Regulation of phosphoenolpyruvate carboxykinase gene transcription in H4IIE hepatoma cells: evidence for a primary role of the catalytic subunit of 3',5'-cyclic adenosine monophosphate-dependent protein kinase - PubMed (original) (raw)

Regulation of phosphoenolpyruvate carboxykinase gene transcription in H4IIE hepatoma cells: evidence for a primary role of the catalytic subunit of 3',5'-cyclic adenosine monophosphate-dependent protein kinase

S J Beebe et al. Mol Endocrinol. 1987 Sep.

Abstract

The purpose of these studies was to determine whether the catalytic subunit of cAMP-dependent protein kinase is involved in the regulation of P-enolpyruvate carboxykinase (PEPCK) gene transcription. Cyclic AMP analog pairs that preferentially stimulate either type I or type II protein kinase in a synergistic manner were used to compare regulation of mRNAPEPCK synthesis in H4IIE rat hepatoma cells with protein kinase activation in vitro. Type II protein kinase is predominant in H4IIE cells and analog pairs directed toward this isozyme resulted in a synergistic increase of mRNAPEPCK that was due to a corresponding enhancement of PEPCK gene transcription. When compared to a single analog the addition of a type II-directed analog pair reduced the total analog concentration required for maximal induction of transcription by about 30-fold. H4IIE cells have a small amount of type I kinase; pairs specific for this form of the enzyme were also effective, but to a lesser extent than those for the type II kinase. (Rp)-cAMPS, a cyclic nucleotide-dependent protein kinase antagonist, inhibited the agonist-induced increase of mRNAPEPCK in a concentration-dependent manner. The results indicate that the activation of PEPCK gene transcription by cAMP in H4IIE cells is mediated by cAMP-dependent protein kinase. Although the type II isozyme is primarily responsible, type I is also effective. These isozymes have identical catalytic subunits, hence this component presumably mediates the cAMP effect.

PubMed Disclaimer

Cited by

Regulation of hepatic glucose production and AMPK by AICAR but not by metformin depends on drug uptake through the equilibrative nucleoside transporter 1 (ENT1).
Logie L, Lees Z, Allwood JW, McDougall G, Beall C, Rena G. Logie L, et al. Diabetes Obes Metab. 2018 Dec;20(12):2748-2758. doi: 10.1111/dom.13455. Epub 2018 Aug 2. Diabetes Obes Metab. 2018. PMID: 29962100 Free PMC article.
Deficient gene expression in protein kinase inhibitor alpha Null mutant mice.
Gangolli EA, Belyamani M, Muchinsky S, Narula A, Burton KA, McKnight GS, Uhler MD, Idzerda RL. Gangolli EA, et al. Mol Cell Biol. 2000 May;20(10):3442-8. doi: 10.1128/MCB.20.10.3442-3448.2000. Mol Cell Biol. 2000. PMID: 10779334 Free PMC article.
Comparison of the effects of insulin and okadaic acid on phosphoenolpyruvate carboxykinase gene expression.
O'Brien RM, Noisin EL, Granner DK. O'Brien RM, et al. Biochem J. 1994 Nov 1;303 ( Pt 3)(Pt 3):737-42. doi: 10.1042/bj3030737. Biochem J. 1994. PMID: 7980440 Free PMC article.
Identification of basal and cyclic AMP regulatory elements in the promoter of the phosphoenolpyruvate carboxykinase gene.
Quinn PG, Wong TW, Magnuson MA, Shabb JB, Granner DK. Quinn PG, et al. Mol Cell Biol. 1988 Aug;8(8):3467-75. doi: 10.1128/mcb.8.8.3467-3475.1988. Mol Cell Biol. 1988. PMID: 2850495 Free PMC article.
Non-histone chromatin proteins in beef thyroid: distinct phosphorylation patterns of several protein kinases.
Levasseur S, Poleck T, Friedman Y, Burke G. Levasseur S, et al. Mol Cell Biochem. 1990 Jun 25;95(2):139-46. doi: 10.1007/BF00219972. Mol Cell Biochem. 1990. PMID: 2164141

Regulation of phosphoenolpyruvate carboxykinase gene transcription in H4IIE hepatoma cells: evidence for a primary role of the catalytic subunit of 3',5'-cyclic adenosine monophosphate-dependent protein kinase - PubMed (original) (raw)