Effect of phenylephrine on pyruvate dehydrogenase activity in rat hepatocytes and its interaction with insulin and glucagon
Abstract
In isolated rat hepatocytes phenylephrine promotes a rapid increase in the amount of pyruvate dehydrogenase present in its active form (PDHa). This action is mediated by alpha 1-adrenergic receptors and is not observed in Ca2+-depleted hepatocytes. It is mimicked by the Ca2+ ionophore A23187. No changes in metabolites known to affect PDH activity are measured 3 min after addition of phenylephrine. Glucagon also increases PDHa, its action is additive to that of phenylephrine. The action of phenylephrine on PDHa could be explained by an increase in mitochondrial free Ca2+.
References
On the mechanism of irreversible pyruvate dehydrogenase inactivation in liver mitochondrial extracts
Citations
The role of mitochondrial Ca2+ transport and matrix Ca2+ in signal transduction in mammalian tissues
No synergism between ionomycin and phorbol ester in fatty acid synthesis by isolated rat hepatocytes
Related Concepts
Related Feeds
Adrenergic Receptors: Trafficking
Adrenergic receptor trafficking is an active physiological process where adrenergic receptors are relocated from one region of the cell to another or from one type of cell to another. Discover the latest research on adrenergic receptor trafficking here.