SR Ca(2+)-ATPase/phospholamban in cardiomyocyte function

Journal of Cardiac Failure
M Tada, T Toyofuku

Abstract

Ca ATPase regulates intracellular Ca levels by pumping Ca into sarcoplasmic and endoplasmic reticulum (SER). Phospholamban was first identified as a phosphoprotein in cardiac myocytes. Functional properties of phospholamban by steady-state and presteady-state kinetic studies of Ca pump ATPase suggest that phospholamban functions as an inhibitory co-factor for cardiac Ca ATPase (SERCA 2). Protein kinase A-catalyzed phosphorylation of phospholamban results in the dissociation of phospholamban from the Ca ATPase, thus augmenting the ATPase activity. Phospholamban is found as a homo-pentamer, formed from subunits of 6080 Da in size. PKA-catalyzed and CAM kinase- catalyzed phosphorylation residues (Ser 16 and Thr 17) are located in the N-terminal cytoplasmic domain, whereas the C-terminal 22 residues are extremely hydrophobic and are considered to be embedded in the SR membrane. At least three kinds of Ca ATPase have been found. SERCA 1 is expressed in fast-twitch skeletal muscle, while the SERCA 2 gene encodes two alternatively spliced products, SERCA 2a and 2b. SERCA 2a is expressed in cardiac and slow-twitch skeletal muscles; SERCA 2b in smooth muscle and non-muscle tissues. SERCA 3 is expressed in a broad variety of muscle and n...Continue Reading

References

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Citations

Apr 21, 2012·Science Translational Medicine·Ning SunJoseph C Wu
Mar 21, 1998·Proceedings of the National Academy of Sciences of the United States of America·S Tertyshnikova, A Fein
May 27, 2008·Annals of Biomedical Engineering·Yen-Chih HuangRavi K Birla
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Sep 11, 2007·Progress in Biophysics and Molecular Biology·Masanori KuzumotoSatoshi Matsuoka
Nov 11, 2009·Biochemical and Biophysical Research Communications·Miguel A RocafullJesús R Del Castillo

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