IndraLab
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"Two types of modified GM3 strongly alter EGF dependent phosphorylation of the EGF receptor in opposite directions, i.e., de-N-acetyl-GM3 (amino-GM3; NeuNH2 alpha 2 ---- 3Gal beta 1 ---- 4Glc beta 1 ---- 1 Ceramide) strongly promotes tyrosine phosphorylation of the EGF receptor of A431 cells, while lyso-GM3 (NeuNAc alpha 2 ---- 3Gal beta 1 ---- 4 Glc beta ---- 1 Sphingosine) as well as GM3 inhibit tyrosine phosphorylation of the EGF receptor in the same cells under the same conditions."
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"It can intervene in EGF signaling, as it enhances Tyr phosphorylation of epidermal growth factor receptor (EGFR) in response to EGF.Pathway Effect EGF-EGFR-Ras-ERK Cell motility EGF-EGFR-Ras-PI3K-PKB Cell survivalEpigen (Epgn) 10 is a widely expressed transmembrane glycoprotein that undergoes cleavage to release a soluble EGF-like domain-containing fragment."
| PMC
"Stimulation of T47D cells with epidermal growth factor (EGF) results in the activation of the intrinsic tyrosine kinases of the receptor and the phosphorylation of multiple cellular proteins including the receptor, scaffold molecules such as c-Cbl, adapter molecules such as Shc, and the serine/threonine protein kinase Akt. "
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"Published and unpublished data indicate that the functional difference appears to be due to the fact that EGF stimulates greater EGFR tyrosine phosphorylation at EGFR Tyr1045 than does AREG, resulting in greater EGFR coupling to the ubiquitin ligase c-Cbl and greater EGFR ubiquitination and more rapid EGFR turnover."
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"The high affinity ligand, EGF, triggered more robust tyrosine phosphorylation of Egfr compared to the low affinity ligand, AREG, as determined by immunoblotting of liver extracts; however, similar activation of downstream Erk and Akt was found with both ligands (XREF_SUPPLEMENTARY)."
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"Our studies of the mechanism underlying the functional differences between ErbB4 full and partial agonists have been inspired by the observation that the EGFR full agonist AR stimulates a pattern of EGFR tyrosine phosphorylation that is distinct from the pattern of EGFR tyrosine phosphorylation stimulated by the EGFR partial agonist EGF [XREF_BIBR]."
"Stimulation of T47D cells with epidermal growth factor (EGF) results in the activation of the intrinsic tyrosine kinases of the receptor and the phosphorylation of multiple cellular proteins including the receptor, scaffold molecules such as c-Cbl, adapter molecules such as Shc, and the serine/threonine protein kinase Akt."
"We used mass spectrometry-based proteomics to comprehensively compare proteins that were tyrosine phosphorylated in response to EGF and PDGF and their associated partners. More than 90% of these signaling proteins were used by both ligands, whereas the phosphatidylinositol 3-kinase (PI3K) pathway was exclusively activated by PDGF,"
"We used mass spectrometry-based proteomics to comprehensively compare proteins that were tyrosine phosphorylated in response to EGF and PDGF and their associated partners. More than 90% of these signaling proteins were used by both ligands, whereas the phosphatidylinositol 3-kinase (PI3K) pathway was exclusively activated by PDGF,"
"we show that exposure to cigarette smoke over the indicated time points or doses results in an increase in total EGFR phosphorylation in a timeand dose-dependent manner (Fig. 1). As with EGF and H2O2, cigarette smoke is able to induce EGFR phosphorylation significantly compared to nontreated cells. Note: human airway epithelial (HAE; A549 or HBE1) were used in the paper"
"we show that exposure to cigarette smoke over the indicated time points or doses results in an increase in total EGFR phosphorylation in a timeand dose-dependent manner (Fig. 1). As with EGF and H2O2, cigarette smoke is able to induce EGFR phosphorylation significantly compared to nontreated cells. Note: human airway epithelial (HAE; A549 or HBE1) were used in the paper"
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"Five biological effects were considered : inhibition of high affinity 125I-EGF binding, change in the phosphorylation state of the EGF receptor, inhibition of the EGF dependent tyrosine phosphorylation of the EGF receptor, inhibition of [3H] phorbol 12 beta, 13 alpha-dibutyrate binding, and stimulation of calcium- and phospholipid dependent protein kinase (C-kinase) in vitro."
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"Treatment with Iressa elicited similar decreases in IL-17E- and EGF induced Y1086-EGFR phosphorylation in the three cell lines and markedly decreased EGFR tyrosine phosphorylation induced by the combination of IL-17E and EGF in BT20 and MDA-MB468 cells and, to a lesser extent, in IJG-1731 cells."
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"Notably, multiple studies have demonstrated that EGF can also stimulate tumor growth via several mechanisms : phosphorylation of EGFR tyrosine residues, ultimate activation of ERK (extracellular signal regulated kinase) pathways, and possible up-regulation of proliferative genes after intranuclear localisation of phosphorylated EGFR."
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"Ras activation by NEU3 was abrogated by PP2 (src inhibitor) or AG1478 (epidermal growth factor receptor (EGFR) inhibitor), and NEU3 actually enhanced EGF stimulated tyrosine phosphorylation of EGFR, suggesting that the upstream targets might be tyrosine kinases including src and EGFR, and the subsequent stimulation of Ras cascade leads to the inhibition of cell apoptosis."
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"In addition, EGF induced the sustained tyrosine phosphorylation of the EGF receptor, mitogen activated protein (MAP) kinases, and 46 and 52 kDa proteins, and the prolonged activation of MAP kinases in PC12h-R cells compared with the parent PC12h, which does not show EGF induced differentiation."
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"To this purpose, the effects of LHRH agonist, Zoladex (LHRH-A), on the mitogenic action of EGF, on EGF activated intracellular signaling mechanisms (tyrosine phosphorylation of EGF receptor and c-fos proto-oncogene expression), and on the concentration of EGF receptors have been evaluated in both LNCaP and DU 145 cells."
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"In KATO-III, a number of tyrosine phosphorylated proteins, including extracellular signal regulated protein kinases (ERKs) and epidermal growth factor receptor (EGFR), were observed irrespective of EGF stimulation and induction of ERK activity and EGFR tyrosine phosphorylation by EGF were less than that in MKN7."
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"Suppressing FUT1/4 expression blocked EGF-induced tyrosine phosphorylation of EGFR and MAPK and inhibited cancer growth (30); Yang et al (21) reported that FUT4 overexpression inhibited cyclophosphamide-induced apoptosis through activating the ERK/MAPK and PI3K/Akt signaling pathways."