Glucagon promotes cAMP-response element-binding protein phosphorylation via activation of ERK1/2 in MIN6 cell line and isolated islets of Langerhans.

@article{Dalle2004GlucagonPC,
  title={Glucagon promotes cAMP-response element-binding protein phosphorylation via activation of ERK1/2 in MIN6 cell line and isolated islets of Langerhans.},
  author={St{\'e}phane Dalle and Christine Longuet and Safia Costes and Christophe Broca and Omar Faruque and Ghislaine Font{\'e}s and El Habib Hani and Dominique Bataille},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 19},
  pages={20345-55}
}
By using the MIN6 cell line and pancreatic islets, we show that in the presence of a low glucose concentration, corresponding to physiological glucagon release from alpha cells, glucagon treatment of the beta cell caused a rapid, time-dependent phosphorylation and activation of p44/p42 mitogen-activated protein kinase (ERK1/2) independently from extracellular calcium influx. Inhibition of either cAMP-dependent protein kinase (PKA) or MEK completely blocked ERK1/2 activation by glucagon. However… CONTINUE READING
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