Protein phosphorylation during activation of Na+/H+ exchange by phorbol esters and by osmotic shrinking. Possible relation to cell pH and volume regulation.

@article{Grinstein1986ProteinPD,
  title={Protein phosphorylation during activation of Na+/H+ exchange by phorbol esters and by osmotic shrinking. Possible relation to cell pH and volume regulation.},
  author={Sergio Grinstein and J D Goetz-Smith and Derek Stewart and B J Beresford and A. E. Mellors},
  journal={The Journal of biological chemistry},
  year={1986},
  volume={261 17},
  pages={8009-16}
}
In lymphocytes, the Na+/H+ antiport can be stimulated by 12-O-tetradecanoylphorbol 13-acetate (TPA) and by osmotic shrinking. Since TPA acts by stimulating protein kinase C, we undertook experiments to determine if protein phosphorylation also underlies the osmotic stimulation of the antiport. We found that at least one of the membrane polypeptides labeled in cells treated with TPA is also phosphorylated by hypertonic shrinking. In both instances phosphorylation is alkali labile and associated… CONTINUE READING