Disease relevance of ACO

• The synthesized photolabile reagents were tested as photoaffinity labels for acyl-CoA oxidase (EC 1.3.99.3) from Arthrobacter species [1].

High impact information on ACO

• As part of an effort to understand how proteins are imported into the peroxisome, we have sought to identify the peroxisomal targeting signals in four unrelated peroxisomal proteins: human catalase, rat hydratase:dehydrogenase, pig D-amino acid oxidase, and rat acyl-CoA oxidase [2].
• Blot analysis of RNA from livers of rats treated with a peroxisome proliferator showed 2- to 3-fold increase in UOxase mRNA content, whereas the fatty acyl-CoA oxidase mRNA increased over 30-fold [3].
• Morris cells responded to the addition of ciprofibrate by increasing the levels of ACO mRNA, whereas HepG2 did not [4].
• A range of 4-thiaacyl-CoA derivatives has been synthesized to study the bioactivation of cytotoxic fatty acids by the mitochondrial medium-chain acyl-CoA dehydrogenase and the peroxisomal acyl-CoA oxidase [5].
• Activities of catalase, acyl-CoA oxidase and the cyanide-insensitive acyl-CoA beta-oxidation system in this tissue were comparable with those in rat liver [6].

Biological context of ACO

• To address species differences in response to DEHP at the molecular level, we used promoter-reporter gene assays to compare the ability of MEHP to induce gene expression from the rat or the human ACO promoter [7].
• The tissue distribution and genetic effect on mRNA concentrations of PPARgamma, PPARalpha, and ACO in two genetic populations of turkeys [randombred control (RBC2) and growth selected (F line)] was determined [8].
• The ACO mRNA was expressed in adipose tissue, skeletal muscle, and liver with no difference between genotypes [9].
• Acyl CoA oxidase (ACO) is a key enzyme of peroxisomal beta-oxidation and its transcriptional activation by PPs is often used as marker for the rodent response [10].
• The peroxisome proliferator (PP)-activated receptor alpha (PPAR alpha) mediates the effects of PPs by heterodimerizing with the retinoid X receptor (RXR) to bind to DNA at PP response elements (PPREs) upstream of PP-regulated genes, such as acyl-CoA oxidase [11].

Anatomical context of ACO

• The ACO mRNA was expressed in adipose tissue, skeletal muscle, and liver with no difference between the genetic populations [8].
• Specific activities of peroxisome acyl-CoA oxidase and microsome omega-lauryl hydroxylase have comparable rates in rat and guinea pig liver, but in human liver the activities are much lower [12].
• Antibodies against the peroxisomal markers catalase and acyl-CoA oxidase recognize the same organelles in double-labeling studies [13].
• Epithelial cells were sequentially isolated along the axis and the specific activities of the peroxisomal enzymes catalase and acyl-CoA oxidase were found to be significantly higher in differentiated and mature cells situated at the villus tip and stem than in the crypt [14].

Associations of ACO with chemical compounds

• On the other hand, the hormonal status does not seem to have a significant effect on the rat liver acyl-CoA oxidase mRNA level suggesting at most that insulin, corticosterone and estradiol have no direct effect on acyl-CoA oxidase gene expression, which contrasts with the well-known effect of peroxisome proliferators [12].

Analytical, diagnostic and therapeutic context of ACO

• These increases are in accordance with the changes in polypeptide patterns of isolated liver peroxisomes as well as in the immunoblotting of acyl-CoA oxidase [15].
• (3) The hybridization of guinea pig liver RNA with the rat liver-inducible acyl-CoA oxidase cDNA probe shows a decrease in the corresponding heterologous mRNA content after treatment with ciprofibrate at 30 mg/kg twice a day [15].

References