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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Cyclic AMP-dependent phosphorylation in the control of biotransformation in the liver.

The possibility of a short-term cAMP-dependent regulation of mixed-function oxidation and of glucuronide formation was investigated in isolated mouse hepatocytes and in mouse liver microsomal membranes. N6, O2-dibutyryl cAMP (in accordance with its increasing effect on gluconeogenesis) decreased aminopyrine oxidation and p-nitrophenol conjugation in isolated hepatocytes, while the phenolphthalein conjugation remained unaltered. Similar to dibutyryl cAMP the Ca2+ ionophore A 23187 also decreased aminopyrine oxidation. In cell-free systems the phosphorylation of isolated microsomal membranes by the exogenous cAMP-dependent protein kinase was inhibitory on aminopyrine oxidation and p-nitrophenol glucuronide formation but aniline oxidation and phenolphthalein glucuronidation were not affected. The correlation between the negative cAMP-dependent control of certain processes of biotransformation and the positive cAMP-dependent regulation of gluconeogenesis is discussed.[1]


  1. Cyclic AMP-dependent phosphorylation in the control of biotransformation in the liver. Bánhegyi, G., Garzó, T., Mészáros, G., Faragó, A., Antoni, F., Mandl, J. Biochem. Pharmacol. (1988) [Pubmed]
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