Activation of microsomal cAMP-dependent protein kinase isoenzyme I by ACTH1-24 in bovine adrenal cells.
In microsomes of bovine fasciculata reticularis cells incubated with or without 10(-8) M ACTH during 20 min, we measured covalent and non covalent cAMP binding under exchange or non-exchange conditions and cAMP-kinase activity. ACTH induced a decrease in cAMP-kinase activity and in the number of free cAMP binding sites. These results indicate an activation by ACTH of a part of microsomal cAMP-dependent protein kinase. Photoaffinity labeling of microsomal protein with 8-azido-cAMP revealed the presence of both cAMP-kinase isoenzyme I and II in this cellular fraction. Using this method, it was demonstrated that ACTH1-24 caused a preferential and nearly complete activation of microsomal protein kinase I.
Deviller
P
P
Vallier
P
P
Saez
J M
JM
D000311:Adrenal Glands / Q000166:cytology / Q000201:enzymology*; D000324:Adrenocorticotropic Hormone / Q000031:analogs & derivatives*; D000818:Animals; D002417:Cattle; D003366:Cosyntropin / Q000494:pharmacology*; D004789:Enzyme Activation; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology*; D011494:Protein Kinases / Q000378:metabolism*
D007527:Isoenzymes; D003366:Cosyntropin; D000324:Adrenocorticotropic Hormone; D011494:Protein Kinases