Cyclic nucleotide-dependent phosphorylation of endogenous proteins in bovine adrenocortical cell membranes.
Activation of one or more cyclic AMP-dependent protein kinases has been suggested as an intermediate step in ACTH-stimulated adrenal cell steroidogenesis. Phosphorylation of a number of proteins from different subcellular fractions has been reported but those phosphorylation events which are relevant to the steroidogenic process have not yet been identified. In this paper we report that plasma membrane enriched fractions from bovine adrenal cortex retain the ability to phosphorylate endogenous membrane proteins and that phosphorylation of these acceptors is markedly enhanced by cyclic AMP or, to a lesser extent, by cyclic GMP. Cyclic nucleotide-dependent phosphorylation was most marked in protein acceptors of 191 000, 148 000, 138 000, 107 000, 65 000, 60 000 and 27 000 daltons. Cyclic nucleotide stimulation of phosphorylation was rapid (within 10 s), and is consistent with the rapid onset of ACTH-stimulated steroidogenesis.
D000302:Adrenal Cortex / Q000201:enzymology*; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002417:Cattle; D002462:Cell Membrane / Q000201:enzymology; D000242:Cyclic AMP / Q000494:pharmacology; D006152:Cyclic GMP / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D004789:Enzyme Activation; D008565:Membrane Proteins / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology; D008970:Molecular Weight; D009712:Nucleotides, Cyclic / Q000494:pharmacology*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*
D008565:Membrane Proteins; D009712:Nucleotides, Cyclic; D000242:Cyclic AMP; D011494:Protein Kinases; D006152:Cyclic GMP; D002118:Calcium