A ~50 kD membrane-associated protein in guinea pig cardiac sarcolemmae is phosphorylated by cGMP-dependent protein kinase, suggesting a possible mechanism for cGMP-mediated control of cardiac function.
Does not support changes in clinical care; leaves open the functional role of cGMP-dependent phosphorylation in cardiac membranes.
Cardiac sarcolemmae from guinea pig ventricles were purified and incubated with cGMP-dependent protein kinase. In the presence of the purified kinase plus 10(-5) M cGMP or 8-Br-cGMP, a protein of approximately 50 kD, (Kilodalton) was phosphorylated. This membrane-associated cGMP-dependent protein kinase substrate is similar in MW to the regulatory subunit of the cAMP-dependent protein kinase, which is known to be a substrate for the cGMP-dependent protein kinase. Thus, this substrate, the identity of which remains to be proven, may be a possible mediator of cGMP-mediated control of cardiac function.
No takes yet. Share an insight, caveat, or question.
Cuppoletti et al. (1987) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: