Serum modification of cyclic nucleotide phosphodiesterase forms independent of protein synthesis

doi:10.1016/0006-291X(76)91108-6

Biochemical and Biophysical Research Communications

Volume 70, Issue 1, 3 May 1976, Pages 58-65

https://doi.org/10.1016/0006-291X(76)91108-6 Get rights and content

Abstract

Addition of 10% fetal calf serum to BHK cells made quiescent by maintenance for 48 hours in sub-optimal serum (0.5%) caused rapid changes in cyclic AMP phosphodiesterase activity (increased maximum velocity and affinity) even in the presence of inhibitors of protein synthesis. Activity changes were associated with an alteration in the number of forms of cyclic AMP phosphodiesterase identified by Agarose gel filtration. Three forms of cyclic nucleotide phosphodiesterase were apparent after serum addition whereas only two forms were resolved in quiescent BHK cells. The initial rapid increase in cyclic AMP phosphodiesterase activity seen when serum was added to quiescent cells was followed temporally by a much slower increase in cyclic AMP phosphodiesterase activity that could be prevented by cycloheximide or actinomycin D.

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Insulin produced a 10-fold activation of cAMP phosphodiesterase activity and a 3-fold reduction in cAMP content in serum-deprived, growth-arrested BHK fibroblasts. Insulin did not promote growth of these cells, as judged by measurement of cell number, but it did promote reentry of cells into the cell cycle and progression into S phase, as determined by rates of macromolecular synthesis, and autoradiographic and microfluorometric analyses. Insulin stimulation of macromolecular synthesis can be blocked by the addition of a phosphodiesterase inhibitor, suggesting that these effects of insulin on the cell cycle may be mediated through its activation of cAMP phosphodiesterase.
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In agreement with other workers, exposure of isolated rat fat cells to insulin shows a dose dependent increase in cyclic AMP phosphodiesterase (PDE) activity. However, when fat cells are pre-exposed to either guinea pig antiserum against insulin, rabbit antiserum against glutathione-insulin transhydrogenase (GIT), or immunogamma globulin against GIT, each antibody preparation totally or almost totally abolished the insulin-dependent increase in PDE activity. In control experiments, appropriate normal (non-immune) sera, normal gamma globulin, or the GIT-antiserum or the GIT-immunogamma globulin which had been previously neutralized with purified rat liver GIT were found to be completely ineffective in abolishing the insulin-dependent PDE activity of fat cells. These results suggest that the GIT-catalyzed sulfhydryl-disulfide inter-change reaction with insulin might be part of the mechanism by which insulin regulates the intracellular cyclic AMP concentration.
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Serum modification of cyclic nucleotide phosphodiesterase forms independent of protein synthesis

Abstract

J. Biol. Chem

J. Biol. Chem

J. Biol. Chem

J. Biol. Chem

Biochem. Biophys. Res. Commun

Biochim et Biophys. Acta

J. Biol. Chem

Biochem. Biophys. Res. Commun

J. Biol. Chem

Arch. Biochem. Biophys

Metabolism

J. Biol. Chem

Biochem. Biophys. Res. Commun

J. Biol. Chem

J. Clin. Invest

Science

Biochemistry

J. Neurochem

Molec. Pharmacol