Inhibition of PKC phosphorylation of cTnI improves cardiac performance in vivo.

  title={Inhibition of PKC phosphorylation of cTnI improves cardiac performance in vivo.},
  author={Brian B. Roman and Paul H. Goldspink and Elyse Spaite and Dalia Urboniene and Ronald D. McKinney and David L. Geenen and R. John Solaro and Peter Buttrick},
  journal={American journal of physiology. Heart and circulatory physiology},
  volume={286 6},
Protein kinase C (PKC) modulates cardiomyocyte function by phosphorylation of intracellular targets including myofilament proteins. Data generated from studies on in vitro heart preparations indicate that PKC phosphorylation of troponin I (TnI), primarily via PKC-epsilon, may slow the rates of cardiac contraction and relaxation (+dP/dt and -dP/dt). To explore this issue in vivo, we employed transgenic mice [mutant TnI (mTnI) mice] in which the major PKC phosphorylation sites on cardiac TnI were… 

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  • Hui WangLin Wang Xian-min Meng
  • Biology
    Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas
  • 2013
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