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The protein encoded by PLN is found as a pentamer and is a major substrate for the cAMP-dependent protein kinase in cardiac muscle. Additionally we are shipping Phospholamban Antibodies (129) and Phospholamban Kits (48) and many more products for this protein.
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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.
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 (show ATP2A2 Proteins).
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 (show ATP2A3 Proteins) have different functional outcomes on the coupling efficiency of SERCA (show ATP2A3 Proteins), both proteins decrease the apparent Ca(2 (show CA2 Proteins)+) affinity of the pump, suggesting that SLN and PLB inhibit SERCA (show ATP2A3 Proteins) 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.
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.
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.
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 (show Calm2 Proteins)-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.
TNAP (show ALPL Proteins) 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 (show CA2 Proteins)+ in human skeletal muscle.
Epac1 (show RAPGEF3 Proteins) KO exhibited decreased cardiac contractility with reduced phospholamban (PLN) phosphorylation at serine-16, the major PKA-mediated phosphorylation site.
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