This review summarizes the fundamental roles of protein phosphorylation in regulating cardiac and vascular smooth muscle function, highlighting key mechanisms like calcium transport and energy metabolism.
Underscores cardiac-vascular knowledge gaps; leaves open targeted arterial smooth muscle phosphorylation research.
In the heart and arterial smooth muscles, several proteins are phosphorylated. This review summarizes our current knowledge about these phosphoproteins and their possible role in the function of these muscles. In the contractile apparatus, the phosphorylation of myosin light chain seems to be an integral part of the contraction cycle of arterial smooth muscle. However, in the heart the relationship between light chain phosphorylation-dehosphorylation and systolic-diastolic states remains open. In the heart, the phosphorylation of the inhibitory subunit of troponin, a myofibrillar protein, parallels the positive inotropic response induced by beta-adrenergic agonists. It seems likely that this phosphorylation is involved in the physiological stimulation of the heart by epinephrine. Cardiac sarcoplasmic reticulum contains a low-molecular-weight protein, phospholamban, the phosphorylation of which is required for Ca2+ transport. Ion fluxes through the heart sarcolemma may also be controlled through membrane protein phosphorylation. Key enzymes of the energy-yielding pathways in the heart, the pyruvate dehydrogenase multienzyme complex and phosphorylase, are turned on and off by phosphorylation-dephosphorylation mechanisms. Our understanding of protein phosphorylation in the heart has advanced greatly. In contrast, with the exception of the myosin light chain, much less is known about the many proteins phosphorylated in arterial smooth muscle.
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Bárány et al. (1981) studied this question.
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