Selective activation of cyclic AMP dependent protein kinase by calcitonin in a calcitonin secreting lung cancer cell line.
The characteristics of the cyclic AMP-dependent protein kinase isoenzyme response to calcitonin have been studied in a calcitonin-secreting human lung cancer cell line (BEN). These cells secrete a high molecular weight calcitonin-like molecule. They have previously been shown to have calcitonin receptors linked to adenylate cyclase. In this study we demonstrate that the cells contain two cyclic AMP-dependent protein kinase iso-enzymes. Using a recently reported method for studying selective activation of these isoenzymes by hormones in intact cells, it is demonstrated that calcitonin causes selective activation of isoenzyme I, with no significant activation of isoenzyme II. Post-extraction activation was excluded by appropriate controls. The response was rapid (2 min) and persisted for 18 hours. Half maximal response occurred at 3 X 10(-10) M salmon calcitonin.
D002116:Calcitonin / Q000378:metabolism / Q000502:physiology*; D002460:Cell Line; D004789:Enzyme Activation; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008175:Lung Neoplasms / Q000378:metabolism*; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*
D007527:Isoenzymes; D002116:Calcitonin; D011494:Protein Kinases