Insulin-induced phosphorylation and activation of phosphodiesterase 3B in rat adipocytes: possible role for protein kinase B but not mitogen-activated protein kinase or p70 S6 kinase.
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Summary
Results suggest that p70 S6 kinase and MAP kinases are not involved in the insulin-induced phosphorylation/activation of PDE 3B in rat adipocytes, and that PKB is consistent with PKB being the kinase that phosphorylates PDE3B.
- Type
- article
- Published
- 1998-01-01
- Cited by
- 35
- References
- 46
- Access
- Open access
- OpenAlex
- https://openalex.org/W2025654952
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:32495367
Keywords
P70-S6 Kinase 1, Mitogen-activated protein kinase kinase, MAPK14, MAP2K7, MAP kinase kinase kinase
References
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- cAMP-dependent protein kinase and lipolysis in rat adipocytes. III. Multiple modes of insulin regulation of lipolysis and regulation of insulin responses by adenylate cyclase regulators.
- Does mitogen-activated-protein kinase have a role in insulin action? The cases for and against.
- Essential role of phosphatidylinositol 3-kinase in insulin-induced glucose transport and antilipolysis in rat adipocytes. Studies with a selective inhibitor wortmannin.
- Discriminative insulin antagonism of stimulatory effects of various cAMP analogs on adipocyte lipolysis and hepatocyte glycogenolysis.
- Insulin activates myelin basic protein (p42 MAP) kinase by a protein kinase C‐independent pathway in rat adipocytes
- Activation of ribosomal protein S6 kinases does not increase glycogen synthesis or glucose transport in rat adipocytes.
- Multiple signalling pathways involved in the stimulation of fatty acid and glycogen synthesis by insulin in rat epididymal fat cells.
- Identification of the Site in the cGMP-inhibited Phosphodiesterase Phosphorylated in Adipocytes in Response to Insulin and Isoproterenol (*)
- Identification of the phosphorylation site in vitro for cAMP-dependent protein kinase on the rat adipocyte cGMP-inhibited cAMP phosphodiesterase.
- The Metabolism of Isolated Fat Cells: I. Effects of Hormones on Glucose Metabolism and Lipolysis
- Potential Role of Protein Kinase B in Glucose Transporter 4 Translocation in Adipocytes.
- Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B.
- A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel.
- Expression of a Constitutively Active Akt Ser/Thr Kinase in 3T3-L1 Adipocytes Stimulates Glucose Uptake and Glucose Transporter 4 Translocation*
- Pervanadate [peroxide(s) of vanadate] mimics insulin action in rat adipocytes via activation of the insulin receptor tyrosine kinase.
- A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region.
- Increasing cAMP attenuates activation of mitogen-activated protein kinase.
Cited by
- Cell-permeable ceramides increase basal glucose incorporation into triacylglycerols but decrease the stimulation by insulin in 3T3-L1 adipocytes
- Early-life programming of susceptibility to dysregulation of glucose metabolism and the development of Type 2 diabetes mellitus.
- Pharmacological modulation of insulin resistance : benefits and harms
- Chronic hormonal control of lipid synthesis and hydrolysis in adipocytes
- Cyclic Nucleotide Phosphodiesterases (PDEs): Diverse Regulators of Cyclic Nucleotide Signals and Inviting Molecular Targets for Novel Therapeutic Agents
- Studies in beta cells and adipocytes in the context of obesity and T2D - focusing on PDE3B, OPN and SCFAs
- Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB.
- Multisite phosphorylation of adipocyte and hepatocyte phosphodiesterase 3B.
- AMPK activation—protean potential for boosting healthspan
- Actions and interactions of AMPK with insulin, the peroxisomal-proliferator activated receptors and sirtuins
- Activation of protein kinase B/cAkt in hepatocytes is sufficient for the induction of expression of the gene encoding glucokinase.
- Phosphodiesterases and cyclic nucleotide signaling in endocrine cells.
- PKB/AKT is involved in resumption of meiosis in mouse oocytes
- The role of cyclic nucleotide phosphodiesterases in the regulation of adipocyte lipolysis Published, JLR Papers in Press, December 16, 2004. DOI 10.1194/jlr.M400362-JLR200
- AKAP signaling complexes: getting to the heart of the matter.
- Insulin-induced formation of macromolecular complexes involved in activation of cyclic nucleotide phosphodiesterase 3B (PDE3B) and its interaction with PKB.
- Signalling pathways involved in insulin cardioprotection : are they comparable in normoxic perfused isolated rat heart vs. ischaemia/reperfusion model?
- C(2)-ceramide influences the expression and insulin-mediated regulation of cyclic nucleotide phosphodiesterase 3B and lipolysis in 3T3-L1 adipocytes.
- Modulation of myocellular fat stores: lipid droplet dynamics in health and disease.
- Differential regulation of adipocyte PDE3B in distinct membrane compartments by insulin and the β3-adrenergic receptor agonist CL316243: effects of caveolin-1 knockdown on formation/maintenance of macromolecular signalling complexes
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