Cytochrome c oxidase subunit IV as a marker of protein kinase Cepsilon function in neonatal cardiac myocytes: implications for cytochrome c oxidase activity.

@article{Ogbi2004CytochromeCO,
  title={Cytochrome c oxidase subunit IV as a marker of protein kinase Cepsilon function in neonatal cardiac myocytes: implications for cytochrome c oxidase activity.},
  author={Mourad Ogbi and Catherine S. Chew and J. Pohl and Olga Stuchlik and Safia N Ogbi and J Aaron Johnson},
  journal={The Biochemical journal},
  year={2004},
  volume={382 Pt 3},
  pages={923-32}
}
We have previously demonstrated that low concentrations of phorbol esters stimulate the selective translocation of protein kinase C (PKC) alpha and epsilon from the cell soluble to the particulate fraction in NCMs (neonatal rat cardiac myocytes). We therefore determined if the in vitro phosphorylation of substrates in these fractions could be used as assays of PKCalpha or epsilon activation. Intact cell phorbol ester treatment caused a decline in the in vitro (32)P-incorporation into several… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 31 extracted citations

Ischemic preconditioning targets the respiration of synaptic mitochondria via protein kinase C epsilon.

The Journal of neuroscience : the official journal of the Society for Neuroscience • 2008
View 11 Excerpts
Highly Influenced

Cardiac mitochondrial matrix and respiratory complex protein phosphorylation.

American journal of physiology. Heart and circulatory physiology • 2012

Similar Papers

Loading similar papers…