Changes in the activities of dihydroxyacetone phosphate and glycerol-3-phosphate acyltransferases in rat liver under various conditions

Horie, Seichi; Utsumi, Keisuke; Suga, Tetsuya

doi:10.1016/0005-2760(90)90156-r

Cited by 11 publications

(8 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, in purified peroxisomes the specific activity of DHAP-AT exhibited no significant increase under conditions causing an at least 10-fold increase in fatty acid f3-oxidation specific activity (206). In homogenates the specific activity of alkyl-DHAP synthase was hardly affected by proliferation (205,206), and a slight decrease in purified peroxisomes was observed (206) . In spite of the increase in total activity of the enzymes per liver cell, the plasmalogen content did not change appreciably upon proliferation (206).…”

Section: Localization and Topologymentioning

confidence: 92%

“…Peroxisome proliferation in liver by clofibrate or plasticizer results in a 2to 3-fold increase in total and specific activity of DHAP-AT (204)(205)(206) and a less than 2-fold increase in acyl/alkyl-DHAP reductase (205 , 207). However, in purified peroxisomes the specific activity of DHAP-AT exhibited no significant increase under conditions causing an at least 10-fold increase in fatty acid f3-oxidation specific activity (206).…”

Section: Localization and Topologymentioning

confidence: 99%

See 1 more Smart Citation

Biochemistry of Peroxisomes

Bosch

Schutgens²,

Wanders³

et al. 1992

Annu. Rev. Biochem.

796

233

View full text Add to dashboard Cite

Section: Localization and Topologymentioning

confidence: 92%

Section: Localization and Topologymentioning

confidence: 99%

Biochemistry of Peroxisomes

Bosch

Schutgens²,

Wanders³

et al. 1992

Annu. Rev. Biochem.

796

233

View full text Add to dashboard Cite

“…The absorptive cells contain large numbers of peroxisomes, which are responsible for a significant part of the metabolic activity of these cells (Novikoff & Novikoff, 1972). Peroxisomes contain various enzymes participating in lipid catabolism and anabolism (Lazarow & de Duve, 1976;Horie et al, 1990). Peroxisomal f-oxidation of fatty acids has been well characterized in rat small intestine, and the f-oxidation activity has been shown to increase after treatment with various compounds such as clofibrate and partially hydrogenated fish oil (PHFO) (Thomassen et al, 1985).…”

Section: Introductionmentioning

confidence: 99%

Studies of dihydroxyacetone phosphate acyltransferase in rat small intestine. Subcellular localization and effect of partially hydrogenated fish oil and clofibrate

Ruyter

Lund

Thomassen

et al. 1992

Biochemical Journal

View full text Add to dashboard Cite

The subcellular localization of dihydroxyacetone phosphate acyltransferase (DHAPAT) activity in rat small intestine was investigated by Nycodenz-gradient centrifugation. We found that DHAPAT had a predominant peroxisomal distribution, with a separate enzyme activity located in the microsomal fraction, the same distribution as found in rat liver. The effect of feeding rats on a diet with 20% (w/w) partially hydrogenated fish oil (PHFO) or 0.3% clofibrate on the activity of DHAPAT in rat small intestine and liver was studied. Both 20% PHFO and 0.3% clofibrate gave a 1.8-fold stimulation of the specific activities of DHAPAT in peroxisomes of the small intestine, whereas in the liver 20% PHFO gave a 1.4-fold stimulation and 0.3% clofibrate a 1.6-fold stimulation of the total DHAPAT activities in the postnuclear supernatant. The specific activities of DHAPAT in liver were not affected.

show abstract

“…The peroxisomal membrane-bound enzymes, which are involved in lipid metabolism, have not been examined much for their response to these agents, with the exception of DHAP-AT. Following administration of hypolipidemic drugs, 1.2-to 2.0-fold increases in the specific activity of DHAP-AT have generally been observed in homogenates or in L fractions of rat [17,111,[199][200][201][202] and mouse [203] liver and embryonic cells [204]. However, figure 4 shows that no significant increase occurs when the DHAP-AT activity is examined in purified peroxisomes of fibrate-treated rat liver.…”

Section: Effects Of Peroxisome Proliferatorsmentioning

confidence: 99%

“…Concerning the other peroxisomal enzymes involved in the ether-lipid biosynthesis, inconsistent changes have been found with regard to the influence of proliferators on acyl/alkyl-DHAP reductase [168,202] and alkyI-DHAP synthetase [202] activities in rodent liver. At the moment, no data are available regarding acyl-CoA reductase.…”

Section: Effects Of Peroxisome Proliferatorsmentioning

confidence: 99%

Proteins and enzymes of the peroxisomal membrane in mammals

Causeret

Bentéjac

Bugaut

1993

Biology of the Cell

View full text Add to dashboard Cite

Proteins of the peroxisomal membrane can be schematically divided into two groups, one being made up of more or less characterized proteins with generally unknown functions and the other consisting of enzyme activities of which the corresponding proteins have not been characterized. In the present report, these proteins and enzymes are described with the addition of unpublished results regarding their induction by peroxisome proliferators at the post-transcriptional level. Integral membrane proteins (IMPs) can be isolated using an alkaline solution of sodium carbonate. A dozen of preponderant IMPs can be seen on sodium dodecyl sulfate polyacrylamide gel electrophoresis, and the major band corresponds to a 70 kDa IMP, of which the corresponding rat cDNA is known. Some IMPs have been characterized by immunoblot analysis. Recently, a cDNA has been cloned for a peroxisome assembly factor (35 kDa IMP). Functions have also been proposed for some IMPs but are not yet firmly settled. Some IMPs (450/520, 70 and 26 kDa) are strongly induced by peroxisome proliferators. Our results extend to cipro- and fenofibrate the observation that the 70 kDa IMP mRNA level is strongly increased in di(2-ethylhexyl)phtalate-treated rats. All the enzyme activities associated with the peroxisomal membrane are involved in lipid metabolism: activation of substrates (fatty acids), ether lipid biosynthesis, and formation of precursors (fatty alcohols). It is believed that the same long-chain acyl-CoA synthetase occurs in the peroxisome as well as in the outer mitochondrial membrane and the endoplasmic reticulum. However, two highly homologous but different cDNAs encoding rat liver and brain long-chain acyl-CoA synthetases have been isolated recently. Evidence has been accumulated for a distinct synthetase that specifically activates very-long chain fatty acids. The first two steps of ether lipid biosynthesis require dihydroxyacetone-phosphate (DHAP) acyltransferase and alkyl-DHAP synthetase, the active sites of which are located on the inner surface of the membrane. In contrast, the catalytic site of the acyl/alkyl-DHAP reductase, which generates sn-1-alkyl-glycerol-3-phosphate, is located on the outer surface. Long-chain fatty alcohols, which are obligate precursors of ether lipids and wax esters, are biosynthetized by the reduction of the corresponding acyl-CoAs via the action of an acyl-CoA reductase. Peroxisome proliferators do not appear to stimulate these enzyme activities specifically. However, we report that feno- and ciprofibrate treatments increase six-fold the palmitoyl-CoA synthetase mRNA level in the rat liver.

show abstract

Changes in the activities of dihydroxyacetone phosphate and glycerol-3-phosphate acyltransferases in rat liver under various conditions

Cited by 11 publications

References 39 publications

Biochemistry of Peroxisomes

Biochemistry of Peroxisomes

Studies of dihydroxyacetone phosphate acyltransferase in rat small intestine. Subcellular localization and effect of partially hydrogenated fish oil and clofibrate

Proteins and enzymes of the peroxisomal membrane in mammals

Contact Info

Product

Resources

About