Expression Profile of Acetyl CoA Carboxylase Beta (ACACB) Gene during the Pre and Post-hatch Period in Chicken

2021 ◽  
Author(s):  
Ch. Shiva Prasad ◽  
R. Vinoo ◽  
R.N. Chatterjee ◽  
M. Muralidhar ◽  
D. Narendranath ◽  
...  
Keyword(s):  
Gene Expression ◽  
Fatty Acid ◽  
Expression Pattern ◽  
Fatty Acyl ◽  
Acid Oxidation ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Layer Chicken ◽  
Differential Expression Pattern ◽  
Long Chain

Background: Acetyl-CoA Carboxylase Beta (ACACB) plays a key role in fatty acid oxidation and was known to be involved in production of very-long-chain fatty acid and other compounds needed for proper development. This gene is mainly expressed in the tissues of heart, muscle, liver and colon. It chiefly involved in the production of malonyl-coA, a potent inhibitor of carnitine palmitoyl transferase I (CPT-I) enzyme needed in transport of long-chain fatty acyl-coAs to the mitochondria for β-oxidation.Methods: The present study was conducted to explore the expression pattern of the ACACB gene in breast muscle tissue during pre-hatch embryonic day (ED) 5th to 18th and post-hatch (18th, 22nd and 40th week of age) periods of White leghorn (IWI line) by using Quantitative real-time PCR (qPCR). Then, fold change of ACACB gene expression was calculated.Result: Our study showed that the ACACB gene expression was down-regulated during embryonic stages from ED6 to ED18. The gene expression was also down-regulated during adult stages i.e. on 22nd and 40th week of age. This result indicated that the initial expression of the ACACB gene is required for embryo development and during adult periods, low gene expression leads to the less fat deposition in muscle of layer chicken. Finally, it can be concluded that there was a differential expression pattern of the ACACB gene during the pre-hatch embryonic and post-hatch adult periods to mitigate varied requirements of lipids during different physiological stages in layer chicken.

scholarly journals Identification of a second human acetyl-CoA carboxylase gene

1996 ◽  
Vol 316 (3) ◽  
pp. 915-922 ◽  
Author(s):  
Jane WIDMER ◽  
Katherine S. FASSIHI ◽  
Susannah C. SCHLICHTER ◽  
Kate S. WHEELER ◽  
Barbara E. CRUTE ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Cultured Cells ◽  
Regulatory Control ◽  
Chromosome 17 ◽  
Acid Oxidation ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Specific Expression ◽  
Mrna Tissue Distribution

Acetyl-CoA carboxylase (ACC), an important enzyme in fatty acid biosynthesis and a regulator of fatty acid oxidation, is present in at least two isoenzymic forms in rat and human tissues. Previous work has established the existence of a 265000 Da enzyme in both the rat and human (RACC265; HACC265) and a higher-molecular-mass species (275000–280000 Da) in the same species (RACC280; HACC275). An HACC265 gene has previously been localized to chromosome 17. In the present study, we report cloning of a partial-length human cDNA sequence which appears to correspond to HACC275 and its rat homologue, RACC280, as judged by mRNA tissue distribution and cell-specific regulation of mRNA/protein expression. The gene encoding this isoenzymic form of ACC has been localized to the long arm of human chromosome 12. Thus, ACC is represented in a multigene family in both rodents and humans. The newly discovered human gene and its rat homologue appear to be under different regulatory control to the HACC265 gene, as judged by tissue-specific expression in vivo and by independent modulation in cultured cells in vitro.

scholarly journals Acetyl-CoA carboxylase regulation of fatty acid oxidation in the heart.

1993 ◽  
Vol 268 (34) ◽  
pp. 25836-25845
Author(s):  
M Saddik ◽  
J Gamble ◽  
L A Witters ◽  
G D Lopaschuk
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Oxidation ◽  
Acid Oxidation ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa

Effect of phosphorylation by AMP-activated protein kinase on palmitoyl-CoA inhibition of skeletal muscle acetyl-CoA carboxylase

2005 ◽  
Vol 98 (4) ◽  
pp. 1221-1227 ◽  
Author(s):  
D. S. Rubink ◽  
W. W. Winder
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acid ◽  
Protein Kinase ◽  
Fatty Acid Oxidation ◽  
Acid Oxidation ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Oxidation Rates ◽  
Malonyl Coa ◽  
Amp Activated Protein Kinase

AMP-activated protein kinase (AMPK) has previously been demonstrated to phosphorylate and inactivate skeletal muscle acetyl-CoA carboxylase (ACC), the enzyme responsible for synthesis of malonyl-CoA, an inhibitor of carnitine palmitoyltransferase 1 and fatty acid oxidation. Contraction-induced activation of AMPK with subsequent phosphorylation/inactivation of ACC has been postulated to be responsible in part for the increase in fatty acid oxidation that occurs in muscle during exercise. These studies were designed to answer the question: Does phosphorylation of ACC by AMPK make palmitoyl-CoA a more effective inhibitor of ACC? Purified rat muscle ACC was subjected to phosphorylation by AMPK. Activity was determined on nonphosphorylated and phosphorylated ACC preparations at acetyl-CoA concentrations ranging from 2 to 500 μM and at palmitoyl-CoA concentrations ranging from 0 to 100 μM. Phosphorylation resulted in a significant decline in the substrate saturation curve at all palmitoyl-CoA concentrations. The inhibitor constant for palmitoyl-CoA inhibition of ACC was reduced from 1.7 ± 0.25 to 0.85 ± 0.13 μM as a consequence of phosphorylation. At 0.5 mM citrate, ACC activity was reduced to 13% of control values in response to the combination of phosphorylation and 10 μM palmitoyl-CoA. Skeletal muscle ACC is more potently inhibited by palmitoyl-CoA after having been phosphorylated by AMPK. This may contribute to low-muscle malonyl-CoA values and increasing fatty acid oxidation rates during long-term exercise when plasma fatty acid concentrations are elevated.

scholarly journals Gene expression pattern of acetyl-coA carboxylase alpha, fatty acid synthase, and stearoyl-CoA desaturase in pregnant Barki sheep under complete feed deprivation

2019 ◽  
pp. 8-13
Author(s):  
Ahmed El-Sayed ◽  
Ahmed Ateya ◽  
Mohamed Hamed ◽  
Sherif Shoieb ◽  
Hussam Ibrahim ◽  
...  
Keyword(s):  
Gene Expression ◽  
Fatty Acid ◽  
Expression Pattern ◽  
Fatty Acid Synthase ◽  
Mrna Level ◽  
Gene Expression Pattern ◽  
Acetyl Coa Carboxylase ◽  
Down Regulation ◽  
Feed Deprivation ◽  
Stearoyl Coa Desaturase

Objective: To assess the mRNA level of acetyl CoA carboxylase alpha (ACACA), fatty acid synthase (FASN), and stearoyl-CoA desaturase (SCD) by means of real-time PCR in Barki sheep subjected to complete feed deprivation. Design: Controlled study. Animals: Seven healthy pregnant ewes. Procedures: Ewes were subjected to complete feed deprivation with ad libitum water for five consecutive days. Venous blood samples were collected from each ewe before (zero time) and on the fifth day post-deprivation of feed for measurement of the mRNA level of ACACA, FASN, and SCD and assessment of serum metabolic profile parameters. Results: On the fifth day post-fasting, the gene expression pattern of ACACA, FASN, SCD genes showed a significant (p < 0.05) down regulation in comparison with pre-deprivation of feed. There was a significant (p < 0.05) increase in the serum level of non-esterified fatty acids (NEFA), beta-hydroxyl buteric acid (BHBA), and triglycerides in pregnant ewes in the fifth day post-fasting in comparison with pre-deprivation of feed. On the other hand, there was a significant (p < 0.05) decrease in the level of glucose, cholesterol, and insulin in pregnant ewes in the fifth day post-fasting compared with pre-deprivation of feed. On histopathology, liver showed marked heptic steatosis in midzonal and periportal area, with formation of small fatty cysts in liver lobule. There was a positive correlation between leptin and insulin (r = 0.996; p < 0.01), BHB and leptin (r = 0.951; p < 0.05) and glucose and SCD (r = 1.0, p < 0.01). However, there was a negative correlation between FASN and NEFA (r = - 0.991; p < 0.05), FASN and leptin (r = -0.683; p < 0.05) and FASN and cholesterol (r = - 0.82; p < 0.05). Conclusion and clinical relevance: Pregnant Barki ewes can clinically tolerate complete feed deprivation for five days, with down regulation of ACACA, FASN, SCD genes and presence of marked metabolic changes. Therefore, metabolic monitoring is warranted to predict the early changes associated with feed deprivation under different stressful conditions.

Metabolic response to an acute jump in cardiac workload: effects on malonyl-CoA, mechanical efficiency, and fatty acid oxidation

2008 ◽  
Vol 294 (2) ◽  
pp. H954-H960 ◽  
Author(s):  
Lufang Zhou ◽  
Hazel Huang ◽  
Celvie L. Yuan ◽  
Wendy Keung ◽  
Gary D. Lopaschuk ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Energy Expenditure ◽  
Fatty Acid Oxidation ◽  
Mechanical Efficiency ◽  
Acid Oxidation ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Malonyl Coa ◽  
High Workload ◽  
Carnitine Palmitoyltransferase I

Inhibition of myocardial fatty acid oxidation can improve left ventricular (LV) mechanical efficiency by increasing LV power for a given rate of myocardial energy expenditure. This phenomenon has not been assessed at high workloads in nonischemic myocardium; therefore, we subjected in vivo pig hearts to a high workload for 5 min and assessed whether blocking mitochondrial fatty acid oxidation with the carnitine palmitoyltransferase-I inhibitor oxfenicine would improve LV mechanical efficiency. In addition, the cardiac content of malonyl-CoA (an endogenous inhibitor of carnitine palmitoyltransferase-I) and activity of acetyl-CoA carboxylase (which synthesizes malonyl-CoA) were assessed. Increased workload was induced by aortic constriction and dobutamine infusion, and LV efficiency was calculated from the LV pressure-volume loop and LV energy expenditure. In untreated pigs, the increase in LV power resulted in a 2.5-fold increase in fatty acid oxidation and cardiac malonyl-CoA content but did not affect the activation state of acetyl-CoA carboxylase. The activation state of the acetyl-CoA carboxylase inhibitory kinase AMP-activated protein kinase decreased by 40% with increased cardiac workload. Pretreatment with oxfenicine inhibited fatty acid oxidation by 75% and had no effect on cardiac energy expenditure but significantly increased LV power and LV efficiency (37 ± 5% vs. 26 ± 5%, P < 0.05) at high workload. In conclusion, 1) myocardial fatty acid oxidation increases with a short-term increase in cardiac workload, despite an increase in malonyl-CoA concentration, and 2) inhibition of fatty acid oxidation improves LV mechanical efficiency by increasing LV power without affecting cardiac energy expenditure.

Regulation of mammalian acetyl-CoA carboxylase

2002 ◽  
Vol 30 (6) ◽  
pp. 1059-1064 ◽  
Author(s):  
M. R. Munday
Keyword(s):  
Fatty Acid ◽  
Protein Kinase ◽  
Critical Role ◽  
Physiological Role ◽  
Acid Synthesis ◽  
Acid Oxidation ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Dependent Protein ◽  
Amp Activated Protein Kinase

Acetyl-CoA carboxylase (ACC) plays a critical role in the regulation of fatty acid metabolism and its two isoforms, ACCα and ACCβ, appear to have distinct functions in the control of fatty acid synthesis and fatty acid oxidation, respectively. They are regulated by similar short-term mechanisms of allosteric activation by citrate, and reversible phosphorylation and inactivation, and there is clearly interaction between these mechanisms. AMP-activated protein kinase is the important physiological ACC kinase for both isoforms and yet there is a potential physiological role for cAMP-dependent protein kinase in the hormonally mediated inactivation of ACCα, and phosphorylation of ACCβ in its unique N-terminus.

scholarly journals Phosphorylation of Acetyl-CoA Carboxylase by AMPK Reduces Renal Fibrosis and Is Essential for the Anti-Fibrotic Effect of Metformin

2018 ◽  
Vol 29 (9) ◽  
pp. 2326-2336 ◽  
Author(s):  
Mardiana Lee ◽  
Marina Katerelos ◽  
Kurt Gleich ◽  
Sandra Galic ◽  
Bruce E. Kemp ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Epithelial Cells ◽  
Lipid Accumulation ◽  
Acid Oxidation ◽  
Acetyl Coa Carboxylase ◽  
Tubular Epithelial Cells ◽  
Acetyl Coa ◽  
Expression Of Genes ◽  
Energy Sensing ◽  
Unilateral Ureteric Obstruction

BackgroundExpression of genes regulating fatty acid metabolism is reduced in tubular epithelial cells from kidneys with tubulointerstitial fibrosis (TIF), thus decreasing the energy produced by fatty acid oxidation (FAO). Acetyl-CoA carboxylase (ACC), a target for the energy-sensing AMP-activating protein kinase (AMPK), is the major controller of the rate of FAO within cells. Metformin has a well described antifibrotic effect, and increases phosphorylation of ACC by AMPK, thereby increasing FAO.MethodsWe evaluated phosphorylation of ACC in cell and mouse nephropathy models, as well as the effects of metformin administration in mice with and without mutations that reduce ACC phosphorylation.ResultsReduced phosphorylation of ACC on the AMPK site Ser79 occurred in both tubular epithelial cells treated with folate to mimic cellular injury and in wild-type (WT) mice after induction of the folic acid nephropathy model. When this effect was exaggerated in mice with knock-in (KI) Ser to Ala mutations of the phosphorylation sites in ACC, lipid accumulation and fibrosis increased significantly compared with WT. The effect of ACC phosphorylation on fibrosis was confirmed in the unilateral ureteric obstruction model, which showed significantly increased lipid accumulation and fibrosis in the KI mice. Metformin use was associated with significantly reduced fibrosis and lipid accumulation in WT mice. In contrast, in the KI mice, the drug was associated with worsened fibrosis.ConclusionsThese data indicate that reduced phosphorylation of ACC after renal injury contributes to the development of TIF, and that phosphorylation of ACC is required for metformin’s antifibrotic action in the kidney.

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