Insulin controls the cyclic AMP‐dependent phosphorylation of integral and peripheral proteins associated with the rat liver plasma membrane

Marchmont, Robert J.; Houslay, Miles D.

doi:10.1016/0014-5793(80)81209-9

Cited by 27 publications

(11 citation statements)

References 29 publications

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“…PDE activity was determined by a modification of the two‐step procedure of Thompson & Appleman (1971) as described previously by us ( Marchmont & Houslay, 1980 ). All assays were conducted at 30°C with initial rates taken from linear time‐courses.…”

Section: Methodsmentioning

confidence: 99%

Sub‐family selective actions in the ability of Erk2 MAP kinase to phosphorylate and regulate the activity of PDE4 cyclic AMP‐specific phosphodiesterases

Baillie

Mackenzie

McPhee

et al. 2000

British J Pharmacology

153

112

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1 Expressed in intact cells and in vitro, PDE4B and PDE4C isoenzymes of cyclic nucleotide phosphodiesterase (PDE), in common with PDE4D isoenzymes, are shown to provide substrates for C-terminal catalytic unit phosphorylation by the extracellular signal-regulated kinase Erk2 (p42 MAPK ). 2 In contrast, PDE4A isoenzymes do not provide substrates for C-terminal catalytic unit phosphorylation by Erk2. 3 Mutant PDE4 enzymes were generated to show that Erk2 phosphorylation occurs at a single, cognate serine residue located within the C-terminal portion of the PDE4 catalytic unit. 4 PDE4 long-form isoenzymes were markedly inhibited by Erk2 phosphorylation. 5 The short-form PDE4B2 isoenzyme was activated by Erk2 phosphorylation. 6 These functional changes in PDE activity were mimicked by mutation of the target serine for Erk2 phosphorylation to the negatively charged amino acid, aspartic acid. 7 Epidermal growth factor (EGF) challenge caused diametrically opposed changes in cyclic AMP levels in COS1 cells transfected to express the long PDE4B1 isoenzyme compared to cells expressing the short PDE4B2 isoenzyme. 8 We suggest that PDE4 enzymes may provide a pivotal point for integrating cyclic AMP and Erk signal transduction in cells with 4 genes encoding enzymes that are either insensitive to Erk2 action or may either be activated or inhibited. This indicates that PDE4 isoenzymes have distinct functional roles, giving credence to the notion that distinct therapeutic bene®ts may accrue using either PDE4 subfamily or isoenzyme-selective inhibitors.

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Section: Methodsmentioning

confidence: 99%

Sub‐family selective actions in the ability of Erk2 MAP kinase to phosphorylate and regulate the activity of PDE4 cyclic AMP‐specific phosphodiesterases

Baillie

Mackenzie

McPhee

et al. 2000

British J Pharmacology

153

112

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“…Cyclic AMP was measured from cells after isoproterenol stimulation using a colorimetric enzyme immunoassay kit (Cayman Chemicals; number 581001). The PDE assay was performed as described previously (37). PDE inhibitor IBMX was added at final concentrations of 0.5 mM before the reaction.…”

Section: Methodsmentioning

confidence: 99%

Ablation of Calcineurin Aβ Reveals Hyperlipidemia and Signaling Cross-talks with Phosphodiesterases

Suk

Zhou

Yang

et al. 2013

Journal of Biological Chemistry

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Background: Transplant patients treated with cyclosporine A, an inhibitor of calcineurin, frequently develop metabolic complications. Results: Mice lacking calcineurin A␤ develop metabolic complications. A cell autonomous mechanism with altered cAMP-PKA signaling is found. Conclusion: Calcineurin plays a role in metabolism via regulating phosphodiesterases. Significance: Potentiated cAMP signaling provides an alternative mechanism for the metabolic complications in transplant patients.

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“…Membranes were always rapidly frozen in liquid N2 and stored therein at a concentration of 10mg of protein/ml in 1 mM-KHCO3, pH 7.4. Washed high-salt-treatedplasma membranes Plasma membranes were treated with 0.4 M-NaCl under conditions described in detail previously (Marchmont & Houslay, 1980a) in order to remove peripheral proteins (Marchmont & Houslay, 1980d). …”

Section: Methodsmentioning

confidence: 99%

The insulin-stimulated cyclic AMP phosphodiesterase binds to a single class of protein sites on the liver plasma membrane

Houslay¹,

Marchmont²

1981

Biochemical Journal

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The peripheral cyclic AMP phosphodiesterase from rat liver plasma membranes binds with high affinity (2.4 nM) to a single class of receptor sites on the liver plasma membrane. These receptor sites appear to be proteins, as they are trypsin-and heat-labile. The sensitivity of these sites to denaturation by trypsin and heat is a first-order process. The presence of Ca2+ (5 mM) increases the affinity of these sites for the enzyme, but does not alter their total number. The receptor sites and the cyclic AMP phosphodiesterase occur in similar numbers, at around 2 pmol/mg of plasma-membrane protein. It is proposed that the peripheral, liver plasma-membrane cyclic AMP phosphodiesterase is attached to a specific site on the insulin receptor and that the binding of insulin to the receptor site triggers a conformational change in the enzyme such that the enzyme can be phosphorylated and activated by an endogenous cyclic AMP-dependent protein kinase.

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Insulin controls the cyclic AMP‐dependent phosphorylation of integral and peripheral proteins associated with the rat liver plasma membrane

Cited by 27 publications

References 29 publications

Sub‐family selective actions in the ability of Erk2 MAP kinase to phosphorylate and regulate the activity of PDE4 cyclic AMP‐specific phosphodiesterases

Sub‐family selective actions in the ability of Erk2 MAP kinase to phosphorylate and regulate the activity of PDE4 cyclic AMP‐specific phosphodiesterases

Ablation of Calcineurin Aβ Reveals Hyperlipidemia and Signaling Cross-talks with Phosphodiesterases

The insulin-stimulated cyclic AMP phosphodiesterase binds to a single class of protein sites on the liver plasma membrane

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