+ Site Statistics
+ Search Articles
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ PDF Full Text
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Translate
+ Recently Requested

Enhanced phosphorylation of phospholamban and downregulation of sarco/endoplasmic reticulum Ca2+ ATPase type 2 (SERCA 2) in cardiac sarcoplasmic reticulum from rabbits with heart failure

Enhanced phosphorylation of phospholamban and downregulation of sarco/endoplasmic reticulum Ca2+ ATPase type 2 (SERCA 2) in cardiac sarcoplasmic reticulum from rabbits with heart failure

Cardiovascular Research 41(1): 135-146

Objectives: To assess the phosphorylation of myocardial phospholamban (PLB) and quantify protein levels of PLB and sarco/ endoplasmic reticulum Ca2+ ATPase type 2 (SERCA 2) in a rabbit model of heart failure. Furthermore, to correlate these parameters with the rate of Ca2+ uptake into sarcoplasmic reticulum (SR) vesicles.

(PDF emailed within 0-6 h: $19.90)

Accession: 010590135

Download citation: RISBibTeXText

PMID: 10325961

DOI: 10.1016/s0008-6363(98)00241-7

Related references

Cloning and characterization of sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA) from crayfish axial muscle. Sarco/Endoplasmic Reticulum Ca(2+)-ATPase. Journal of Experimental Biology 203(Pt 22): 3411-3423, 2000

The N-Termini of Sarcolipin and Phospholamban Play an Important Role in Distinct Regulation of Sarco-Endoplasmic Reticulum Ca2+ ATPase (SERCA) Function. Biophysical Journal 110(3): 367a-368a, 2016

Characterizing phospholamban to sarco(endo)plasmic reticulum Ca2+-ATPase 2a (SERCA2a) protein binding interactions in human cardiac sarcoplasmic reticulum vesicles using chemical cross-linking. Journal of Biological Chemistry 287(10): 7582-7593, 2012

Phospholamban degradation is induced by phosphorylation-mediated ubiquitination and inhibited by interaction with cardiac type Sarco(endo)plasmic reticulum Ca(2+)-ATPase. Biochemical and Biophysical Research Communications 472(3): 523-530, 2016

Mechanism of action of sarcoplasmic reticulum calcium-uptake activators: Discrimination between sarco(endo)plasmic reticulum Ca-2+ ATPase and phospholamban interaction. European Journal of Biochemistry 247(3): 801-809, 1997

Cloning and characterization of the heart muscle isoform of sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) from crayfish. Journal of Experimental Biology 205(Pt 17): 2677-2686, 2002

In cold-hardy insects, seasonal, temperature, and reversible phosphorylation controls regulate sarco/endoplasmic reticulum Ca2+-ATPase (SERCA). Physiological and Biochemical Zoology 83(4): 677-686, 2010

Conditional mutations in SERCA, the Sarco-endoplasmic reticulum Ca2+-ATPase, alter heart rate and rhythmicity in Drosophila. Journal of Comparative Physiology. B, Biochemical, Systemic, and Environmental Physiology 176(3): 253-263, 2005

The sarcoplasmic reticulum calcium atpase serca 1a contains endoplasmic reticulum targeting information. Biochemical & Biophysical Research Communications 186(1): 219-227, 1992

Sarcoplasmic reticulum Ca(2+) atpase (SERCA) 1a structurally substitutes for SERCA2a in the cardiac sarcoplasmic reticulum and increases cardiac Ca(2+) handling capacity. Circulation Research 89(2): 160-167, 2001

Dynamic imaging of endoplasmic reticulum Ca2+ concentration in insulin-secreting MIN6 Cells using recombinant targeted cameleons: roles of sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA)-2 and ryanodine receptors. Diabetes 51 Suppl 1: S190-S201, 2002

Reduced Ca-2+-uptake and Ca-2+-ATPase-activity but unchanged protein levels of SERCA II- and phospholamban in cardiac sarcoplasmic reticulum from patients with dilated cardiomyopathy. European Heart Journal 16(SUPPL N): 113, 1995

Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban. Proceedings of the National Academy of Sciences of the United States of America 100(9): 5040-5045, 2003

The sarco/endoplasmic reticulum Ca(2+) ATPase (SERCA) is the third element in capacitative calcium entry. Cell Calcium 47(5): 412-418, 2010

Sarcolipin protein interaction with sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA) is distinct from phospholamban protein, and only sarcolipin can promote uncoupling of the SERCA pump. Journal of Biological Chemistry 288(10): 6881-6889, 2013