scholarly journals Corrigendum to: Biotin attachment domain-containing proteins mediate hydroxy fatty acid-dependent inhibition of acetyl CoA carboxylase

2021 ◽  
Author(s):  
Xiao-Hong Yu ◽  
Yuanheng Cai ◽  
Jantana Keereetaweep ◽  
Kenneth Wei ◽  
Jin Chai ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Hydroxy Fatty Acid ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Dependent Inhibition

Relative Activities of Acetyl-CoA Carboxylase and Fatty Acid Synthetase in Chick Liver: Effects of Dietary Fat

1973 ◽  
Vol 51 (7) ◽  
pp. 1029-1033 ◽  
Author(s):  
Gregory I. Liou ◽  
W. E. Donaldson
Keyword(s):  
Fatty Acid ◽  
Corn Oil ◽  
Fatty Acid Synthetase ◽  
Basal Diet ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Carboxylase Activity ◽  
Cytosol Fraction ◽  
Activity Concentrations

The specific activities of acetyl-CoA carboxylase and fatty acid synthetase were measured in the cytosol fraction of livers from chicks fed various levels of corn oil, cottonseed oil, corn-oil free fatty acids, or crude (79%) oleic acid. Activities of both enzymes were depressed by the addition of fat to a fat-free basal diet. The ratios of synthetase to carboxylase activity were greater than unity when up to 4% fat was fed, but less than unity when 8% or higher levels of fat were fed. The depressions of the activities of these enzymes appeared to be unrelated to the dietary level of linoleate. In in vitro experiments, 2 μM concentrations of palmityl-CoA or oleoyl-CoA depressed acetyl-CoA carboxylase activity. Concentrations of 20 μM of these acyl-CoA esters did not affect the activity of fatty acid synthetase.

scholarly journals HFA1 Encoding an Organelle-specific Acetyl-CoA Carboxylase Controls Mitochondrial Fatty Acid Synthesis inSaccharomyces cerevisiae

2004 ◽  
Vol 279 (21) ◽  
pp. 21779-21786 ◽  
Author(s):  
Ursula Hoja ◽  
Sandra Marthol ◽  
Jörg Hofmann ◽  
Sabine Stegner ◽  
Rainer Schulz ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Acid Synthesis ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Mitochondrial Fatty Acid

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

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.

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.

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