cAMP mediated proteolysis of the catalytic subunit of cAMP-dependent protein kinase.
The cAMP-dependent protein kinase from LLC-PK1 cells can be activated in vivo by calcitonin and vasopressin, or forskolin. Continuous treatment of cells with these agents results in a decrease of total cAMP-PK activity. The loss of kinase activity was enhanced when either of these three agents was incubated in the presence of isobutylmethylxanthine. Results obtained using affinity purified antibodies to the catalytic subunit show that the loss of kinase was due to specific proteolysis of this subunit.
Hemmings
B A
BA
D015056:1-Methyl-3-isobutylxanthine / Q000494:pharmacology; D000818:Animals; D002116:Calcitonin / Q000494:pharmacology; D002460:Cell Line; D000242:Cyclic AMP / Q000494:pharmacology*; D004848:Epithelium; D007122:Immunoelectrophoresis; D011494:Protein Kinases / Q000276:immunology / Q000378:metabolism*; D013552:Swine
D002116:Calcitonin; D000242:Cyclic AMP; D011494:Protein Kinases; D015056:1-Methyl-3-isobutylxanthine