High impact information on ACACA

• Exposure of bovine aortic endothelial cells (BAEC) to chemically synthesized ONOO- acutely and significantly increased phosphorylation of c-Src, PDK1, AMPK, and its downstream target, acetyl-CoA carboxylase (ACC), without affecting cellular AMP [1].
• We show that, in different mammalian species, unrelated genome segments of different origins have been recruited to express as functionally homologous PI the ancient and otherwise highly conserved ACC-alpha-encoding gene [2].
• Preparations of acetyl-CoA carboxylase [acetyl-CoA-carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] have been obtained from the plastids of avocado (Persea americana) fruit mesocarp and from spinach (Spinacia oleracea) chloroplasts [3].
• Glucose and DL-lactate infusion increased acetyl-CoA carboxylase activity about 12-fold compared to preinfusion activity of 5.3 +/- 4.2 nmoles/minute/g of wet weight [4].
• This implies that, in principle, none of these promoters can be singled out as the key element controlling the ACC-alpha-related contribution to establishment of milk fat content, although the activity of PIII only is known to be disproportionally stimulated by lactation in MECs [5].

Biological context of ACACA

• Exposure of BAEC to hypoxia-reoxygenation (H/R) caused a biphasic increase in AMPK and ACC phosphorylation, which was prevented by adenoviral overexpression of superoxide dismutase (SOD) or inhibition of nitric-oxide synthase (NOS) implicating a role of ONOO- formed during H/R [1].
• In liver, the activity of acetyl-CoA carboxylase was already significantly lower in the experimental group before parturition [6].
• On d 5 of infusion, mammary gland biopsies were performed and a portion of the tissue analyzed for mRNA expression of acetyl CoA carboxylase, fatty acid synthetase, delta 9-desaturase, lipoprotein lipase, fatty acid binding protein, glycerol phosphate acyltransferase and acylglycerol phosphate acyltransferase [7].

Anatomical context of ACACA

• The regulation of acetyl-CoA carboxylase and malonyl-CoA levels in skeletal muscle may involve a calcium-dependent mechanism [8].
• Expression levels of acetyl-CoA carboxylase and delta 9-stearoyl-CoA desaturase genes measured in the mammary gland did not differ significantly between diets [9].
• Both FED and INF had no effect on the mRNA abundance of leptin, lipoprotein lipase, or acetyl-CoA carboxylase in adipose tissue [10].
• However, dietary Cu did not influence the level of subcutaneous adipose tissue ACC and SCD mRNA [11].
• Somatotropin treatment resulted in smaller adipocytes, decreased rate of fatty acid synthesis and decreased total acetyl-CoA carboxylase activity of adipocytes, but with no change in the proportion of this enzyme in the active state [12].

Associations of ACACA with chemical compounds

• Acetyl-coenzyme A carboxylase alpha (ACACA), the major regulatory enzyme of fatty acid biosynthesis, catalyzes the conversion of acetyl-CoA to malonyl-CoA [13].
• Large-scale syntheses of metal-containing oligonucleotides are achieved using 5' modified phosporamidites containing [Ru(acac)(2)(IMPy)](2+) (acac is acetylacetonato; IMPy is 2'-iminomethylpyridyl-2'-deoxyuridine) (3) and [Ru(bpy)(2)(IMPy)](2+) (bpy is 2,2'-bipyridine; IMPy is 2'-iminomethylpyridyl-2'-deoxyuridine) (4) [14].
• Perfusion with medium containing AICAR was found to activate AMP-activated protein kinase in skeletal muscle, inactivate acetyl-CoA carboxylase, and decrease malonyl-CoA at all concentrations of palmitate [15].
• A decline in malonyl-CoA with 0.12 and 0.5 mM caffeine without an increase in cAMP supports the hypothesis that a calcium-dependent mechanisms of acetyl-CoA carboxylase and malonyl-CoA regulation exists, but a cAMP-dependent mechanism may also be involved with 3 mM caffeine [8].
• Methylmalonyl-CoA at 50 microM concentration inhibited the partially purified acetyl-CoA carboxylase uncompetitively by 10% and the propionyl-CoA carboxylase activity of the enzyme preparation competitively (apparent Ki = 21 microM) by 40% [16].

Other interactions of ACACA

• After parturition, the activities of acetyl-CoA carboxylase and fatty acid synthase dropped in the experimental group [6].
• The cellular consequences of residual milk accumulation were evident in the activities of acetyl-CoA carboxylase, fatty acid synthetase and galactosyltransferase, key enzyme markers of cellular differentiation, which decreased in glands undergoing lactation failure and were lower than values measured in tissue of control cows [17].

References