Protein Kinase B/Akt Phosphorylates and Inhibits the Cardiac Na+/H+ Exchanger NHE1

• Published in: Circulation research Vol. 103; no. 8; pp. 881 - 890
• Main Authors: Snabaitis, Andrew K., Cuello, Friederike, Avkiran, Metin
• Format: Journal Article
• Language: English
• Published: Hagerstown, MD American Heart Association, Inc 10.10.2008; Lippincott
• Subjects: Acidosis - enzymology; Animals; Biological and medical sciences; Calmodulin - metabolism; Cation Transport Proteins - genetics; Cation Transport Proteins - metabolism; Cells, Cultured; Fundamental and applied biological sciences. Psychology; Glycogen Synthase Kinase 3 - metabolism; Glycogen Synthase Kinase 3 beta; Humans; Hydrogen-Ion Concentration; Mutation; Myocytes, Cardiac - drug effects; Myocytes, Cardiac - enzymology; Phosphorylation; Protein Kinase Inhibitors - pharmacology; Proto-Oncogene Proteins c-akt - antagonists & inhibitors; Proto-Oncogene Proteins c-akt - genetics; Proto-Oncogene Proteins c-akt - metabolism; Rats; Recombinant Fusion Proteins - metabolism; Sarcolemma - enzymology; Serine; Sodium-Hydrogen Exchanger 1; Sodium-Hydrogen Exchangers - genetics; Sodium-Hydrogen Exchangers - metabolism; Time Factors; Transduction, Genetic; Vertebrates: cardiovascular system; Phosphorylation; Na+/H+ exchanger; Enzyme; Transferases; Non-specific serine/threonine protein kinase; PKB; Acid base balance disorder; Akt; Metabolic disorder; Vertebrata; Mammalia; Sodium; Circulatory system; Acidosis; Calmodulin

Sarcolemmal Na/H exchanger (NHE) activity is mediated by NHE isoform 1 (NHE1), which is subject to regulation by protein kinases. Our objectives were to determine whether NHE1 is phosphorylated by protein kinase B (PKB), identify any pertinent phosphorylation site(s), and delineate the functional co...