◀ Back to PRKAR2B
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