Phosphorylation and activation of beta-adrenergic receptor kinase by protein kinase C.

@article{Chuang1995PhosphorylationAA,
  title={Phosphorylation and activation of beta-adrenergic receptor kinase by protein kinase C.},
  author={Tsu Tshen Chuang and H I Levine and Antonio de Blasi},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 31},
  pages={18660-5}
}
The aim of this study was to test the possible modification of beta-adrenergic receptor kinase (beta ARK) activity by second messengers and/or their downstream components. Using human mononuclear leukocytes (MNL), we found that calcium ionophores could elevate beta ARK activity by about 80% in a protein kinase C (PKC)-dependent manner. This was confirmed by the ability of the PKC activator phorbol 12-myristate 13-acetate (PMA) to produce a similar effect, suggesting a PKC-dependent modulation… CONTINUE READING

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