Thesis (Ph.D.), University of Manchester, Faculty of Medicine.
|Contributions||University of Manchester. Faculty of Medicine.|
|The Physical Object|
|Number of Pages||177|
Title: Insulin Regulation of PEPCK Gene Expression: A Model for Rapid and Reversible Modulation VOLUME: 5 ISSUE: 4 Author(s):P. G. Quinn and D. Yeagley Affiliation:The Pennsylvania State University College of Medicine, Department of Cellular and MolecularPhysiology, Rm C, University Drive, H, Hershey, PA , USA. Keywords:hyperinsulinemia, chromatin condensation, cAMP Cited by: Sutherland C, O’Brien RM, Granner DK. Phosphatidylinositol 3-kinase but not p70/p85 ribosomal S6 protein kinase is required for the regulation of phosphoenolpyruvate carboxykinase (PEPCK) gene expression by insulin Dissociation of signaling pathways for insulin and phorbol ester regulation of PEPCK gene expression. J Biol Chem ; This inhibitory effect of insulin or phorbol esters on PEPCK gene expression was accompanied by an increase in the rate of transcription and mRNA content of nuclear factors such as c-fos and c-myc. Epidermal growth factor inhibits ~~os~hu~~ul~y~uvat~ carboxykinase gene expression in rat hepatocytes in primary culture Cristina Fillat, Alfons Valera and Fatima Bosch Department of Biochemistry and Molecular Biology, School of Veterinary Medicine, Autonomous University of Barcelona, ~~~9~-~e~~ateY~a, ~~rce~o~a, Spain.
Schubart UK () Regulation of gene expression in rat hepatocytes and hepatoma cells by insulin: quantitation of messenger ribonucleic acid’s coding for tyrosine aminotransferase, tryptophan oxygenase, and phosphoenolpyruvate carboxykinase. Endocrinology – PubMed . Glucose decreases hormone-activated PEPCK gene expression in primary hepatocytes and Fao hepatoma cells, but fails to regulate PEPCK in H4IIE cells (9, 12). This difference in the ability of glucose to regulate PEPCK gene expression may reflect the intrinsic glucose phosphorylating capacity in . In addition, PI3-kinase was implicated in the insulin down-regulation of gene expression for the PEPCK, G6Pase and IGFBP-1 genes (Band and Posner ; Dickens et al. ; Mounier et al. ; Sutherland et al. , ). Our observations are in agreement with the fact that activation of a PI3-kinase dependent pathway is the major route. For example, ERK1/2 and PKB/Akt, components activated upon insulin stimulation, can be activated by hepatic growth factor and epidermal growth factor treatments in rat primary hepatocytes. This observation provides another mechanism for the modulation of insulin-regulated gene expression. Moreover, the activities of transcription complex on.
The expression of IGF-binding protein-1 (IGFBP-1) is induced in rat liver by dexamethasone and glucagon and is completely inhibited by n m insulin. Various studies have implicated phosphatidylinositol 3-kinase, protein kinase B (Akt), phosphorylation of the transcription factors forkhead in rhabdomyosarcoma 1 (Foxo1)/Foxo3, and the mammalian target of rapamycin (mTOR) in insulin’s . Abstract. Insulin is a key hormone that controls glucose homeostasis. In liver, insulin suppresses gluconeogenesis by inhibiting the transcriptions of phosphoenolpyruvate carboxylase (PEPCK) and glucosephosphatase (G6Pase) insulin resistance and type II diabetes there is an elevation of hepatic gluconeogenesis, which contributes to hyperglycemia. Accordingly, the aim of this work was to investigate, firstly, the initial induction of PEPCK gene expression by cAMP and the regulatory effect of insulin or phorbol esters on PEPCK gene expression. Secondly, the role of nuclear factors such as C/ EBPoc, c-fos and c-myc in the regulation of PEPCK gene expression in fetal hepatocytes was. Patel S, Lochhead PA, Rena G, Fumagalli S, Pende M, Kozma SC, Thomas G, Sutherland C. Insulin regulation of insulin-like growth factor-binding protein-1 gene expression is dependent on the mammalian target of rapamycin, but independent of ribosomal S6 kinase activity. J. Biol. Chem.