IndraLab

"When the EGFR extracellular domain binds to its ligands, such as epidermal growth factor (EGF) and transforming growth factor-α (TGF-α), it forms dimers with other EGFR or other HER family members and undergoes autophosphorylation at the key tyrosine residues, thus activating several downstream signalling pathways such as protein kinase B (AKT/PKB) and mitogen-activated protein kinases (MAPK), which regulate multiple cellular processes, including proliferation, survival and apoptosis."

"For example, one method by which the pathway begins involves the binding of epidermal growth factor and transforming growth factor α (TGFα) to the epidermal growth factor receptor (EGFR), a tyrosine kinase [88]."

"At least two ligands bind to the EGFR, EGF, and transforming growth factor—α."

"Upon the specific ligands such as EGF and transforming growth factor-α (TGF-α) binding to the extracellular domain of EGFR, homodimerization or heterodimerization with other ErbB family members activates the tyrosine kinase domain and consequent modulation of signal transduction cascades involved in cellular responses including proliferation, migration, adhesion, angiogenesis, and apoptosis [ xref , xref , xref , xref , xref ]."

"Ligands such as EGF or transforming growth factor bind to EGFR, which stimulates the tyrosine kinase activity of the receptor."

"For instance, both transforming growth factor (TGF) α and epidermal growth factor (EGF) bind to the EGF receptor (EGFR), but whereas TGFα and EGFR are located on the basolateral surface, EGF is located on the apical surface of epithelial cells. xref , xref The difficulty in studying autocrine signaling is also related to the complexity of autocrine signaling systems (Figure  xref ), which include many more entities than just one ligand and one receptor; they consist of proteinases, signaling proteins, extracellular matrix proteins, competing ligands, competing receptors, and cellular components (Figure  xref )."

"Specific ligands, such as epidermal growth factor (EGF) and transforming growth factor-α (TGF-α), bind to EGFR resulting in receptor dimerization and activation of tyrosine kinase, with receptor auto-phosphorylation and downstream signal transduction. xref – xref Signaling through EGFR has been reported to induce proliferation, invasion, and angiogenesis of tumor cells. xref , xref EGFR is frequently overexpressed in both cell lines and tissues of NSCLC xref – xref and overexpression has been reported to be associated with higher incidence of lymph node metastasis, advanced stage, poor differentiation, and a worse prognosis. xref – xref However, several reports, including a meta-analysis failed to confirm a correlation between overexpression of EGFR and patient outcome. xref , xref In addition, no correlation was found between EGFR expression and tumor response to gefitinib, an EGFR tyrosine kinase inhibitor, in patients with NSCLC. xref Therefore, the clinical significance of EGFR expression in NSCLC is still controversial."

"Complementing these receptors is a family of ligands: e.g. EGF and transforming growth factor-α (TGF-α) bind only to ErbB1 (EGFR), heparin-binding EGF (HB-EGF) binds to both ErbB1 and ErbB4, and neuregulin 1 (NRG1) which binds to ErbB3 and ErbB4."

"For example, one method by which the pathway begins involves the binding of epidermal growth factor and transforming growth factor α (TGFα) to the epidermal growth factor receptor (EGFR), a tyrosine kinase [ xref ]."

"The data presented by Doctor Schwab indicated that the anti-epidermal growth factor receptor antibody was no better than C225 for blocking epidermal growth factor/transforming growth factor-α binding [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"It has been shown that the overexpression of EGFR is common in ESCC, with an incidence of 50–70%, xref , xref , xref and the overexpression is significantly related to prognosis. xref , xref , xref Nimotuzumab is a recombinant humanized monoclonal IgG1 antibody against human EGFR and blocks the binding of EGF and transforming growth factor‐a to EGFR."

"Epidermal growth factor (EGF) and transforming growth factor-α bind directly only to EGFR, whereas neuregulins (also known as heregulins) are specific for ErbB3 and ErbB4 xref , xref ."

"High EGFR expression is said to be found in 25–77% of colon cancers and 90% or more of HNSCC [ xref , xref ], when ligands such as EGF and transforming growth factor-α (TGF-α) bind to EGFR, they form a dimer with EGFR or other human epidermal growth factor receptor (HER) family members."

"Extracellular ligands, such as epidermal growth factor (EGF) and transforming growth factor-α (TGF-α), can interact with the EGFR [ xref ], resulting in the stimulation of Akt/PI3K and downstream molecules, including mTOR, eNOS, and the Bcl2-associated antagonist of cell death (BAD)."

"Nimotuzumab, a recombinant humanized monoclonal immunoglobulin G 1 antibody against human EGFR (HER-1), blocks the binding of epidermal growth factor (EGF) and transforming growth factor-α to EGFR."

"When a ligand, such as epidermal growth factor or transforming growth factor-α, binds to EGFR, EGFR dimerizes and a downstream signaling pathway is initiated via the phosphoinositide 3-kinase (PI3K)/Akt and mitogen-activated protein kinase (MAPK) pathways."

"Ligands such as epidermal growth factor (EGF) or transforming growth factor-α (TGF-α) bind to EGFR, resulting in its activation and receptor transphosphorylation."

"Upon the specific ligands such as EGF and transforming growth factor-α (TGF-α) binding to the extracellular domain of EGFR, homodimerization or heterodimerization with other ErbB family members activates the tyrosine kinase domain and consequent modulation of signal transduction cascades involved in cellular responses including proliferation, migration, adhesion, angiogenesis, and apoptosis [9,10,11,12,13]."

"The PI3K pathway is activated when EGFR binds to ligands such as EGF or transforming growth factor-α (TGF-α), and subsequently promotes phosphatidylinositol 3,4,5-trisphosphate production which initiates Akt activation."