Phosphorylation of cardiac myofibrillar proteins by protein kinase C (PKC) in isolated adult rat cardiomyocytes has been compared with that mediated by the cAMP-dependent protein kinase (PKA). PKA activation by β-adrenoreceptor (isoproterenol) stimulation results in stoichiometric phosphorylation of troponin I (TnI) and C-protein. PKC activation by either 12-O- tetradecanoylphorbol-13-acetate (TPA) or by α-adrenoreceptor (phenylephrine plus propranolol) stimulation results in phosphorylation of the same two proteins to similar extents. Two-dimensional phosphopeptide mapping shows that the same sites in TnI are modified by PKC in vitro and in TPA- or α- agonist-stimulated cells. These sites are distinct from those phosphorylated in isoproterenol-stimulated cells or by PKA in vitro. Phosphopeptide mapping analysis of C-protein shows that PKC and PKA phosphorylate identical residues in this protein in vitro and in situ. TPA-stimulated phosphorylation in myocytes is associated with a reduction in maximal activity of myofibrillar Ca2+-dependent actomyosin MgATPase. Isoproterenol-stimulated phosphorylation has no effect on maximal activity but reduces the Ca2+ sensitivity of the MgATPase. These data demonstrate that TnI and C-protein are phosphorylated in myocardial cells by both PKA and PKC, resulting in different functional consequences in each case.
|Original language||English (US)|
|Number of pages||7|
|Journal||Journal of Biological Chemistry|
|Publication status||Published - Jan 1 1993|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology