Key result
Protein kinase C isoforms differentially phosphorylate the Cav1.2 alpha1c subunit, with Ser1674 phosphorylation being specific to certain PKC isoforms but not others.
Population
HEK cells and Langendorff-perfused rat hearts
Comparison
PMA and bisindolylmaleimide vs Control/unstimulated conditions
Design
Preclinical
Authors
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Hypothesis-generating for isoform-selective PKC targeting of cardiac Cav1.2; leaves open translation to human contractility or arrhythmias.
Identifies specific phosphorylation sites on the Cav1.2 calcium channel that are differentially targeted by PKC isoforms, providing a molecular basis for their complex effects on cardiac contractility.
Yang et al. (2009) studied Cardiac contractility regulation. PMA and bisindolylmaleimide was evaluated on Phosphorylation of Ser1674 and Ser1928 within the alpha1c subunit. Protein kinase C isoforms differentially phosphorylate the Cav1.2 alpha1c subunit, with Ser1674 phosphorylation being specific to certain PKC isoforms but not others.
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