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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 PLN 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, SYNPO2, PDLIM7, PLN, and SYNM down-regulation reflect the altered phenotype of smooth muscle cells in vascular disease and could be early sensitive markers of SMC dedifferentiation.
microRNAs (miRNAs) 1 and 21 bind PLN strongly and relieve PLN inhibition of SERCA 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 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(3) and degraded through Ser(16)-phosphorylation-mediated poly-ubiquitination during heart failure.
hereditary mutants of phospholamban are associated with heart failure [review]
PLN pentamers reduce phosphorylation of monomers at baseline and delay monomer phosphorylation upon PKA stimulation leading to increased interaction of PLN monomers with SERCA2a.
Phospholamban R14del mutation carriers are at high risk for malignant ventricular arrhythmias and end-stage heart failure, with left ventricular ejection fraction <45% and sustained or nonsustained ventricular tachycardia as independent risk factors.
Although SLN and PLB binding to SERCA have different functional outcomes on the coupling efficiency of SERCA, both proteins decrease the apparent Ca(2+) affinity of the pump, suggesting that SLN and PLB inhibit SERCA by using a similar mechanism.
Phospholamban, and its interacting partners, regulates excitation contraction coupling and myocardial contraction. [Review]
PLN mutations rarely cause cardiomyopathy
analysis of how the conformational dynamics of protein kinase A induced by a lethal mutant of phospholamban hinder phosphorylation
Aim of the present study is to determine the exact pattern of fibrosis and fatty replacement in PLN p.Arg14del mutation positive patients.
Engineered upregulation of PLB expression in hESC/iPSC-vCMs restores a positive inotropic response to beta-adrenergic stimulation.
a previously unrecognized mechanism for ESM cell contraction that depends on TGF-beta1, its receptors, and PLN.
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 or SERCA2 was assessed in ventricle, atrium, and skeltal msucle of mouse, rat, rabbit and pig.
Oxidative stress upregulates pVHL 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/phospholamban pathway.
combined deletion of Phd2 and Phd3 dramatically decreased expression of phospholamban (PLN), resulted in sustained activation of calcium/calmodulin-activated kinase II (CaMKII), and sensitized mice to chronic beta-adrenergic stress-induced myocardial injury
the N termini of SLN and PLB influence their respective unique functions
CaMKII-dependent increase in PLN phosphorylation during reperfusion opposes rather than contributes to ischemia/reperfusion damage.
TNAP plays a role in governing the phosphorylation status of phospholamban in the sarcoplasmic reticulum.
SLN and PLN are co-expressed in most fibers, which suggests that super-inhibition of SERCAs may be physiologically important in the regulation of intracellular Ca2+ in human skeletal muscle.
Epac1 KO exhibited decreased cardiac contractility with reduced phospholamban (PLN) phosphorylation at serine-16, the major PKA-mediated phosphorylation site.
Phospholamban knockout breaks cell-wide propagating spontaneous Ca2+ waves in isolated ventricular myocytes & protects RyR2-mutant mice from stress-induced ventricular tachycardia.
Data indicate that phospholamban (PLB) is not involved in heat generation and that sarcolipin (SLN) alone is responsible for muscle thermogenesis.
PLN is a critical target for CaMKII effects on FFR, while CaMKII effects on frequency-dependent acceleration of relaxation partially require PLN-alternative targets.
Dynamic regulation of the SERCA pump by phospholamban and/or sarcolipin maintains cardiac contractility in normal conditions and during pathophysiological states.
Data indicate that cardiomyocytes from PLN-KO/CaMKII-TG mice showed poor viability, improved by inhibiting SR Ca(2+) release and mitochondrial Ca(2+) loading.
although both phospholamban phosphorylation sites are involved in the mechanical recovery after myocardial ischemia, Thr17 appears to play a major role.
PLB phosphorylation by CaMKII plays an important role in limiting the decline in Ca transients (and contraction) during acidosis
Acute expression of R9C mutation of phospholamban in cardiomyocytes was positively inotropic/lusitropic.
Ca(2+) and PLB phosphorylation relieve SERCA-PLB inhibition by distinct mechanisms, but both are achieved primarily by structural changes within the SERCA-PLB complex, not by dissociation of that complex.
Phosphorylated phospholamban stabilizes a unique conformation of SERCA 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+) affinity within a physiological window.
demonstrate that the role of Arg(9) in phospholamban function is multifaceted: it is important for inhibition of SERCA, 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 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