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Background: Epidermal growth factor receptor (EGFR) is a 175 kDa transmembrane glycoprotein receptor tyrosine kinase that, activated by epidermal growth factor (EGF), affects cell growth and differentiation (1). Binding of EGF or TGF alpha to EGFR activates tyrosine kinase activity of the receptor (2). The epidermal growth factor (EGF) receptor is regulated by EGF-stimulated autophosphorylation and by phorbol ester-stimulated, protein kinase C (Ca2+/phospholipid-dependent enzyme) mediated phosphorylation at identified sites. Analysis of predicted secondary structure of the EGF receptor reveals that all of the phosphorylation sites are located near beta turns (3). I t has been reported that stimulating human glioblastoma cells with recombinant HGF induces biologically relevant EGFR activation. EGFR phosphorylation at Tyr(845) and Tyr(1068) increased 6 to 24 h after cell stimulation with HGF and temporally coincided with the induction of transforming growth factor-alpha (~5-fold) and HB-EGF (~23-fold) expression. Tyr(845) and Tyr(1068) phosphorylation, in response to HGF, was inhibited by cycloheximide and actinomycin D, consistent with a requirement for DNA transcription and RNA translation (4).