Serine 68 phosphorylation of phospholemman: acute isoform-specific activation of cardiac Na/K ATPase

The mechanism by which the cardiac Na/K ATPase (NKA) is regulated by phosphorylation is controversial. We have used the perforated-patch technique to limit cell dialysis and maintain conditions as near physiological as possible. NKA pump current (I(p)) was measured in isolated guinea pig ventricular...

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Veröffentlicht in:	Cardiovascular research 2005, Vol.65 (1), p.93-103
Hauptverfasser:	SILVERMAN, Benjamin D. Z, FULLER, William, EATON, Philip, JUELIN DENG, MOORMAN, J. Randall, CHEUNG, Joseph Y, JAMES, Andrew F, SHATTOCK, Michael J
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Biological and medical sciences Cardiology. Vascular system Colforsin - pharmacology Cyclic AMP - metabolism Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors Enzyme Activation Guinea Pigs Heart Ventricles Isoquinolines - pharmacology Medical sciences Membrane Proteins - metabolism Microscopy, Fluorescence Myocytes, Cardiac - metabolism Patch-Clamp Techniques Phosphoproteins - metabolism Phosphorylation Protein Isoforms - metabolism Serine - metabolism Sodium-Potassium-Exchanging ATPase - antagonists & inhibitors Sodium-Potassium-Exchanging ATPase - metabolism Sulfonamides - pharmacology
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Zusammenfassung:	The mechanism by which the cardiac Na/K ATPase (NKA) is regulated by phosphorylation is controversial. We have used the perforated-patch technique to limit cell dialysis and maintain conditions as near physiological as possible. NKA pump current (I(p)) was measured in isolated guinea pig ventricular myocytes, and its components (I(alpha 1) and I(alpha 2)) defined by their differing dihydroouabain sensitivities. Treatment with 1 micromol/l forskolin for 4 min at 35 degrees C caused a significant increase in I(alpha1) of 36+/-15% (P
ISSN:	0008-6363 1755-3245
DOI:	10.1016/j.cardiores.2004.09.005