February 1, 1996Journal of Biological ChemistryOpen Access

Distinct Structural Domains Confer cAMP Sensitivity and ATP Dependence to the Na+/H+ Exchanger NHE3 Isoform

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Population

Antiport-deficient Chinese hamster ovary cells heterologously expressing wild-type, truncated, or chimeric…

Design

Preclinical

Authors

ACAna G. CabadoANFACO-CECOPESCA FYFrank H. YuElectrophysiology AKAndrás KapùsSt. Michael's Hospital

Discussion

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Implication

No immediate clinical implications; leaves open whether NHE3 domain mapping advances cardiovascular therapeutics.

Structured PICO

Population

Antiport-deficient Chinese hamster ovary cells heterologously expressing wild-type, truncated (NHE3delta684, NHE3delta638, NHE3delta579), or chimeric (NHE3/1, NHE1/3) Na+/H+ exchanger constructs

Intervention

Forskolin (to stimulate adenylate cyclase and increase cAMP) and ATP depletion

Outcome

Na+/H+ exchanger activity assessed by fluorimetric measurements of intracellular pH and radioisotope determinations of Na+ influxsurrogate

Distinct structural domains of the NHE3 isoform mediate its inhibition by cAMP (cytoplasmic domain between amino acids 579 and 684) and its dependence on ATP (transmembrane domain).

Cite This Study

Cabado et al. (1996) studied this question.

synapsesocial.com/papers/6a09314c0d765b5cefd25a88 https://doi.org/10.1074/jbc.271.7.3590

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Distinct Structural Domains Confer cAMP Sensitivity and ATP Dependence to the Na+/H+ Exchanger NHE3 Isoform

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Distinct Structural Domains Confer cAMP Sensitivity and ATP Dependence to the Na+/H+ Exchanger NHE3 Isoform

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider