acyl-CoA Oxidase (acyl-coa + oxidase)

Distribution by Scientific Domains


Selected Abstracts


Impact of perfluorooctanoic acid on fathead minnow (Pimephales promelas) fatty acyl-coa oxidase activity, circulating steroids, and reproduction in outdoor microcosms

ENVIRONMENTAL TOXICOLOGY & CHEMISTRY, Issue 8 2004
Ken D. Oakes
Abstract This study investigates reproductive impairment and biochemical changes in fathead minnow (Pimephales promelas) exposed for 39 d to varying concentrations of perfluorooctanoic acid (PFOA) under microcosm conditions. While the concentrations tested in this study were much higher than those normally found in the environment, no mortality was associated with PFOA exposure. Only modest changes were observed in condition factor and in relative liver and gonad size. Significant declines in circulating plasma steroids were observed, but these were accompanied by only limited increases in time to first oviposition and decreases in overall egg production. Peroxisome proliferation, as quantified by fatty acyl-CoA oxidase (FAO) activity, was elevated with low PFOA concentrations but attenuated with exposure to higher PFOA doses. Little evidence was seen of differential induction of peroxisome-associated enzyme activity with sex. Oxidative stress, as quantified by the 2-thiobarbituric acid reactive substances (TBARS) assay, was only modestly influenced by PFOA exposure and is not a significant consequence of FAO activity in fathead minnow. Perfluorooctanoic acid appears to be relatively nontoxic at environmentally relevant concentrations but may impact biochemical and reproductive endpoints under conditions associated with environmental spills. [source]


PPAR gamma activators induce differentiation of B12 oligodendrocyte-like cells and rat spinal cord oligodendrocytes

JOURNAL OF NEUROCHEMISTRY, Issue 2002
A. D. Roth
The regulation of CNS lipid metabolism by nuclear receptors and their relation to cell differentiation remains undetermined. Since myelinating oligodendrocytes are the major lipid-synthesizing cells in the CNS, we characterized the effect of PPAR activation in a CNS derived cell line that expresses oligodendrocyte markers and compared these effects with oligodendrocyte primary cultures (90,95% pure). The rat glioma derived B12 cell line express the three major PPAR isoforms (PPAR ,, , and ,) and present a large number of peroxisomes, indicating an important lipid metabolism. Treatment with ciprofibrate, a general PPAR activator and clinical hypolipidemic, induces proliferation arrest, process extension and a moderate rise in the expression of acyl-CoA oxidase, a specific marker of peroxisomal proliferation. Cell growth arrest by ciprofibrate is enhanced 100-fold by low concentrations of retinoic acid (0.01 ,m), suggesting the involvement of the PPAR-retinoid acid receptor heterodimers. Since ciprofibrate possibly acts by modifying the concentration of endogenous PPAR ligands, we traced its effects to PPAR, by using isoform specific ligands: Troglitazone and 15-deoxy-prostaglandin J2, both of which induce growth arrest and process extension in B12 cells. These effects were corroborated on rat spinal cord derived oligodendrocytes primary cultures, where a significant rise in the number of mature oligodendrocytes is observed in response to PPAR, activators. These results show that PPAR,, a master gene in the differentiation of adipose tissue could be involved in the lipid metabolism of maturing oligodendrocytes. [source]


Gene expression of fatty acid-binding proteins, fatty acid transport proteins (cd36 and FATP) and ,-oxidation-related genes in Atlantic salmon (Salmo salar L.) fed fish oil or vegetable oil

AQUACULTURE NUTRITION, Issue 4 2009
B.E. TORSTENSEN
Abstract Relative gene expression pattern of fatty acid transport proteins (FATP and cd36), intracellular fatty acid-binding proteins (FABP3, FABP10 and FABP11), ,-oxidation-related genes [carnitine palmitoyl transferase II (CPTII), peroxisome proliferator-activated receptor , (PPAR,), acyl-CoA oxidase (AOX), long-chain fatty acyl-CoA synthetase (FACS), acyl-CoA dehydrogenase (dehydrogenase)] and uncoupling protein 2 (UCP2) was assessed by RT-qPCR in Atlantic salmon muscle (red and white), liver, heart, myosepta and visceral fat. FABP11, a FABP isoform not previously described in Atlantic salmon, was highly expressed in visceral fat and myosepta and at the lower level in red muscle, white muscle, myosepta and heart. Furthermore, Atlantic salmon were fed either a diet containing fish oil (FO) or a complete replacement of FO with a vegetable oil blend (55% rapeseed oil, 30% palm oil and 15% linseed oil; VO) for the production cycle (27 months from start of feeding and until ,4.5 kg mean weight). The expression of genes related to ,-oxidation, fatty acid uptake and transport in the white muscle indicate (n = 3) significant down-regulation in VO fed Atlantic salmon and correlated with previously reported white muscle triacylglycerol stores and ,-oxidation. FABP11 in visceral fat and myosepta was also down-regulated in VO fed fish. [source]


Auraptene, a citrus fruit compound, regulates gene expression as a PPAR, agonist in HepG2 hepatocytes

BIOFACTORS, Issue 1 2008
Nobuyuki Takahashi
Abstract Citrus fruit compounds have various activities that improve pathological conditions in many tissues. In this study, we examined the effect of auraptene contained mainly in the peel of citrus on peroxisome proliferator-activated receptor-, (PPAR,) activation. To examine effects of auraptene on the PPAR, activation in hepatocytes, PPAR ligand assay system was developed using HepG2 hepatocytes, in which the endogenous PPAR, expression level is very low. In the PPAR ligand assay, the addition of auraptene showed significant effects on the transactivation of GAL4/PPAR, chimera proteins in a dose-dependent manner. Actually, treatment with auraptene induced the up-regulation of PPAR target genes, such as acyl-CoA oxidase (ACO), carnitine-palmitoyl transferase 1A (CPT1A) and acyl-CoA synthetase (ACS), in PPAR,-expressing HepG2 hepatocytes. The regulation of gene expression was dependent on PPAR, because mock-transfected HepG2 hepatocytes showed no regulation. The up-regulation of PPAR target gene expression by auraptene was sufficient to enhance oleic acid uptake into PPAR,-expressing HepG2 hepatocytes. These results indicate that auraptene acts as a PPAR, agonist in hepatocytes and that auraptene may improve lipid abnormality through PPAR, activation in the liver. [source]