Disease relevance of ACACA

• Appreciable homology was observed among the sequences in close vicinity of the biotin sites of chicken liver acetyl-CoA carboxylase and other biotin-dependent carboxylases including biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase [1].
• The purpose of the work was to explore the diversity and function of alloantigens in chickens differing in genetic resistance to acute cecal coccidiosis, Eimeria tenella (ACC) [2].
• In each experiment, body weight, feed consumption, liver weight, liver fat, body fat, in vivo lipogenesis, and the hepatic activities of the lipogenic enzymes, acetyl-Coenzyme A carboxylase (ACC) and fatty acid synthetase (FAS), were measured [3].

High impact information on ACACA

• Thus, it appears that glucagon, acting via cyclic AMP, inhibits fatty acid synthesis by blocking the formation of citrate, an essential activator of acetyl-CoA carboxylase [4].
• However, the cytoplasmic concentration of citrate, a required allosteric activator of acetyl-CoA carboxylase, is depressed more than 90% by glucagon or dibutyrl cyclic AMP [4].
• Thyroid hormone stimulates acetyl-coA carboxylase-alpha transcription in hepatocytes by modulating the composition of nuclear receptor complexes bound to a thyroid hormone response element [5].
• Localization of possible functional domains including biotin carboxylase subsite in the acetyl-CoA carboxylase polypeptide is discussed [6].
• The complete amino acid sequence of acetyl-CoA carboxylase from chicken liver has been deduced by cloning and sequence analysis of DNA complementary to its messenger RNA [6].

Biological context of ACACA

• Measurements taken included in vitro lipogenesis (IVL), malic enzyme (ME), isocitrate dehydrogenase (ICD) and aspartate aminotransferase (AAT) activities and the expression of the genes for ME, fatty acid synthase (FAS) and acetyl coenzyme carboxylase (ACC) [7].
• Limited proteolysis of chicken liver acetyl-CoA carboxylase by staphylococcal serine proteinase yielded a fragment of 31 kDa which contained the biotinyl active site [1].
• Kinetics of activation of acetyl-CoA carboxylase by citrate. Relationship to the rate of polymerization of the enzyme [8].
• Multiple phosphorylation of acetyl-CoA carboxylase in chick liver cells. A cyclic AMP-independent process [9].
• Dimerization is the rate-limiting step of acetyl-CoA carboxylase polymerization [10].

Anatomical context of ACACA

• Acetyl-CoA carboxylase. Evidence for polymeric filament to protomer transition in the intact avian liver cell [11].
• Digitonin treatment of chick liver cells in monolayer culture perforates the plasma membrane, causing release of acetyl-CoA carboxylase and other cytosolic enzymes [11].
• Purification, characterization, and ontogeny of acetyl-CoA carboxylase isozyme of chick embryo brain [12].
• Although acetyl-CoA carboxylase mRNA was detected in adult chicken brain, heart, lung, kidney, uropygial gland, spleen, testis, and chest muscle as well as liver, the mRNA level in these tissues was much lower than that in liver of growing chicks [13].
• Phosphorylation of AMPKalpha on Thr172 and of acetyl-CoA carboxylase on Ser79 are higher in F4 and F3 than in F1 granulosa cells [14].

Associations of ACACA with chemical compounds

• The amino-terminal portion of the acetyl-CoA carboxylase has been found to exhibit a homologous primary structure to that of carbamyl phosphate synthetase [6].
• Neither acetyl-CoA carboxylase [acetyl-CoA:carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] activity assayed in the presence of citrate nor fatty acid synthetase activity is decreased in extracts of cells treated with glucagon [4].
• Depolymerization of fully polymerized acetyl-CoA carboxylase is caused by malonyl-CoA, ATP X Mg, and Mg2+ [10].
• When chick liver cells in monolayer culture were incubated with 32Pi in the presence of insulin, acetyl-CoA carboxylase became extensively labeled with 32Pi reaching a stoichiometry of 9 to 10 mol of phosphoryl group per mol of 240,000-dalton enzyme subunit [9].
• R286 of the tomato ACC synthase was mutated to a leucine via site-directed mutagenesis [15].

Regulatory relationships of ACACA

• The mechanisms by which triiodothyronine (T3), glucose, insulin, and glucagon regulate acetyl-CoA carboxylase expression in primary cultures of chick embryo hepatocytes have been investigated [16].

Other interactions of ACACA

• Avidin affinity chromatography was used to rapidly purify acetyl-CoA carboxylase to homogeneity in high yield from chicken liver [17].
• Hepatic expression of sterol regulatory element binding protein-1, ATP-citrate lyase, fatty acid synthase, malic enzyme, acetyl-CoA carboxylase and stearoyl-CoA (Delta9) desaturase 1 genes in ad libitum birds declined from their highest levels just before photostimulation as the birds came into and maintained egg production [18].
• 2. Biotin deficiency decreased hepatic activity of pyruvate carboxylase [EC 6.4.1.1] but activity of acetyl-CoA carboxylase [EC 6.4.1.2] was comparatively unaffected [19].

Analytical, diagnostic and therapeutic context of ACACA

• ACC transcription was low in livers of starved chicks; feeding them with a high-carbohydrate, low-fat diet induced ACC transcription, increasing it 11-fold [20].
• In contrast with rat ACC gene expression, reverse transcriptase PCR analysis performed on chicken liver mRNA did not reveal alternative splicing in the 5'-untranslated region of these messengers [21].
• Utilizing RNA blot hybridization and immunoblotting techniques, the changes of the hepatic contents of acetyl-CoA carboxylase mRNA and of the enzyme protein in growing chicks have been investigated [13].
• 1. Male chickens (Gallus domesticus) were treated with a single intramuscular injection of oestradiol-17 beta, then changes in the liver and plasma levels of triacylglycerol, phospholipid, nonesterified fatty acids and in the hepatic activities of acetyl-CoA carboxylase and fatty acid synthetase were measured at various times after injection [22].

References