Cloning and characterization of the 5′ end and promoter region of the chicken acetyl-CoA carboxylase gene

Mounier, Cathérine; Fur, Nathalie Le; Powell, Rohan S.; Diot, Christian; Langlois, Patrick; Mallard, J.; Douaire, Madeleine

doi:10.1042/bj3140613

Cited by 15 publications

(9 citation statements)

References 52 publications

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“…Sequences corresponding to E4 are well conserved from chicken to man and alternative exon splicing of E4 has been demonstrated in a number of species , Ha et al 1994, Barber & Travers 1995. In contrast to our findings in ovine adipose tissue, in which transcripts that lack E4 predominate, the majority of ACC-transcripts in rat tissues, including adipose tissue (LopezCasillas et al 1991) and in chicken liver appear to include E4 (El Khadir-Mounier et al 1996). Thus, the significance of transcript heterogeneity due to the inclusion or exclusion of E4 in ACC-mRNA is unclear at present and remains to be determined.…”

Section: Discussioncontrasting

confidence: 55%

Insulin-glucocorticoid interactions in the regulation of acetyl-CoA carboxylase-alpha transcript diversity in ovine adipose tissue

Travers

Barber²

1999

Journal of Molecular Endocrinology

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Transcription of the acetyl-CoA carboxylase (ACC)-gene is initiated from two promoters, promoter I (PI) and promoter II (PII) types when compared with explants prior to culture. PII transcripts, by contrast, were increased 2-fold by culture in insulin plus dexamethasone and this was entirely attributed to an increase in the expression of the E[2/4/5] type. Dexamethasone acts to potentiate the action of insulin on PI and PII transcript abundance and this effect is greatest for PI transcripts. This study has demonstrated that repression of the ACC-gene in adipose tissue during lactation is largely achieved through attenuation of PI transcript abundance and may be related, in part, to a change in the sensitivity of the apparatus that regulates PI transcript steady-state levels to insulin.

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Section: Discussioncontrasting

confidence: 55%

Insulin-glucocorticoid interactions in the regulation of acetyl-CoA carboxylase-alpha transcript diversity in ovine adipose tissue

Travers

Barber²

1999

Journal of Molecular Endocrinology

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“…However, no complete structures of the genes for any of the mammalian biotin carboxylases have yet been published. Only two studies have reported the isolation of the 5Ј non-coding exons of rat and chicken acetyl-CoA carboxylase genes (28,29), thus limiting the comparison of our data for genomic structures to those enzymes.…”

Section: Organization Of the Coding Exons-mentioning

confidence: 94%

The Rat Pyruvate Carboxylase Gene Structure

Jitrapakdee¹,

Booker²,

Cassady³

et al. 1997

Journal of Biological Chemistry

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“…The sequence of the primers used to generate the Ϫ1500 to Ϫ855 bp fragment was derived from the published ACC␣ promoter 2 sequence (38). ACC␣ DNA fragments used to construct reporter plasmids were named by designating the 5Ј-and 3Ј-ends of each fragment relative to the transcription start site.…”

Section: Methodsmentioning

confidence: 99%

Thyroid Hormone Stimulates Acetyl-CoA Carboxylase-α Transcription in Hepatocytes by Modulating the Composition of Nuclear Receptor Complexes Bound to a Thyroid Hormone Response Element

Zhang

Yin

Hillgartner

2001

Journal of Biological Chemistry

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Triiodothyronine (T3) stimulates a 7-fold increase in transcription of the acetyl-CoA carboxylase-␣ (ACC␣) gene in chick embryo hepatocytes. Here, we characterized an ACC␣ T3 response element (ACC␣-T3RE) with unique functional and protein binding properties. ACC␣-T3RE activated transcription both in the absence and presence of T3, with a greater activation observed in the presence of T3. In nuclear extracts from hepatocytes incubated in the absence of T3, ACC␣-T3RE bound protein complexes (complexes 1 and 2) containing the liver X receptor (LXR) and the retinoid X receptor (RXR). In nuclear extracts from hepatocytes incubated in the presence of T3 for 24 h, ACC␣-T3RE bound a different set of complexes. One complex contained LXR and RXR (complex 3) and another contained the nuclear T3 receptor (TR) and RXR (complex 4). Mutations of ACC␣-T3RE that inhibited the binding of complexes 1 and 2 decreased transcriptional activation in the absence of T3, and mutations of ACC␣-T3RE that inhibited the binding of complexes 3 and 4 decreased transcriptional activation in the presence of T3. The stimulation of ACC␣ transcription caused by T3 was closely associated with changes in the binding of complexes 1-4 to ACC␣-T3RE. These data suggest that T3 regulates ACC␣ transcription by a novel mechanism involving changes in the composition of nuclear receptor complexes bound to ACC␣-T3RE. We propose that complexes containing LXR/RXR ensure a basal level of ACC␣ expression for the synthesis of structural lipids in cell membranes and that complexes containing LXR/RXR and TR/RXR mediate the stimulation of ACC␣ expression caused by T3.When the intake of dietary carbohydrate exceeds the immediate energy needs of the animal, excess carbohydrate is converted to triacylglycerols, which can be used for energy during periods of fasting. One of the enzymes that plays a pivotal role in mediating this response is acetyl-CoA carboxylase (ACC). 1 ACC catalyzes the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA, which is the donor of all but two () of the carbon atoms for the synthesis of long-chain fatty acids. This reaction is the pace-setting step of the fatty acid synthesis pathway (1, 2). There are two ACC isoforms that are encoded by distinct genes. ACC␣ (260 kDa) is the principal isoform expressed in tissues that exhibit high rates of fatty acid synthesis such as liver, adipose tissue, and mammary gland. ACC␤ (280 kDa) is the major isoform observed in heart and skeletal muscle, where it is thought to function primarily in the regulation of ␤-oxidation of fatty acids (3).The concentration of ACC␣ in liver is subject to nutritional and hormonal regulation. For example, in starved animals, the concentration of hepatic ACC␣ is low; feeding a high carbohydrate, low fat diet stimulates an 8 -20-fold increase in the amount of the enzyme (4 -7). The effects of nutritional manipulation on ACC␣ concentration are mediated primarily by changes in the rate of transcription of the ACC␣ gene (8). Diet-induced changes in ACC␣ transcription are mi...

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Cloning and characterization of the 5′ end and promoter region of the chicken acetyl-CoA carboxylase gene

Cited by 15 publications

References 52 publications

Insulin-glucocorticoid interactions in the regulation of acetyl-CoA carboxylase-alpha transcript diversity in ovine adipose tissue

Insulin-glucocorticoid interactions in the regulation of acetyl-CoA carboxylase-alpha transcript diversity in ovine adipose tissue

The Rat Pyruvate Carboxylase Gene Structure

Thyroid Hormone Stimulates Acetyl-CoA Carboxylase-α Transcription in Hepatocytes by Modulating the Composition of Nuclear Receptor Complexes Bound to a Thyroid Hormone Response Element

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