Peroxisome proliferation: Organelles or activity as an endpoint?

1993 ◽  
Vol 51 ◽  
pp. 396-397
Author(s):  
Catherine A. Taylor ◽  
Bruce M. Jarnot
Keyword(s):  
Acid Oxidation ◽  
Peroxisome Proliferation ◽  
Post Dose ◽  
Oxidation Activity ◽  
Wasting Syndrome ◽  
Perfluorodecanoic Acid ◽  
Hypolipidemic Agent ◽  
Commercially Important ◽  
Acyl Coa Oxidase ◽  
Mitochondrial Disruption

Peroxisome induction can be expressed as an increase in peroxisome area (proliferation) or as an increase in peroxisomal fatty acid oxidation (activity). This study compares proliferation and activity as endpoints for hepatic peroxisome induction by perfluorodecanoic acid (PFDA). Fluorocarboxylic acids such as PFDA represent a class of compounds possessing commercially important surfactant properties. A single 50 mg/Kg ip. dose of PFDA produces a characteristic “wasting syndrome” in male F-344 rats. Symptoms include hypophagia, weight loss, hepatomegaly, and delayed lethality. Hepatic studies reveal changes similar to those seen with the hypolipidemic agent clofibrate. These include mitochondrial disruption, endoplasmic reticulum and peroxisome proliferation, and increased peroxisomal acyl-CoA oxidase activity.Male Fisher-344 rats received a single ip. dose of 2, 20, or 50mg/Kg PFDA dissolved in 1:1 propylene glycol/water and were sacrificed 8 days post-dose. All control rats received an equal volume of vehicle ip. Animals were provided food and water ad libitum, except pair-fed controls which received the same restrictive food intake consumed by their weight-paired dosed partners (50mg/Kg PFDA group) to simulate the hypophagia associated with PFDA.

scholarly journals Deletion of nuclear factor-κB p50 upregulates fatty acid utilization and contributes to an anti-obesity and high-endurance phenotype in mice

2015 ◽  
Vol 309 (6) ◽  
pp. E523-E533 ◽  
Author(s):  
Yoshihiko Minegishi ◽  
Satoshi Haramizu ◽  
Koichi Misawa ◽  
Akira Shimotoyodome ◽  
Tadashi Hase ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Nuclear Factor Κb ◽  
Whole Body ◽  
Acid Oxidation ◽  
Endurance Capacity ◽  
Peroxisome Proliferator ◽  
Primary Role ◽  
Nuclear Factor ◽  
Oxidation Activity ◽  
Fatty Acid Utilization

The transcription factor nuclear factor-κB (NF-κB) plays an important role in regulating physiological processes such as immunity and inflammation. In addition to this primary role, NF-κB interacts physically with peroxisome proliferator-activated receptors regulating lipid metabolism-related gene expression and inhibits their transcriptional activity. Therefore, inhibition of NF-κB may promote fatty acid utilization, which could ameliorate obesity and improve endurance capacity. To test this hypothesis, we attempted to elucidate the energy metabolic status of mice lacking the p50 subunit of NF-κB (p50 KO mice) from the tissue to whole body level. p50 KO mice showed a significantly lower respiratory quotient throughout the day than did wild-type (WT) mice; this decrease was associated with increased fatty acid oxidation activity in liver and gastrocnemius muscle of p50 KO mice. p50 KO mice that were fed a high-fat diet were also resistant to fat accumulation and adipose tissue inflammation. Furthermore, p50 KO mice showed a significantly longer maximum running time compared with WT mice, with a lower respiratory exchange ratio during exercise as well as higher residual muscle glycogen content and lower blood lactate levels after exercise. These results suggest that p50 deletion facilitates fatty acid catabolism, leading to an anti-obesity and high-endurance phenotype of mice and supporting the idea that NF-κB is an important regulator of energy metabolism.

scholarly journals MicroRNA-15a Regulates the Differentiation of Intramuscular Preadipocytes by Targeting ACAA1, ACOX1 and SCP2 in Chickens

2019 ◽  
Vol 20 (16) ◽  
pp. 4063
Author(s):  
Guoxi Li ◽  
Shouyi Fu ◽  
Yi Chen ◽  
Wenjiao Jin ◽  
Bin Zhai ◽  
...  
Keyword(s):  
Target Gene ◽  
Adipogenic Differentiation ◽  
Mrna Level ◽  
Chicken Breast ◽  
Acid Oxidation ◽  
Expression Levels ◽  
Over Expression ◽  
Triglyceride Accumulation ◽  
Acyl Coa Oxidase ◽  
Sterol Carrier Protein 2

Our previous studies showed that microRNA-15a (miR-15a) was closely related to intramuscular fat (IMF) deposition in chickens; however, its regulatory mechanism remains unclear. Here, we evaluated the expression characteristics of miR-15a and its relationship with the expression of acetyl-CoA acyltransferase 1 (ACAA1), acyl-CoA oxidase 1 (ACOX1) and sterol carrier protein 2 (SCP2) by qPCR analysis in Gushi chicken breast muscle at 6, 14, 22, and 30 weeks old, where we performed transfection tests of miR-15a mimics in intramuscular preadipocytes and verified the target gene of miR-15a in chicken fibroblasts (DF1). The miR-15a expression level at 30 weeks increased 13.5, 4.5, and 2.7-fold compared with the expression levels at 6, 14, and 22 weeks, respectively. After 6 days of induction, miR-15a over-expression significantly promoted intramuscular adipogenic differentiation and increased cholesterol and triglyceride accumulation in adipocytes. Meanwhile, 48 h after transfection with miR-15a mimics, the expression levels of ACAA1, ACOX1 and SCP2 genes decreased by 56.52%, 31.18% and 37.14% at the mRNA level in intramuscular preadipocytes. In addition, the co-transfection of miR-15a mimics and ACAA1, ACOX1 and SCP2 3′UTR (untranslated region) dual-luciferase vector significantly inhibited dual-luciferase activity in DF1 cells. Taken together, our data demonstrate that miR-15a can reduce fatty acid oxidation by targeting ACAA1, ACOX1, and SCP2, which subsequently indirectly promotes the differentiation of chicken intramuscular preadipocytes.

scholarly journals Comparison of the activities of some peroxisomal and extraperoxisomal lipid-metabolizing enzymes in liver and extrahepatic tissues of the rat

1985 ◽  
Vol 227 (3) ◽  
pp. 737-741 ◽  
Author(s):  
P Van Veldhoven ◽  
G P Mannaerts
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Oxidation ◽  
Acid Oxidation ◽  
Dihydroxyacetone Phosphate ◽  
Metabolizing Enzymes ◽  
Mitochondrial Fatty Acid ◽  
Lipid Metabolizing Enzymes ◽  
Extrahepatic Tissues ◽  
Glycerolipid Synthesis ◽  
Acyl Coa Oxidase

Peroxisomal (acyl-CoA oxidase and peroxisomal dihydroxyacetone-phosphate acyltransferase) and extraperoxisomal (mitochondrial fatty acid oxidation, extraperoxisomal dihydroxyacetone-phosphate acyltransferase, mitochondrial and microsomal glycerophosphate acyltransferases) lipid-metabolizing enzymes were measured in homogenates from rat liver and from seven extrahepatic tissues. Except for jejunal mucosa and kidney, extrahepatic tissues contained very little acyl-CoA oxidase activity. Peroxisomal dihydroxyacetone-phosphate acyltransferase, taken as the activity that was not inhibited by 5 mM-glycerol 3-phosphate, was present in all tissues examined, and its specific activity in liver and extrahepatic tissues was roughly of the same order of magnitude. Clofibrate treatment increased the activity of acyl-CoA oxidase in liver, and to a smaller extent also in kidney, but did not influence the activity of peroxisomal dihydroxyacetone-phosphate acyltransferase. Comparison of the activities of peroxisomal and extraperoxisomal lipid-metabolizing enzymes in extrahepatic tissues and in liver, an organ in which the contribution of peroxisomes to fatty acid oxidation and to glycerolipid synthesis has been estimated previously, suggests that, as in liver, peroxisomal long-chain fatty acid oxidation is of minor quantitative importance in extrahepatic tissues, but that in these tissues (micro)-peroxisomes are responsible for most of the dihydroxyacetone phosphate acylation and, consequently, for initiating ether glycerolipid synthesis.

Hepatic peroxisome proliferation in vitamin A-deficient mice without a simultaneous increase in peroxisomal Acyl-CoA oxidase activity

1996 ◽  
Vol 51 (6) ◽  
pp. 821-827 ◽  
Author(s):  
Anna-Karin Sohlenius ◽  
Maria Reinfeldt ◽  
Katrin Bäckström ◽  
Anders Bergstrand ◽  
Joseph W. DePierre
Keyword(s):  
Vitamin A ◽  
Oxidase Activity ◽  
Simultaneous Increase ◽  
Peroxisome Proliferation ◽  
Acyl Coa Oxidase ◽  
Deficient Mice

Induction of fatty acid β-oxidation and peroxisome proliferation in the liver of rhesus monkeys by DL-040, a new hypolipidemic agent

1985 ◽  
Vol 34 (19) ◽  
pp. 3473-3482 ◽  
Author(s):  
Narendra D. Lalwani ◽  
M. Kumudavalli Reddy ◽  
Santibrata Ghosh ◽  
Stephen D. Barnard ◽  
Joseph A. Molello ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Rhesus Monkeys ◽  
Peroxisome Proliferation ◽  
Hypolipidemic Agent

scholarly journals Gene Expression Associated with Apple Aroma Biosynthesis

HortScience ◽  
2006 ◽  
Vol 41 (4) ◽  
pp. 977C-977
Author(s):  
Nobuko Sugimoto ◽  
Steve van Nocker ◽  
Schuyler Korban ◽  
Randy Beaudry
Keyword(s):  
Gene Expression ◽  
Fatty Acid ◽  
Ethylene Biosynthesis ◽  
Acid Oxidation ◽  
Beta Oxidation ◽  
Ripening Stages ◽  
Ester Formation ◽  
Ester Biosynthesis ◽  
Marked Decline ◽  
Acyl Coa Oxidase

A microarray containing over 10,000 gene fragments was used to link changes in gene expression with changes in aroma biosynthesis in ripening apple (Malus ×domestica Borkh). The microarray was probed with fluorescent-tagged cDNA derived from RNA extracted from `Jonagold' apple skin and cortex tissue representing eight distinct physiological stages spanning 70 days during ripening and senescence. The ripening stages, in chronological order, were: 1) early preclimacteric; 2) late preclimacteric and onset of trace ester biosynthesis; 3) onset of the autocatalytic ethylene and rapidly increasing ester biosynthesis; 4) half-maximal ester biosynthesis and engagement of the respiratory climacteric; 5) near maximal ester biosynthesis, peak in respiratory activity, and the onset of rapid tissue softening; 6) maximal ester biosynthesis prior to its decline, the conclusion of the respiratory climacteric, and the completion of tissue softening; 7) midpoint in the decline in ester biosynthesis and maximal ethylene biosynthesis; and 8) postclimacteric minimum in ester production. Patterns in gene expression reflecting the rise and fall in ester formation were found in some putative genes for beta-oxidation (acyl-CoA oxidase, enoyl-CoA hydratase, and acetyl-CoA acetyl transferase), ester formation (aminotransferase, alcohol dehydrogenase, and alcohol acyl transferase), and fatty acid oxidation (lipoxygenase), but not fatty acid biosynthetic genes. A marked decline coinciding with the onset of ester production was detected in several putative genes for ADH.

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