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Acyl-Coenzyme A oxidase 3, pristanoyl

pristanoyl-CoA oxidase, ACOX3, PCOX, hBRCACox
Acyl-Coenzyme A oxidase 3 also know as pristanoyl -CoA oxidase (ACOX3)is involved in the desaturation of 2-methyl branched fatty acids in peroxisomes. Unlike the rat homolog, the human gene is expressed in very low amounts in liver such that its mRNA was undetectable by routine Northern-blot analysis or its product by immunoblotting or by enzyme activity measurements. However the human cDNA encoding a 700 amino acid protein with a peroxisomal targeting C-terminal tripeptide S-K-L was isolated and is thought to be expressed under special conditions such as specific developmental stages or in a tissue specific manner in tissues that have not yet been examined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, V1a, STEP, CAN, fibrillin-1
Papers on pristanoyl-CoA oxidase
Acyl-coenzyme A oxidases 1 and 3 in brown trout (Salmo trutta f. fario): Can peroxisomal fatty acid β-oxidation be regulated by estrogen signaling?
Rocha et al., Porto, Portugal. In Fish Physiol Biochem, Nov 2015
UNASSIGNED: Acyl-coenzyme A oxidases 1 (Acox1) and 3 (Acox3) are key enzymes in the regulation of lipid homeostasis.
Changes of Dietary Fat and Carbohydrate Content Alter Central and Peripheral Clock in Humans.
Pfeiffer et al., Potsdam, Germany. In J Clin Endocrinol Metab, Jun 2015
The LC/HFD also affected the expression of nonoscillating genes contributing to energy metabolism (SIRT1) and fat metabolism (ACOX3 and IDH3A).
Homozygous and heterozygous GH transgenesis alters fatty acid composition and content in the liver of Amago salmon (Oncorhynchus masou ishikawae).
Mori et al., Fujisawa, Japan. In Biol Open, 2012
Furthermore, 3'-tag digital gene expression profiling was performed using liver tissues from Tg/Tg and +/+ fish, and showed that Mid1 interacting protein 1 (Mid1ip1), which is an important factor to activate Acetyl-CoA carboxylase (ACC), was down-regulated in Tg/Tg fish, while genes involved in FA catabolism were up-regulated, including long-chain-fatty-acid-CoA ligase 1 (ACSL1) and acyl-coenzyme A oxidase 3 (ACOX3).
Association between single nucleotide polymorphism-genotype and outcome of patients with chronic lymphocytic leukemia in a randomized chemotherapy trial.
Houlston et al., Oxford, United Kingdom. In Haematologica, 2011
RESULTS: The strongest associations were shown for rs1949733 (ACOX3; P=8.22x10-7), rs1342899 (P=7.72×10(-7)) and rs11158493 (PPP2R5E; P=8.50×10(-7)).
Gene expression profiles of adipose tissue of obese rats after central administration of neuropeptide Y-Y5 receptor antisense oligodeoxynucleotides by cDNA microarrays.
Guo et al., Nanjing, China. In Peptides, 2008
Different clusters of genes associated with apoptosis, signal transduction, energy metabolism, lipid metabolism, etc., such as FXR1, PHLDA1, MAEA, PIK3R1, ICAM2, PITPN, CALM2, CAMK2D, PKIA, DRD2, SLC25A14, CKB, AADAC, LIPA, ACOX3, FADS1, were concerned.
Peroxisomes contain a specific phytanoyl-CoA/pristanoyl-CoA thioesterase acting as a novel auxiliary enzyme in alpha- and beta-oxidation of methyl-branched fatty acids in mouse.
Alexson et al., Huddinge, Sweden. In J Biol Chem, 2007
Acot6 mRNA was mainly expressed in white adipose tissue and was co-expressed in tissues with Acox3 (the pristanoyl-CoA oxidase).
Peroxisomal branched chain fatty acid beta-oxidation pathway is upregulated in prostate cancer.
Isaacs et al., Boston, United States. In Prostate, 2005
ACOX3, which is expressed at extremely low level in other human organs studied including the liver, might contribute significantly to peroxisomal branched chain fatty acid beta-oxidation in human prostate tissue and some prostate cancer cell lines
Transcriptional regulation of cyclo-oxygenase expression: three pillars of control.
Mantamadiotis et al., Australia. In Int J Immunopathol Pharmacol, 2003
For instance, COX-1 splice variants (also known as COX-3 and PCOX-1a) may broaden the spectrum of COX activities in disease.
COX-3, a cyclooxygenase-1 variant inhibited by acetaminophen and other analgesic/antipyretic drugs: cloning, structure, and expression.
Simmons et al., Provo, United States. In Proc Natl Acad Sci U S A, 2002
Here we describe a third distinct COX isozyme, COX-3, as well as two smaller COX-1-derived proteins (partial COX-1 or PCOX-1 proteins).
Peroxisomal beta-oxidation and peroxisome proliferator-activated receptor alpha: an adaptive metabolic system.
Hashimoto et al., Chicago, United States. In Annu Rev Nutr, 2000
The peroxisomal beta-oxidation system consists of (a) a classical peroxisome proliferator-inducible pathway capable of catalyzing straight-chain acyl-CoAs by fatty acyl-CoA oxidase, L-bifunctional protein, and thiolase, and (b) a second noninducible pathway catalyzing the oxidation of 2-methyl-branched fatty acyl-CoAs by branched-chain acyl-CoA oxidase (pristanoyl-CoA oxidase/trihydroxycoprostanoyl-CoA oxidase), D-bifunctional protein, and sterol carrier protein (SCP)x.
Peroxisomal beta-oxidation enzyme gene expression in the developing mouse brain.
Garbay et al., Bordeaux, France. In Neurosci Lett, 2000
Using the northern blot technique, the steady-state levels for the mRNAs encoding acyl-CoA oxidase, pristanoyl-CoA oxidase, trans2, 3enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase multifunctional enzyme type 2, 3-ketoacyl-CoA thiolase and sterol-carrier-protein x during postnatal brain development were measured.
Localization of the gene for a novel autosomal recessive neurodegenerative Huntington-like disorder to 4p15.3.
Meyer et al., Riyadh, Saudi Arabia. In Am J Hum Genet, 2000
Among the three known genes residing in the linked interval (ACOX3, DRD5, QDPR), the most likely candidate, DRD5, encoding the dopamine receptor D5, was excluded, since all five affected family members were heterozygous for an intragenic dinucleotide repeat.
Peroxisomal lipid degradation via beta- and alpha-oxidation in mammals.
Casteels et al., Leuven, Belgium. In Cell Biochem Biophys, 1999
2-Methyl-branched acyl-CoAs are degraded via pristanoyl-CoA oxidase, multifunctional protein-2 (MFP-2) (which displays 2-enoyl-CoA hydratase and D-3-hydroxyacyl-CoA dehydrogenase activities) and sterol carrier protein-X (SCPX; displaying 2-methyl-3-oxoacyl-CoA thiolase activity).
Role and organization of peroxisomal beta-oxidation.
Mannaerts et al., Leuven, Belgium. In Adv Exp Med Biol, 1998
Finally, pristanic acid is degraded in rat tissues by pristanoyl-CoA oxidase, the D-specific multifunctional protein-2 and SCPX-thiolase.
New insights in peroxisomal beta-oxidation. Implications for human peroxisomal disorders.
Van Veldhoven, Leuven, Belgium. In Verh K Acad Geneeskd Belg, 1997
beta-oxidation of pristanic acid can occur in all tissues and relies on the action of 2-methylacyl-CoA racemase (for the 2R-isomer), pristanoyl-CoA oxidase (in rat) or branched chain acyl-CoA oxidase (in man), D-specific multifunctional protein 2 (MFP 2) and sterol carrier protein X/thiolase.
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