Angiotensin II activates at least two tyrosine kinases in rat liver epithelial cells. Separation of the major calcium-regulated tyrosine kinase from p125FAK.

@article{Earp1995AngiotensinIA,
  title={Angiotensin II activates at least two tyrosine kinases in rat liver epithelial cells. Separation of the major calcium-regulated tyrosine kinase from p125FAK.},
  author={H. Shelton Earp and William R. Huckle and Thomas L. Dawson and Xinghai Li and Lee M Graves and Ruth Dy},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 47},
  pages={28440-7}
}
In rat liver epithelial cell lines (WB or GN4), angiotensin II (Ang II) stimulates cytosolic tyrosine kinase activity, in part, through a calcium-dependent mechanism. In other cell types, selected hormones that activate Gi- or Gq-coupled receptors stimulate the soluble tyrosine kinase, p125FAK. Immunoprecipitation of p125FAK from Ang II-activated GN4 cells demonstrated a doubling of p125FAK kinase activity. However, an additional Ang II-activated tyrosine kinase (or kinases) representing the… CONTINUE READING
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