Phospholamban: a crucial regulator of cardiac contractility
Top Cited Papers
- 1 July 2003
- journal article
- review article
- Published by Springer Nature in Nature Reviews Molecular Cell Biology
- Vol. 4 (7) , 566-577
- https://doi.org/10.1038/nrm1151
Abstract
Heart failure is a major cause of death and disability. Impairments in blood circulation that accompany heart failure can be traced, in part, to alterations in the activity of the sarcoplasmic reticulum Ca2+ pump that are induced by its interactions with phospholamban, a reversible inhibitor. If phospholamban becomes superinhibitory or chronically inhibitory, contractility is diminished, inducing dilated cardiomyopathy in mice and humans. In mice, phospholamban seems to encumber an otherwise healthy heart, but humans with a phospholamban-null genotype develop early-onset dilated cardiomyopathy.Keywords
This publication has 110 references indexed in Scilit:
- Time Course and Mechanisms of Phosphorylation of Phospholamban Residues in Ischemia-reperfused Rat Hearts. Dissociation of Phospholamban Phosphorylation PathwaysJournal of Molecular and Cellular Cardiology, 2002
- Rescue of Contractile Parameters and Myocyte Hypertrophy in Calsequestrin Overexpressing Myocardium by Phospholamban AblationPublished by Elsevier ,2001
- Cardiac-specific Overexpression of a Superinhibitory Pentameric Phospholamban Mutant Enhances Inhibition of Cardiac Functionin VivoPublished by Elsevier ,2000
- Reduced Ca2+-Sensitivity of SERCA 2a in Failing Human Myocardium due to Reduced Serin-16 Phospholamban PhoshorylationJournal of Molecular and Cellular Cardiology, 1999
- Characterization of the Gene Encoding Human Sarcolipin (SLN), a Proteolipid Associated with SERCA1: Absence of Structural Mutations in Five Patients with Brody DiseaseGenomics, 1997
- Overexpression of the rat sarcoplasmic reticulum Ca2+ ATPase gene in the heart of transgenic mice accelerates calcium transients and cardiac relaxation.Journal of Clinical Investigation, 1997
- Mutation and Phosphorylation Change the Oligomeric Structure of Phospholamban in Lipid BilayersBiochemistry, 1997
- Structure of a Peptide Inhibitor Bound to the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein KinaseScience, 1991
- Complete complementary DNA-derived amino acid sequence of canine cardiac phospholamban.Journal of Clinical Investigation, 1987
- Phosphorylation of troponin I and phospholamban during catecholamine stimulation of rabbit heartNature, 1982