Activation of the particulate low K sub(m) phosphodiesterase of adipocytes by addition of cAMP-dependent protein kinase

The purified catalytic subunit (C) of cAMP-dependent protein kinase produced a 2-fold activation of the low K sub(m) phosphodiesterase in crude microsomes (P-2 pellet) or rat adipocytes. The present findings are consistent with the suggestion that protein kinase regulates the concentration of cAMP t...

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Bibliographic Details
Published in:The Journal of biological chemistry 1988-01, Vol.263 (21), p.10359-10363
Main Authors: Gettys, T W, Vine, A J, Simonds, M F, Corbin, J D
Format: Article
Language:English
Subjects:
3',5'-cyclic-nucleotide phosphodiesterase
adipocytes
microsomes
protein kinase
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Summary:The purified catalytic subunit (C) of cAMP-dependent protein kinase produced a 2-fold activation of the low K sub(m) phosphodiesterase in crude microsomes (P-2 pellet) or rat adipocytes. The present findings are consistent with the suggestion that protein kinase regulates the concentration of cAMP through phosphodiesterase activation and provide direct evidence that the mechanism of activation involves phosphorylation.
ISSN:0021-9258