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2 lethal PLN mutations, R9C and R25C, which lead to dilated cardiomyopathy, were studied by biomolecular NMR. R25C enhances phospholmaban dynamics and shifts the conformational equilibrium toward the R state. R9C drives the amphipathic cytoplasmic domain toward the membrane-associate state, enriching the T state.
Structure-Function Relationship of the SERCA Pump and Its Regulation by Phospholamban and Sarcolipin.
The co-transfection of VHL and PL (show VHL Proteins)N in HEK293 cells decreased PLN expression under oxidative stress, whereas knockdown of VHL increased PLN expression both under normal and oxidative stress conditions.
Hearts from patients with a p. Arg14del PLN mutation have a pattern of Right Ventricle Fibrofatty Replacement and Left Ventricular Fibrosis with fatty changes mostly in the posterolateral wall, independently of clinical presentation.
LMOD1 (show LMOD1 Proteins), SYNPO2 (show SYNPO2 Proteins), PDLIM7 (show PDLIM7 Proteins), PLN, and SYNM (show SYNM Proteins) down-regulation reflect the altered phenotype of smooth muscle cells in vascular disease and could be early sensitive markers of SMC (show DYM Proteins) dedifferentiation.
microRNAs (miRNAs) 1 and 21 bind PLN strongly and relieve PLN inhibition of SERCA (show ATP2A3 Proteins) to a greater extent than a similar length random sequence RNA mixture.
Data suggest phospholamban (PLN) gene is a rare cause of cardiomyopathy in African patients.
Phospholamban and sarcolipin are membrane proteins that differentially regulate SERCA (show ATP2A3 Proteins) function. (Review)
PLN may be a key molecular player in rigid substrate-induced cellular hypertrophy in eosinophilic esophagitis.
These data suggest that PLN is, at least partially, oligo-ubiquitinated at Lys (show LYZ Proteins)(3) and degraded through Ser (show SIGLEC1 Proteins)(16)-phosphorylation-mediated poly-ubiquitination during heart failure.
Phosphorylation of PLB induces spatial rearrangements between the N- and P-domain elements of proximal Ca-ATPase.
Molecular dynamics simulations of phospholamban in solution and in membrane bilayer show two main features: the presence of two well-defined helical domains at the N- and C-termini, and large-amplitude rigid-body motions of these domains.
The expression of SLN and PLB mRNA and protein relative to SERCA1 (show ATP2A1 Proteins) or SERCA2 (show ATP2A2 Proteins) was assessed in ventricle, atrium, and skeltal msucle of mouse, rat, rabbit and pig.
Oxidative stress upregulates pVHL (show VHL Proteins) expression to induce PLN degradation in failing hearts.
A single-dose injection of PLN-targeting locked nucleic acid antisense oligonucleotide improved contractility in pressure overload-induced cardiac dysfunction.
PLN overexpression is associated with severe muscle atrophy and weakness.
the commercially available overexpressing phospholamban mouse phenotypically resembles human Centronuclear myopathy and could be used as a model to test potential mechanisms and therapeutic strategies.
Cardioprotective effects of H2S are mediated through acGMP/PKG (show PRKG1 Proteins)/phospholamban pathway.
PLN pentamers reduce phosphorylation of monomers at baseline and delay monomer phosphorylation upon PKA stimulation leading to increased interaction of PLN monomers with SERCA2a (show ATP2A2 Proteins).
combined deletion of Phd2 (show EGLN1 Proteins) and Phd3 (show EGLN3 Proteins) dramatically decreased expression of phospholamban (PLN), resulted in sustained activation of calcium/calmodulin-activated kinase II (CaMKII (show CAMK2G Proteins)), and sensitized mice to chronic beta-adrenergic stress-induced myocardial injury
the N termini of SLN and PLB influence their respective unique functions
CaMKII (show CAMK2G Proteins)-dependent increase in PLN phosphorylation during reperfusion opposes rather than contributes to ischemia/reperfusion damage.
Acute expression of R9C mutation of phospholamban in cardiomyocytes was positively inotropic/lusitropic.
Ca(2 (show CA2 Proteins)+) and PLB phosphorylation relieve SERCA (show ATP2A3 Proteins)-PLB inhibition by distinct mechanisms, but both are achieved primarily by structural changes within the SERCA (show ATP2A3 Proteins)-PLB complex, not by dissociation of that complex.
Phosphorylated phospholamban stabilizes a unique conformation of SERCA (show ATP2A3 Proteins) that is characterized by a compact architecture.
Data suggest that phospholamban PLN's conformational equilibrium is central to maintain sarcoplasmic reticulum Ca(2+)-ATPase SERCA's apparent Ca(2 (show CA2 Proteins)+) affinity within a physiological window.
demonstrate that the role of Arg(9) in phospholamban function is multifaceted: it is important for inhibition of SERCA (show ATP2A3 Proteins), it increases the efficiency of phosphorylation, and it is critical for protein kinase A recognition
The interaction energies between the N-terminal helix of phospholamban and different POPC lipid/cholesterol bilayers quantitatively confirm its stronger interaction with a higher cholesterol-containing membrane.
The lipid bilayer composition influences the regulation of SERCA (show ATP2A3 Proteins) by PLN.
Phospholamban overexpression in rabbit ventricular myocytes does not alter sarcoplasmic reticulum Ca transport.
The protein encoded by this gene is found as a pentamer and is a major substrate for the cAMP-dependent protein kinase in cardiac muscle. The encoded protein is an inhibitor of cardiac muscle sarcoplasmic reticulum Ca(2+)-ATPase in the unphosphorylated state, but inhibition is relieved upon phosphorylation of the protein. The subsequent activation of the Ca(2+) pump leads to enhanced muscle relaxation rates, thereby contributing to the inotropic response elicited in heart by beta-agonists. The encoded protein is a key regulator of cardiac diastolic function. Mutations in this gene are a cause of inherited human dilated cardiomyopathy with refractory congestive heart failure.
, cardiac phospholamban