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J. Biol. Chem., Vol. 266, Issue 16, 10023-10026, Jun, 1991
K Kariya, LR Karns and PC Simpson
Cultured neonatal rat cardiac myocytes express at least three isozymes of
protein kinase C (PKC), and two PKC isozymes are translocated to different
intracellular sites on activation with alpha 1-adrenergic agonists or
phorbol myristate acetate. Differential intracellular localization upon
activation was compatible with differential function, and we therefore
asked whether PKC isozymes had distinct roles in regulating transcription
of the cardiac myosin heavy chain (MHC) genes. Cardiac myocytes were
transfected with chloramphenicol acetyltransferase reporter plasmids
containing the promoters of the beta-MHC or alpha-MHC isogenes. An alpha
1-adrenergic agonist stimulated the beta-MHC promoter by 3-fold but had no
effect on the alpha-MHC promoter. This pattern of MHC promoter regulation
by an alpha 1 agonist was the same as that found previously for the
endogenous MHC mRNAs in this model system. Myocytes were then
co-transfected with the beta- or alpha-MHC-chloramphenicol
acetyltransferase plasmids and expression plasmids encoding wild-type or
constitutively activated mutants of the alpha- and beta-isozymes of PKC.
Co-transfection with wild-type alpha-PKC or wild-type beta-PKC did not
stimulate the beta- MHC promoter, and none of the expressed PKCs affected
the alpha-MHC promoter. However, the constitutively activated mutant of
beta-PKC stimulated the beta-MHC promoter by 8-fold, whereas stimulation by
the activated alpha-PKC mutant was only 40% as great (3-fold). In contrast,
the constitutively activated alpha-PKC and beta-PKC mutants were equally
potent in stimulating a reporter plasmid containing AP-1 recognition
sequences. All transfected PKCs were expressed equally in the myocytes, as
judged by immunofluorescence. These data indicate that transcription of the
beta-MHC isogene is stimulated preferentially by beta-PKC in cardiac
myocytes and provide direct evidence for differential functions of alpa-PKC
and beta-PKC in transcriptional regulation.
Expression of a constitutively activated mutant of the beta-isozyme of protein kinase C in cardiac myocytes stimulates the promoter of the beta-myosin heavy chain isogene
Division of Cardiology and Research Service, Veterans Affairs Medical Center, San Francisco, California 94121.
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K. Kinugawa, K. Yonekura, R. C.J. Ribeiro, Y. Eto, T. Aoyagi, J. D. Baxter, S. A. Camacho, M. R. Bristow, C. S. Long, and P. C. Simpson Regulation of Thyroid Hormone Receptor Isoforms in Physiological and Pathological Cardiac Hypertrophy Circ. Res., September 28, 2001; 89(7): 591 - 598. [Abstract] [Full Text] [PDF]
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