Regulation of Na(+)-K(+)-ATPase by cAMP-dependent protein kinase anchored on membrane via its anchoring protein.

  title={Regulation of Na(+)-K(+)-ATPase by cAMP-dependent protein kinase anchored on membrane via its anchoring protein.},
  author={Kinji Kurihara and Nobuo Nakanishi and Takao Ueha},
  journal={American journal of physiology. Cell physiology},
  volume={279 5},
Na(+)-K(+)- ATPase alpha-subunits in basolateral membrane vesicles (BLMVs) purified from rat parotid glands were (32)P-labeled within 5 s by incubation with [gamma-(32)P]ATP at 37 degrees C in the presence of cAMP, but no labeling occurred without cAMP. Phosphorylation of Na(+)-K(+)-ATPase was associated with a decrease in its activity. This alpha-subunit phosphorylation disappeared when BLMVs were briefly incubated with cAMP and subsequent washing before the incubation with [gamma-(32)P]ATP… 

Regulation of renal Na(+),K(+)-ATPase and ouabain-sensitive H(+),K(+)-ATPase by the cyclic AMP-protein kinase A signal transduction pathway.

It is concluded that the cAMP-PKA pathway stimulates Na(+,K(+)-ATPase in the renal cortex as well as ouabain-sensitive H(+),K(+)-ATPases in the cortex and medulla by a mechanism requiring insertion of proteins into the plasma membrane.

Phosphorylation of the salivary Na(+)-K(+)-2Cl(-) cotransporter.

It is shown that when ATP is added to purified acinar basolateral membranes (BLM), NKCC1 is phosphorylated as a result of membrane-associated protein kinase activity, and this effect can be blocked by a specific PKA inhibitor.

Protein kinases A and C stimulate the Na+ active transport in frog skeletal muscle without an appreciable change in the number of sarcolemmal Na+ pumps.

  • R. A. Venosa
  • Biology, Medicine
    Acta physiologica Scandinavica
  • 2005
In frog skeletal muscle fibres, activation of both PKA and PKC stimulate the Na+ pump by increasing its rate of ionic translocation, and two modes of Na+ active transport are operative, and can be at work simultaneously, a phenomenon to be reckoned with.

Ischemia‐induced phosphorylation of phospholemman directly activates rat cardiac Na/K ATPase

The results indicate that the ischemia‐induced activation of the Na/K ATPase is indirect, through phosphorylation of PLM, which is an integral part of theNa/k ATPase enzyme complex in the heart, analogous to phospholamban in regulating the sarcoplasmic reticulum calcium ATPase.

Expression of Na+/K+-ATPase Was Affected by Salinity Change in Pacific abalone Haliotis discus hannai

Na+/K+-ATPase belongs to the P-type ATPase family, whose members are located in the cell membrane and are distributed in diverse tissues and cells, and the sudden salinity changes may affect NKA transcription activation, translation and enzyme activity via a cAMP-mediated pathway.

Cyclic nucleotide phosphodiesterases.

  • D. Essayan
  • Biology
    The Journal of allergy and clinical immunology
  • 2001
The available in vitro, preclinical, and clinical data supporting the potential for selective PDE inhibitors as immunomodulatory agents are reviewed.



Identification of the phosphorylation site for cAMP-dependent protein kinase on Na+,K(+)-ATPase and effects of site-directed mutagenesis.

Phosphorylation of the catalytic subunit of Na+,K(+)-ATPase inhibits the activity of the enzyme.

Two distinct protein kinases were examined for their ability to phosphorylate and regulate the activity of three different types of Na+,K(+)-ATPase preparation, including shark rectal gland preparation and preparations of basolateral membrane vesicles from rat renal cortex.

Conformation-dependent phosphorylation of Na,K-ATPase by protein kinase A and protein kinase C.

Identification of a 15-kDa cAMP-dependent Protein Kinase-anchoring Protein Associated with Skeletal Muscle L-type Calcium Channels*

A physical link between PKA and the calcium channel is demonstrated and anti-peptide antibodies directed against the α1 subunit of the calcium channels co-immunoprecipitate AKAP-15 are suggested to mediate their interaction.

Involvement of Direct Phosphorylation in the Regulation of the Rat Parotid Na+-K+-2Cl− Cotransporter (*)

Results indicate that direct phosphorylation is only one of the mechanisms involved in secretagogue-induced regulation of the rat parotid Na+-K+-2Cl− cotransporter.

Phosphorylated Mr 32,000 dopamine- and cAMP-regulated phosphoprotein inhibits Na+,K(+)-ATPase activity in renal tubule cells.

The results indicate that dopamine acts through a protein phosphorylation pathway to regulate the activity of an ion pump and suggest that inhibition of protein phosphatase 1 by phophorylated DARPP-32 is a component of the mechanism by which dopamine regulates urinary Na+ excretion.

Sodium-dependent regulation of sodium, potassium-adenosine-tri-phosphatase (Na+, K(+)-ATPase) activity in medullary thick ascending limb of Henle segments. Effect of cyclic-adenosine-monophosphate guanosine-nucleotide-binding-protein activity and arginine vasopressin.

Increased cyclic adenosine monophosphate (cAMP) levels inhibit Na+, K(+)-ATPase activity in mTAL, and AVP can, depending on Nai, produce this effect by adenylate cyclase activation.

Anchoring protein is required for cAMP-dependent stimulation of L-type Ca2+ channels in rabbit portal vein.

The data suggest that stimulation of Ca2+ channels in vascular myocytes by endogenous PKA requires localization of PKA through binding to AKAP, which is similar to the requirement of AKAP in PKA-dependent regulation of L-type Ca2-channel regulation in vascular smooth muscle cells.