• 1 January 1978
    • journal article
    • research article
    • Vol. 4  (5) , 359-374
Abstract
ACTH at levels as low as 0.05 mU[units]/ml stimulated lipolysis, protein kinase and cyclic AMP accumulation in isolated fat cells from fed and fasted rats. Changes in cyclic AMP levels and in the protein kinase activity ratio were well correlated temporally. The protein kinase activity ratio was potentiated by adenosine deaminase. A sudden increase or decrease in either ACTH or dibutyryl cyclic AMP concentration was associated with a rapid and corresponding change in the rate of glycerol production. With ACTH, the changes in glycerol production were accompanied by appropriate changes in cyclic AMP levels. Actinomycin-D (10 .mu.M) did not affect lipolysis or cyclic AMP accumulation activated by ACTH in fat cells.