We showed previously that the levels of type I regulatory subunit of cyclic AMP-dependent protein kinase increase during differentiation of L6 skeletal myoblasts as a result of a specific decrease in its rate of degradation. Studies on the rates of degradation of the catalytic subunit show that unlike the type I regulatory subunit, catalytic subunit is degraded very slowly in myoblasts (t1/2 = 29 h) and more rapidly in myotubes (t1/2 = 14 h). As with the regulatory subunit, the degradation of catalytic subunit is increased by treatment of myoblasts with cyclic AMP analogues. These results suggest that the overall increase in the amount of type I cyclic AMP-dependent protein kinase holoenzyme during myogenesis is due to the increase in levels of mRNA for the catalytic subunit. This probably leads to an increase in the amount of catalytic subunit, which then stabilizes the regulatory subunit, thereby causing an increase in the levels of this protein also.
Research Article|November 15 1989
Regulation of cyclic AMP-dependent protein kinase levels during skeletal myogenesis
I A J Lorimer;
Biochem J (1989) 264 (1): 305-308.
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I A J Lorimer, B D Sanwal; Regulation of cyclic AMP-dependent protein kinase levels during skeletal myogenesis. Biochem J 15 November 1989; 264 (1): 305–308. doi: https://doi.org/10.1042/bj2640305
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