Intracellular transactivation of epidermal growth factor receptor by α1A-adrenoceptor is mediated by phosphatidylinositol 3-kinase independently of activation of extracellular signal regulated kinases 1/2 and serine-threonine kinases in Chinese hamster ovary cells.

@article{Ulu2013IntracellularTO,
  title={Intracellular transactivation of epidermal growth factor receptor by α1A-adrenoceptor is mediated by phosphatidylinositol 3-kinase independently of activation of extracellular signal regulated kinases 1/2 and serine-threonine kinases in Chinese hamster ovary cells.},
  author={Nadir Ulu and Robert H. Henning and Sahika Guner and Teuta Zoto and Basak Duman-Dalkilic and M. van Duin and Hakan Gurdal},
  journal={The Journal of pharmacology and experimental therapeutics},
  year={2013},
  volume={347 1},
  pages={47-56}
}
Transactivation of epidermal growth factor receptor (EGFR) by α1-adrenoceptor (α1-AR) is implicated in contraction and hypertrophy of vascular smooth muscle (VSM). We examine whether all α1-AR subtypes transactivate EGFR and explore the mechanism of transactivation. Chinese hamster ovary (CHO) cells stably expressing one subtype of α1-AR were transiently transfected with EGFR. The transactivation mechanism was examined both by coexpression of a chimeric erythropoietin (EPO)-EGFR with an… CONTINUE READING

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Moreover , α1A - AR stimulation enhanced phosphorylation of extracellular signal regulated kinase ( ERK ) 1/2 and serine - threonine kinases ( Akt ) , which were both unaffected by AG1478 , indicating that ERK1/2 and Akt phosphorylation is independent of EGFR transactivation .
Moreover , α1A - AR stimulation enhanced phosphorylation of extracellular signal regulated kinase ( ERK ) 1/2 and serine - threonine kinases ( Akt ) , which were both unaffected by AG1478 , indicating that ERK1/2 and Akt phosphorylation is independent of EGFR transactivation .
Moreover , α1A - AR stimulation enhanced phosphorylation of extracellular signal regulated kinase ( ERK ) 1/2 and serine - threonine kinases ( Akt ) , which were both unaffected by AG1478 , indicating that ERK1/2 and Akt phosphorylation is independent of EGFR transactivation .
Moreover , α1A - AR stimulation enhanced phosphorylation of extracellular signal regulated kinase ( ERK ) 1/2 and serine - threonine kinases ( Akt ) , which were both unaffected by AG1478 , indicating that ERK1/2 and Akt phosphorylation is independent of EGFR transactivation .
Moreover , α1A - AR stimulation enhanced phosphorylation of extracellular signal regulated kinase ( ERK ) 1/2 and serine - threonine kinases ( Akt ) , which were both unaffected by AG1478 , indicating that ERK1/2 and Akt phosphorylation is independent of EGFR transactivation .
Moreover , α1A - AR stimulation enhanced phosphorylation of extracellular signal regulated kinase ( ERK ) 1/2 and serine - threonine kinases ( Akt ) , which were both unaffected by AG1478 , indicating that ERK1/2 and Akt phosphorylation is independent of EGFR transactivation .
Moreover , α1A - AR stimulation enhanced phosphorylation of extracellular signal regulated kinase ( ERK ) 1/2 and serine - threonine kinases ( Akt ) , which were both unaffected by AG1478 , indicating that ERK1/2 and Akt phosphorylation is independent of EGFR transactivation .
Moreover , α1A - AR stimulation enhanced phosphorylation of extracellular signal regulated kinase ( ERK ) 1/2 and serine - threonine kinases ( Akt ) , which were both unaffected by AG1478 , indicating that ERK1/2 and Akt phosphorylation is independent of EGFR transactivation .
Moreover , α1A - AR stimulation enhanced phosphorylation of extracellular signal regulated kinase ( ERK ) 1/2 and serine - threonine kinases ( Akt ) , which were both unaffected by AG1478 , indicating that ERK1/2 and Akt phosphorylation is independent of EGFR transactivation .
Moreover , α1A - AR stimulation enhanced phosphorylation of extracellular signal regulated kinase ( ERK ) 1/2 and serine - threonine kinases ( Akt ) , which were both unaffected by AG1478 , indicating that ERK1/2 and Akt phosphorylation is independent of EGFR transactivation .
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