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Heart protein kinase C activity increases during progression of disease in the cardiomyopathic hamster

T C Chambers1, G Eilon

  • 1Department of Biological Chemistry, Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.

Biochemical and Biophysical Research Communications
|December 15, 1988
PubMed

Insights

Cardiomyopathic hamster hearts show increased protein kinase C activity and protein phosphorylation during disease progression. This suggests a role for protein kinase C in the development of heart disease.

Area of Science:

  • Biochemistry
  • Cardiovascular Biology
  • Molecular Cardiology

Background:

  • Protein kinase C (PKC) plays a crucial role in cellular signaling pathways.
  • Dysregulation of PKC activity is implicated in various cardiovascular diseases, including cardiomyopathy.
  • Understanding PKC involvement in heart disease is vital for developing therapeutic strategies.

Purpose of the Study:

  • To investigate the activity of protein kinase C in the heart during the progression of cardiomyopathy.
  • To examine the endogenous protein phosphorylation patterns in cardiomyopathic hearts.
  • To compare PKC activity and phosphorylation in diseased versus healthy control hearts.

Main Methods:

  • Enzyme assays were performed to measure protein kinase C activity in heart particulate fractions.
  • Endogenous protein phosphorylation was analyzed using gel electrophoresis in solubilized particulate fractions.
  • Comparisons were made between myopathic hamsters and age-matched healthy controls.

Main Results:

  • Protein kinase C activity was found to be elevated two-fold in the particulate fraction of hearts from mid-stage cardiomyopathic hamsters compared to controls.
  • Several endogenous proteins (Mr 26, 31, 45, 53, 69, 98, 105, and 126 kDa) exhibited increased phosphorylation in myopathic hearts.
  • No significant differences in cytosolic protein kinase C or phosphoinositide-specific phospholipase C activities were observed between groups.

Conclusions:

  • The study demonstrates an upregulation of protein kinase C activity and enhanced protein phosphorylation in the heart during experimental cardiomyopathy.
  • These findings suggest that protein kinase C dysregulation contributes to the pathogenesis of heart muscle disease.
  • Further research into PKC signaling pathways may reveal novel therapeutic targets for cardiomyopathy.

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