BRAIN ACYL‐COENZYME A HYDROLASE: DISTRIBUTION, PURIFICATION AND PROPERTIES<sup>1</sup>

Anderson, A.Duane; Erwin, V. Gene

doi:10.1111/j.1471-4159.1971.tb00216.x

Cited by 56 publications

(16 citation statements)

References 25 publications

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“…Among them, brain exhibits the highest activity which is localized in the soluble fraction [I, 6,8]. It is interesting that approximately 90% of the rat brain enzyme was titrated with an antibody produced against the new enzyme.…”

Section: Discussionmentioning

confidence: 99%

Induction of a Novel Long‐Chain Acyl‐CoA Hydrolase in Rat Liver by Administration of Peroxisome Proliferators

Miyazawa

Furuta

Hashimoto

1981

European Journal of Biochemistry

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The activity of long-chain acyl-CoA hydrolase in rat liver was increased by the administration of peroxisome proliferators, such as ethyl p-chlorophenoxyisobutyrate, di(2-ethy1hexyl)phthalate or acetylsalicylic acid. The induced activity was mainly confined 'in the soluble fluid after the subcellular fractionation. The enzyme was purified nearly to homogeneity from livers of rats treated with di(2-ethy1hexyl)phthalate. The specific activity of the final preparation was 247 pmol palmitoyl-CoA hydrolyzed min-' mg protein-'. The molecular weight of the native enzyme was estimated to be 150000 by gel filtration and that of the subunits was 41 000 by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. The activity of the enzyme was not increased but inhibited by bovine serum albumin or Triton X-100. The molecular. and catalytic properties of the enzyme suggest that the induced enzyme was different from mitochondria1 and microsomal long-chain acyl-CoA hydrolases in liver.Long-chain fatty acyl-CoA hydrolases are present in various mammalian tissues [I -81. In rat liver, the enzymes are mainly localized in mitochondria and microsomes [2,3]. These enzymes in both particulates have been purified and characterized [4,5]. During the course of our study on the effect of di(2-ethylhexyl)phthalate, which is a potent inducer of peroxisomal /%oxidation system [9], on activities of acylCoA dehydrogenases in rat liver mitochondria, we noticed that the reducing activity of 2,6-dichloroindophenol in the presence of palmitoyl-CoA was markedly induced by the administration of di(2-ethylhexy1)phthalate. The increased rate of the dye reduction was due to the elevated activity of long-chain acyl-CoA hydrolase.In the present study, the induced hydrolase was found in the soluble fraction after the subcellular fractionation of rat livers. The enzyme was purified to a nearly homogeneous preparation and found to be a new enzyme with respect to its molecular and catalytic properties. MATERIALS AND METHODS MaterialsAcetyl-CoA and butyryl-CoA were prepared from the corresponding acid anhydrides. Other acyl-CoA derivatives were synthesized by the mixed anhydride method [lo] and purified as described previously [ l l , 121. CoA, bovine serum albumin and cytochrome c were from Sigma. Enzymes and coenzymes were purchased froin Boehringer. Analytical grades of fatty acids and other reagents were commercial products.Enzymes. Acyl-CoA oxidase (EC 1.3.-.-); adenylate kinase (EC 2.7.4.3); dlcohol dehydrogenase (EC 1.1.1.1); aldolase (EC 4.1.2.13); catalase (EC 1.11.1.6); citrate synthase (EC 4.1.3.7); glutamate dehydrogenase (EC 1.4.1.3); horseradish peroxidase (EC 1.11.1.7); lactate dehydrogendse (EC 1.1.1.27); long-chain acyl-CoA hydrolase (EC 3.1.2.2); malate dehydrogenase (EC 1.1.1.37) ; NADPH-cytochrome c reductase (EC 1.6.2.4); phosphorylase (EC 2.4.1.1). Animals and Subcellular FractionationMale Wistar rats (200-250 g) were fed a powdered diet (Oriental M, Tokyo) containing 2 (w/w) di(2-ethylhexy1)-phthalate for 2-4 weeks, when they were us...

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Section: Discussionmentioning

confidence: 99%

Induction of a Novel Long‐Chain Acyl‐CoA Hydrolase in Rat Liver by Administration of Peroxisome Proliferators

Miyazawa

Furuta

Hashimoto

1981

European Journal of Biochemistry

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“…A fairly active acetyl-CoA hydrolase with an activity of about 50,umol/h per g wet wt. has been found in rat brain, mainly in the postmitochondrial supernatant (Anderson & Erwin, 1971). Finally, acetate is produced by the hydrolysis of acetylcholine, occurring in vivo at a rate of the order of 0.6,umol/h per g wet wt.…”

Section: Short-chain Fatty Acid Activation In Brainmentioning

confidence: 99%

Short-chain fatty acid synthesis in brain. Subcellular localization and changes during development

Reijnierse

Veldstra

Ber

1975

Biochemical Journal

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Acetyl-CoA synthase (EC 6.2.1.1), Propionyl-CoA synthase (EC 6.2.1.-) and butyryl-CoA synthase (EC 6.2.1.2) were measured in subcellular fractions prepared by primary and density-gradient fractionation from adult rat brain by a method resulting in recoveries close to 100%. Most of the activity of the three enzymes was recovered in the crude mitochondrial fraction. On subfractionation of this crude mitochondrial fraction with continuous sucrose density gradients, most of the activity of the three enzymes was found at a higher density than NAD+-isocitrate dehydrogenase and at about the same density as glutamate dehydrogenase, confirming earlier reported data for acetyl-CoA synthase. The finding that propionyl-CoA synthase and butyryl-CoA synthase had about the same distribution in the gradients as acetyl-CoA synthase adds support to the hypothesis that mitochondria involved in the metabolism of these short-chain fatty acids (all three of which have been shown to result in a rapid and high labelling of glutamine in vivo) form a distinct subpopulation of the total mitochondrial population. The three synthase activities were found to differ from each other in their rate of change and their subcellular localization during rat brain development. This, in combination with the observation that in gradients of adult brain preparations the three activities did not completely overlap, suggests that the three synthase activities are not present in the same proportion to each other in the same subpopulation (s) of mitochondria in the brain.

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“…In contrast with the stimulation ofchain elongation by albumin, the microsomal hydrolase [and the soluble hydrolase from rat brain (Anderson & Erwin, 1971)] is dramatically inhibited by albumin. Barden & Cleland (1969) have attributed a similar effect by albumin on the palmitoyl-CoA hydrolase in rat liver 1976 250n I microsomal fractions to a preference for substrate in the micellar form.…”

Section: Effect Of Bovine Serum Albumin On the Elongation And Hydrolymentioning

confidence: 99%

The synthesis and hydrolysis of long-chain fatty acyl-coenzyme A thioesters by soluble and microsomal fractions from the brain of the developing rat

Brophy

Vance

1976

Biochemical Journal

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1. The specific activities of long-chain fatty acid-CoA ligase (EC6.2.1.3) and of long-chain fatty acyl-CoA hydrolase (EC3.1.2.2) were measured in soluble and microsomal fractions from rat brain. 2. In the presence of either palmitic acid or stearic acid, the specific activity of the ligase increased during development; the specific activity of this enzyme with arachidic acid or behenic acid was considerably lower. 3. The specific activities of palmitoyl-CoA hydrolase and of stearoyl-CoA hydrolase in the microsomal fraction decreased markedly (75%) between 6 and 20 days after birth; by contrast, the corresponding specific activities in the soluble fraction showed no decline. 4. Stearoyl-CoA hydrolase in the microsomal fraction is inhibited (99%) by bovine serum albumin; this is in contrast with the microsomal fatty acid-chain-elongation system, which is stimulated 3.9-fold by albumin. Inhibition of stearoyl-CoA hydrolase does not stimulate stearoyl-CoA chain elongation. Therefore it does not appear likely that the decline in the specific activity of hydrolase during myelogenesis is responsible for the increased rate of fatty acid chain elongation. 5. It is suggested that the decline in specific activity of the microsomal hydrolase and to a lesser extent the increase in the specific activity of the ligase is directly related to the increased demand for long-chain acyl-CoA esters during myelogenesis as substrates in the biosynthesis of myelin lipids.

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BRAIN ACYL‐COENZYME A HYDROLASE: DISTRIBUTION, PURIFICATION AND PROPERTIES¹

Cited by 56 publications

References 25 publications

Induction of a Novel Long‐Chain Acyl‐CoA Hydrolase in Rat Liver by Administration of Peroxisome Proliferators

Induction of a Novel Long‐Chain Acyl‐CoA Hydrolase in Rat Liver by Administration of Peroxisome Proliferators

Short-chain fatty acid synthesis in brain. Subcellular localization and changes during development

The synthesis and hydrolysis of long-chain fatty acyl-coenzyme A thioesters by soluble and microsomal fractions from the brain of the developing rat

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BRAIN ACYL‐COENZYME A HYDROLASE: DISTRIBUTION, PURIFICATION AND PROPERTIES1

Cited by 56 publications

References 25 publications

Induction of a Novel Long‐Chain Acyl‐CoA Hydrolase in Rat Liver by Administration of Peroxisome Proliferators

Induction of a Novel Long‐Chain Acyl‐CoA Hydrolase in Rat Liver by Administration of Peroxisome Proliferators

Short-chain fatty acid synthesis in brain. Subcellular localization and changes during development

The synthesis and hydrolysis of long-chain fatty acyl-coenzyme A thioesters by soluble and microsomal fractions from the brain of the developing rat

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BRAIN ACYL‐COENZYME A HYDROLASE: DISTRIBUTION, PURIFICATION AND PROPERTIES¹