Alpha- and Beta-Adrenergic Stimulation of Protein Synthesis in Cultured Adult Ventricular Cardiomyocytes

A. Pinson, K. D. Schlüter, X. J. Zhou, P. Schwartz, G. Kessler-Icekson, H. M. Piper*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


The effect of the α1-adrenoceptor agonist phenylephrine (PE, 1-10 μM) and the β-adrenoceptor agonist isoprenaline (ISO, 1-10 μM) on protein synthesis and ultrastructure of ventricular cardiomyocytes from adult rat in culture (6 days in medium 199 plus 20% fetal calf serum) was studied. In these cultures cardiomyocytes were spread, but not spontaneously contractile. ISO and PE significantly increased total cell protein and incorporation of (14C)-phenylalanine within 24 h of exposure. These effects were inhibited by the antagonists propranolol and prazosin, respectively. The incorporation of (14C)-uridine was stimulated only by PE but not ISO. Induction of fetal BB-isoform of cytosolic creatine kinase was also caused only by P.E. but not ISO. The ultrastructure of PE-treated cardiomyocytes was altered as compared to controls, by a greater number of Golgi complexes, denser myofibrillar structures and the appearance of paracrystalline hands in mitochondrial matrices. In conclusion, in this culture model protein synthesis of cardiomyocytes can be stimulated, independently of the contractility, by either α1- or β-adrenoceptor agonists. Catecholamines differ, however, in their effects on specific cellular proteins and structures. Only α1-adrenergic stimulation leads to a "fetal shift" in the expression of CK-isofoms.

Original languageEnglish
Pages (from-to)477-490
Number of pages14
JournalJournal of Molecular and Cellular Cardiology
Issue number4
StatePublished - Apr 1993
Externally publishedYes


  • Creatine kinase
  • Isolated cardiomyocytes
  • Myocardial hypertrophy
  • Protein synthesis
  • RNA synthesis
  • α-adrenergic receptor
  • β-adrenergic receptor


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