Growth hormone and prolactin stimulate tyrosine phosphorylation of insulin receptor substrate-1, -2, and -3, their association with p85 phosphatidylinositol 3-kinase (PI3-kinase), and concomitantly PI3-kinase activation via JAK2 kinase.

@article{Yamauchi1998GrowthHA,
  title={Growth hormone and prolactin stimulate tyrosine phosphorylation of insulin receptor substrate-1, -2, and -3, their association with p85 phosphatidylinositol 3-kinase (PI3-kinase), and concomitantly PI3-kinase activation via JAK2 kinase.},
  author={Tatsuyuki Yamauchi and Yosuke Kaburagi and Kohjiro Ueki and Yuji Tsuji and George R Stark and Ian M. Kerr and Toshio Tsushima and Yasuo Akanuma and Issei Komuro and Kazuyuki Tobe and Yoshio Yazaki and Takashi Kadowaki},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 25},
  pages={15719-26}
}
Growth hormone (GH) and prolactin (PRL) binding to their receptors, which belong to the cytokine receptor superfamily, activate Janus kinase (JAK) 2 tyrosine kinase, thereby leading to their biological actions. We recently showed that GH mainly stimulated tyrosine phosphorylation of epidermal growth factor receptor and its association with Grb2, and concomitantly stimulated mitogen-activated protein kinase activity in liver, a major target tissue. Using specific antibodies, we now show that GH… CONTINUE READING
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