Key result
Isoproterenol stimulation markedly increased the phosphorylation of Ser-2030, but not Ser-2808, in both normal and failing rat hearts, indicating Ser-2030 is the major PKA phosphorylation site.
Why the study?
Does isoproterenol stimulation increase phosphorylation of RyR2 at Ser-2030 or Ser-2808 in normal and failing rat hearts?
Population
Recombinant and native RyR2 from multiple species, rat cardiac myocytes, and normal and failing rat hearts
Comparison
Isoproterenol (beta-adrenergic stimulation) vs Unstimulated state (baseline)
Design
Preclinical
Authors
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Challenges prevailing view of RyR2 hyperphosphorylation by PKA in heart failure; leaves open confirmation in human myocardium.
Does isoproterenol stimulation increase phosphorylation of RyR2 at Ser-2030 or Ser-2808 in normal and failing rat hearts?
Ser-2030, not Ser-2808, is the major PKA phosphorylation site on RyR2 responding to beta-adrenergic stimulation in normal and failing hearts, suggesting RyR2 is not hyperphosphorylated by PKA in heart failure.
Xiao et al. (2006) studied Heart failure. Isoproterenol (beta-adrenergic stimulation) was evaluated on Phosphorylation of RyR2 at Ser-2030 and Ser-2808. Isoproterenol stimulation markedly increased the phosphorylation of Ser-2030, but not Ser-2808, in both normal and failing rat hearts, indicating Ser-2030 is the major PKA phosphorylation site.
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