation in PC12 neuroendocrine cells, whereas nerve growth factor-induced prolonged ERK activation via the Raf-MEK-ERK axis leads to the differentiation of PC12 cells into sympathetic neuron-like cells [ xref , xref ]."
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"Mitogenesis in response to EGF can not be studied in COS-7 cells as they are partially transformed, but it is known that picomolar EGF doses are able to activate the Ras and extracellular signal regulated kinase (ERK) signaling cascade, the central driver of cell proliferation in a PI3K dependent mode, in this cell type XREF_BIBR."