[HTML][HTML] Distinct Structural Domains Confer cAMP Sensitivity and ATP Dependence to the Na+/H+ Exchanger NHE3 Isoform (∗)
AG Cabado, HY Frank, A Kapus, G Lukacs… - Journal of Biological …, 1996 - ASBMB
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 series of mutations were constructed …
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 series of mutations were constructed …