Activation of a microtubule-associated protein-2 kinase by insulin-like growth factor-I in bovine chromaffin cells.

@article{Cahill1991ActivationOA,
  title={Activation of a microtubule-associated protein-2 kinase by insulin-like growth factor-I in bovine chromaffin cells.},
  author={Anne L. Cahill and Robert L. Perlman},
  journal={Journal of neurochemistry},
  year={1991},
  volume={57 6},
  pages={1832-9}
}
Treatment of bovine chromaffin cells with insulin-like growth factor-I (IGF-I) caused the activation of a protein kinase that phosphorylates microtubule-associated protein-2 (MAP-2) in vitro. Activation of MAP-2 kinase by IGF-I varied with the time of treatment (maximal at 10-15 min) and the concentration of IGF-I (maximal at 10 nM). The IGF-I-activated MAP-2 kinase was localized to the soluble fraction of chromaffin cell extracts and required Mg2+ for activity. The IGF-I-activated kinase also… CONTINUE READING

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Treatment of bovine chromaffin cells with insulin - like growth factor - I ( IGF - I ) caused the activation of a protein kinase that phosphorylates microtubule - associated protein-2 ( MAP-2 ) in vitro .
Treatment of bovine chromaffin cells with insulin - like growth factor - I ( IGF - I ) caused the activation of a protein kinase that phosphorylates microtubule - associated protein-2 ( MAP-2 ) in vitro .
Treatment of bovine chromaffin cells with insulin - like growth factor - I ( IGF - I ) caused the activation of a protein kinase that phosphorylates microtubule - associated protein-2 ( MAP-2 ) in vitro .
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