Distinct structural domains confer cAMP sensitivity and ATP dependence to the Na+/H+ exchanger NHE3 isoform.

@article{Cabado1996DistinctSD,
  title={Distinct structural domains confer cAMP sensitivity and ATP dependence to the Na+/H+ exchanger NHE3 isoform.},
  author={Ana Garc{\'i}a Cabado and F H Yu and Andr{\'a}s Kapus and G{\'a}bor Luk{\'a}cs and Sergio Grinstein and John Orlowski},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 7},
  pages={3590-9}
}
Agents known to increase cAMP levels in renal and intestinal epithelia decrease sodium absorption by inhibiting NHE3, an isoform of the Na+/H+ exchanger expressed at high levels in apical membranes of these cells. In contrast, the ubiquitous, housekeeping isoform of the exchanger (NHE1) is stimulated by cAMP in some cell types. Optimal activity of NHE3 as well as NHE1 requires the presence of ATP. To gain insight into the molecular mechanisms of ATP dependence and cAMP regulation of NHE3, a… CONTINUE READING