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PLN — PRKAR2B

Text-mined interactions from Literome

Yao et al., Biochemistry 2001 : A second-order loss of Ca-ATPase activation by PKA is observed as a function of the fractional contribution of FITC-PLB, indicating that PKA dependent activation of two PLB molecules within a quaternary complex containing the Ca-ATPase is necessary for activation of the Ca-ATPase ... We suggest that the requirement for activation of two PLB molecules by PKA represents a physiological mechanism to ensure that activation of the Ca-ATPase following beta-adrenergic stimulation in the heart only occurs above a threshold level of PKA activation
Antos et al., Circ Res 2001 (Cardiomyopathy, Dilated...) : As seen in human heart failure, these abnormalities correlated with PKA mediated hyperphosphorylation of the cardiac ryanodine receptor/Ca ( 2+ ) -release channel, which enhances Ca ( 2+ ) release from the sarcoplasmic reticulum, and phospholamban , which regulates the sarcoplasmic reticulum Ca ( 2+ ) -ATPase
Li et al., Circ Res 2002 (Calcium Signaling) : However, clear cellular data on PKA dependent modulation of cardiac RyRs is limited because of difficulty in distinguishing between PKA effects on RyR, phospholamban (PLB), and Ca2+ current ... In intact resting myocytes, PKA activation increased CaSpF 2.8-fold in WT, but not in PLB-KO , confirming results in permeabilized myocytes
Said et al., Pflugers Arch 2002 : The relative contribution of Thr ( 17 ) phosphorylation to the isoproterenol induced phosphorylation of PLB and relaxation thus increased with the level of beta-adrenoceptor stimulation and the consequent increase in PKA activity
Ait-Mamar et al., J Biol Chem 2005 : This was correlated with PKA dependent phosphorylation of PLB ( Ser16 )
Szentandrássy et al., J Physiol 2007 (Calcium Signaling) : Several different approaches indicated activation of PKA by EPA ( 5-10 micromol l ( -1 ) ) : the time constant of decay of the systolic Ca2+ transient decreased to 65.3 +/- 5.0 % of control, Western blot analysis showed a fourfold increase in phospholamban phosphorylation, and PKA activity increased by 21.0 +/- 7.3 %
Yu et al., Apoptosis 2008 (Myocardial Reperfusion Injury) : Moreover, insulin blunted ISO mediated increase in PKA activity, enhanced the PKA dependent phosphorylation of phospholamban (PLB) , resulting in increased sarcoplasmic reticulum Ca2+-ATPase ( SERCA2a ) activity
Lyashkov et al., Am J Physiol Heart Circ Physiol 2009 (Calcium Signaling) : At IC ( 50 ), CCh reduced cAMP and reduced PKA dependent phospholamban (PLB) phosphorylation by approximately 50 %
Wu et al., J Mol Cell Cardiol 2011 : These results demonstrate that FN acts via a5ß1 integrin to increase force production in myocardium and that this effect is partly mediated by increases in [ Ca ( 2+ ) ] ( i ) and Ca ( 2+ ) sensitivity, PKA activation and phosphorylation of phospholamban
Macdougall et al., J Mol Cell Cardiol 2012 : This was not linked to modulation of L-type Ca ( 2+ ) current, but instead to a discrete PKA mediated phosphorylation of phospholamban at Ser ( 16 )
Liu et al., J Mol Cell Cardiol 2011 (Calcium Signaling) : Inhibition of intrinsic PKA activity or inhibition of PDE in SANC, respectively : reduces or increases PLB phosphorylation, and markedly prolongs or reduces the LCR period ; and markedly reduces or accelerates SAN spontaneous firing rate
Xu et al., J Mol Cell Cardiol 1997 : Activation of SR CaM kinase with Ca2+ and calmodulin, or induction of phospholamban phosphorylation by exogenous PKA , resulted in stimulation of the Ca2+ uptake activity of SR in fetal, newborn and adult heart