Key result
Protein kinase D facilitates cardiomyocyte contraction during high frequency by increasing Ca2+ sensitivity and maximal tension through phosphorylation of cMyBP-C at Ser315.
Why the study?
Does protein kinase D increase maximal Ca2+-activated tension of contraction by phosphorylation of cMyBP-C in cardiomyocytes?
Population
Permeabilized ventricular myocytes isolated from wild-type (WT) and cMyBP-C knockout (KO) mice
Comparison
Incubation in the presence of full-length active… vs WT vs cMyBP-C KO myocytes
Design
Preclinical
Authors
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Suggests protein kinase D as a contractile target; leaves open translation from this animal model to clinical use.
Does protein kinase D increase maximal Ca2+-activated tension of contraction by phosphorylation of cMyBP-C in cardiomyocytes?
Protein kinase D facilitates cardiomyocyte contraction during high frequency by increasing Ca2+ sensitivity and maximal tension through phosphorylation of cMyBP-C at Ser315.
Dirkx et al. (2012) studied this question. Protein kinase D (PKD) vs. Wild-type vs cMyBP-C knockout myocytes was evaluated on Myofilament Ca2+ sensitivity (pCa50) and maximal Ca2+-activated tension of contraction (Tmax). Protein kinase D facilitates cardiomyocyte contraction during high frequency by increasing Ca2+ sensitivity and maximal tension through phosphorylation of cMyBP-C at Ser315.
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