Activation of the phosphoenolpyruvate carboxykinase gene retinoic acid response element is dependent on a retinoic acid receptor/coregulator complex.

Hall, Robert K.; Scott, Donald K.; Noisin, E L; Lucas, Peter C.; Granner, Daryl K.

doi:10.1128/mcb.12.12.5527

Cited by 90 publications

(98 citation statements)

References 50 publications

(59 reference statements)

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“…We have inspected the nucleic acid sequence of MAPT (83) and determined that it contains a RAR response element, TGAACxxTGAAC (84), beginning at 5Ј Ϫ16. There are four different TGACC motifs throughout the gene, which also may confer retinoid responsivity (85,86). We suggest that the transcriptional activation of these elements may be modified by variants of one or another of the RARs.…”

Section: Functions In Ad Of Retinoid-related Genesmentioning

confidence: 91%

Evidence for defective retinoid transport and function in late onset Alzheimer's disease

Goodman¹,

Pardee²

2003

Proc. Natl. Acad. Sci. U.S.A.

163

124

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The hypothesis of this article is that late onset Alzheimer's disease (AD) is influenced by the availability in brain of retinoic acid (RA), the final product of the vitamin A (retinoid) metabolic cascade. Genetic, metabolic, and environmental͞dietary evidence is cited supporting this hypothesis. Significant genetic linkages to AD are demonstrated for markers close to four of the six RA receptors, RA receptor G at 12q13, retinoid X receptor B at 6p21.3, retinoid X receptor G at 1q21, and RA receptor A at 17q21. Three of the four retinol-binding proteins at 3q23 and 10q23 and the RA-degrading cytochrome P450 enzymes at 10q23 and 2p13 map to AD linkages. Synthesis of the evidence supports retinoid hypofunction and impaired transport as contributing factors. These findings suggest testable experiments to determine whether increasing the availability of retinoid in brain, possibly through pharmacologic targeting of the RA receptors and the cytochrome P450 RAinactivating enzymes, can prevent or decrease amyloid plaque formation.

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Section: Functions In Ad Of Retinoid-related Genesmentioning

confidence: 91%

Evidence for defective retinoid transport and function in late onset Alzheimer's disease

Goodman¹,

Pardee²

2003

Proc. Natl. Acad. Sci. U.S.A.

163

124

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“…Like C/EBPa, C/EBP/J does not therefore activate transcription through all the sites to which it binds [112]. HNF-1 binds to the P2 element [107] and HNF-4 to the P6 element [113]. While both P1 and P6 positively regulate the PEPCK promoter, the individual functions of HNF-1 and HNF-4 were not investigated.…”

Section: Tissue-specific Controlmentioning

confidence: 99%

Transcriptional control of genes that regulate glycolysis and gluconeogenesis in adult liver

Lemaigre¹,

Rousseau²

1994

Biochemical Journal

100

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“…The culture of HL1C cells and the assay for measurement of CAT activity have been described (16,17).…”

Section: Methodsmentioning

confidence: 99%

c-Myc Is Required for the Glucose-mediated Induction of Metabolic Enzyme Genes

Collier

Doan²,

Daniels³

et al. 2003

Journal of Biological Chemistry

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Glucose exerts powerful effects on hepatocyte gene transcription by mechanisms that are incompletely understood. c-Myc regulates hepatic glucose metabolism by increasing glycolytic enzyme gene transcription while concomitantly decreasing gluconeogenic and ketogenic enzyme gene expression. However, the molecular mechanisms by which c-Myc exerts these effects is not known. In this study, the glucose-mediated induction of L-type pyruvate kinase and glucose-6-phosphatase mRNA levels was diminished by maneuvers involving recombinant adenoviral vectors that interfere with (i) c-Myc protein levels by antisense expression or (ii) c-Myc function through a dominant-negative Max protein. These results were obtained using both HL1C rat hepatoma cells and primary rat hepatocytes. Furthermore, a decrease in c-Myc abundance reduced glucose production in HL1C cells, presumably by decreasing glucose-6-phosphatase activity. The repression of hormone-activated phosphoenolpyruvate carboxykinase gene transcription by glucose was not affected by a reduction in c-Myc levels. The basal mRNA levels for Lpyruvate kinase and glucose-6-phosphatase were not altered to any significant degree by adenoviral treatment. Furthermore, adenoviral overexpression of the c-Myc protein induced glucose-6-phosphatase mRNA in the absence of glucose stimulation. We conclude that multiple mechanisms exist to communicate the glucose-derived signal and that c-Myc has a key role in the hepatic glucose signaling pathway.Insulin and glucose act jointly to influence glucose homeostasis by altering hepatic gene expression patterns. Insulin increases glucokinase (GK) 1 gene transcription and protein levels in hepatocytes (1). The phosphorylation of glucose by GK leads to increased glucose flux and metabolism, generating signaling metabolites that modify the gene expression profile of the liver (2). For example, the L-pyruvate kinase (L-PK) and glucose-6-phosphatase (Glc-6-Pase) genes (encoding key glycolytic and gluconeogenic enzymes, respectively) are stimulated by increases in hepatic glucose metabolism (3-5). Conversely, glucose metabolism can also negatively regulate gene transcription, exemplified by the repression of hormone-activated phosphoenolpyruvate carboxykinase (PEPCK) gene promoter activity (6, 7). Although glucose metabolism modulates the gene expression patterns of key glycolytic and gluconeogenic enzymes, the signaling mechanisms and coordinating transcription factors involved are not fully characterized.One transcription factor that is a candidate for establishing hepatic glucose-dependent gene expression patterns is the basic, helix-loop-helix leucine-zipper (bHLH-LZ) transcription factor c-Myc (8, 9). The Myc family of proteins (e.g. c-, N-, L-Myc, USF, Max, Mad, etc.) participates in control of proliferation, growth, differentiation, apoptosis, and metabolism (10, 11). c-Myc binds DNA by interacting with the E box sequence CACGTG (and other related non-canonical sites) as a heterodimer with Max, another bHLH-LZ protein. The Myc/Max heterodimer ...

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Activation of the phosphoenolpyruvate carboxykinase gene retinoic acid response element is dependent on a retinoic acid receptor/coregulator complex.

Cited by 90 publications

References 50 publications

Evidence for defective retinoid transport and function in late onset Alzheimer's disease

Evidence for defective retinoid transport and function in late onset Alzheimer's disease

Transcriptional control of genes that regulate glycolysis and gluconeogenesis in adult liver

c-Myc Is Required for the Glucose-mediated Induction of Metabolic Enzyme Genes

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