• Proceedings of the Korean Society of Developmental Biology Conference
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• 2003.10a
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• pp.96-96
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• 2003

Acyl-CoA synthetase 4는 생쥐에 있어서 거의 모든 조직에서 발현하며 아라키돈산에 특이적인 효소이다. 아라키돈산은 세포막의 인지질로부터 cPLA2에 의하여 유리되고 cyclooxygenase-1, -2에 의하여 eicosanoid로 변환된다. 이렇게 생산된 prostaglandin과 같은 eicosanoid는 배란, 수정, 임신에 있어서 중요한 기능을 수행하고 있다. 그러나 세포막으로부터 유리된 아라키돈산은 acyl-CoA synthetase 4에 의하여 다시 세포막으로 재에스테르화되어 eicosaniod의 생산을 조절하는 것으로 생각되어지고 있다. 또한 acyl-CoA synthetase 4 유전자 한쪽이 knock-out된 heterozygote mouse에서는 사산, 유산과 난소에 있어서 황체 수의 증가 등을 보고하고 있다. 그러므로 본 연구에서는 정상 생쥐 (C57BL/6) 임신 기간 중 acyl-CoA synthetase 4 유전자의 발현을 확인하기 위하여 자궁, 난소, 태아에서 RT-PCR을 수행하였다. 또한 cPLA2, cyclooxygenase-1, cyclooxygenase-2 유전자의 발현 양상을 분석하여 eicosanoid 생산에 관여하는 유전자 상호간의 발현 을 확인하였다. acyl-CoA synthetase 4는 임신 0 day에서부터 19.5 day까지 자궁과 난소에서 모두 발현하고 있었다. 또한 5.5 day에서부터 19.5 day까지의 태아에서도 그 발현이 확인되었다. 그리고 cPLA2와 cyclooxygenase-1은 acyl-CoA synthetase 4와 유사한 양상을 보였으나 cyclooxygenase-2는 임신기간 중의 자궁, 난소, 태아에서 전혀 발현하지 않았다. 그러므로 임신 중 생쥐 자궁, 난소, 태아에 있어서 eicosanoid 생산에는 cPLA2, cyclooxygenase-1, acyl-CoA synthetase 4 유전자가 관여하고 있는 것으로 생각된다.

• BMB Reports
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• v.33 no.4
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• pp.332-336
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• 2000

Phenazine 1-carboxylic acid (PCA) is an antifungal antibiotic isolated from a culture filtrate of Bacillus sp. B-6 producing an acyl CoA synthetase inhibitor. This antibiotic is reported as an inhibitor of an acyl CoA synthetase from Pseudomonas sp.. Bacillus sp. B-6 was resistant to PCA up to 350 ${\mu}g/ml$. We investigated the mechanism of the resistance of Bacillus sp. B-6 to PCA. The rate of growth in a medium containing up to 100 ${\mu}g/ml$ was as rapid as the PCA-free medium. At a PCA concentration of 300 ${\mu}g/ml$, the growth rate was more than half that of the control. In this work, we purified acyl CoA synthetase from Bacillus sp. B-6 and found that this acyl CoA synthetase was much less sensitive to PCA than the acyl CoA synthetase from other source. These findings suggested that the insensitivity of Bacillus sp. B-6 acyl CoA synthetase plays an important role in the PCA resistance of this bacterium.

• YAKHAK HOEJI
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• v.40 no.6
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• pp.713-719
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• 1996

Identification of soil microorganism strain B-6. a producer of acyl CoA synthetase inhibitor, based on its morphological, physiological, biochemical and chemotaxonomical charact eristics was performed. The strain B-6 was identified as Bacillus subtilis. Ihe acyl CoA synthetase inhibitor produced by this strain was highly achieved in fermentation medium that contained glucose 1.0%, soluble starch 1.0%, NH$_4$Cl 0.3%, oatmeal 1.0%, pharmamedia 1.0%, basic magnesium carbonate 0.5%. pH 7.5 at 30$^{\circ}$C for 7 days. The optimal pH and temperature for growth were 9.0 and 30$^{\circ}$C, respectively. Butanol extract of culture filterate of strain B-6 in acyl CoA synthetase inhibitor production medium containing corn steep liquor exhibited high acyl CoA synthetase inhibitor activity and antimicrobial activity against C. albicans. But chloroform extract of culture filterate of strain B-6 in medium containing NH$_4$Cl, ($NH_4)_2SO_4$ or urea instead of corn steep liquor exhibited higher antimicrobial activity against C. albicans than that of butanol extract.

• Reproductive and Developmental Biology
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• v.28 no.2
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• pp.89-94
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• 2004

This study was conducted to determine expression of acyl-CoA synthetase 4(ACS4), which is involved in converts arachidonic acid to postaglandins, in the mouse uterus during pregnancy. In arachidonic acid metabolism, acyl-CoA synthetase plays a key role in the esterification of free arachidonic acid into membrane phospholipids. Following its release by the action of calcium dependent phospholipases, free arachidonic acid is believed to be rapidly converted to arachidonoyl-CoA and reesterified into phospholipids in order to prevent excessive synthesis of prostaglandins. Here we demonstrate that ACS4 gene are differentially regulated in the peri-implatation mouse uterus. During the preimplantation period(days 0.5∼3.5), the ACS4 gene was expressed in the uterus until day 3.5 after which the expression was downregulated. The expression of cPLA2, COX1, and COX2 gene was similar to that of ACS4 gene in the preimplantation periods. However expression levels of COX1 gene show much variation on the various days of pregnancy examined. These data, suggest that ACS4 expression in preimplantation period is involved in initial attachment reaction with cPLA2, COX1, and COX2 gene.

• Korean Journal of Animal Reproduction
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• v.24 no.4
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• pp.339-341
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• 2000

In mammals, fatty acid utilization is initiated by activation of fatty acid, catalyzed by acyl-CoA synthetase(ACS, EC6.2.1.3). This enzyme reaction is essential in fatty acid metabolism, since mammalian fatty acid synthetase contains a specific thioesterase to produce fatty acid as th $\varepsilon$ final reaction product. Acyl-CoA, the product of ACS, is utilized in various metabolic pathways including membrane biogenesis, energy production and fat deposition. (omitted)

• Reproductive and Developmental Biology
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• v.35 no.3
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• pp.215-219
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• 2011

Acyl-CoA synthetase 4(ACSL4) is an arachidonate-preferring enzyme abundant in steroidogenic tissues and postulated to modulate eicosanoid production. The human and mouse ACSL4 gene are mapped on chromosome X. The female mice heterozygous for ACSL4 deficiency became pregnant less frequent1y and produced small litters, with 40% of embryos surviving gestation. In this study, we examined the regulation of ACS4 by estradiol-$17{\beta}$ and progesterone (P4) in the human endometrial cancer cell line HTB-1B. ACSL4 mRNA was increased in a dose-dependent manner. Also, expression of ACSL4 gene was up-regulated in a time-dependent manner in HTB-1B cells. However, combined treatment with progesterone and estradiol-$17{\beta}$ modestly decreased the levels of ACS4L mRNA as compared with the estradiol-$17{\beta}$ and progesterone respectively. Overall, these results suggest that the ACSL4 gene is regulated by progesterone and estradiol-$17{\beta}$ in the HTB-1B cells.

• Proceedings of the KSAR Conference
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• 2000.10a
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• pp.3-4
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• 2000

The synthesis of acyl-CoA catalyzed by acyl-CoA synthetase (ACS, EC 6.2.1.3) from fatty acid, ATP, and CoA is a crucial reaction in mammalian fatty acid metabolism. In arachidonate metabolism, acyl-CoA synthetase(ACS) plays a key role in the esterification of free arachidonate into membrane phospholipids. Following its release by the action of calcium dependent phospholipase, free arachidonate is believed to be rapidly converted to arachidonoyl-CoA and reesterified into phospholipids in order to prevent excessive synthesis of eicosanoids. In previous studies, we have characterized five ACSs (designated as ACS1-5) with different tissue distribution. ACS1, ACS2, and ACS5 are similar in structure and fatty acid preference, and completely different from ACS3 and ACS4. The latter are arachidonate-preferring enzymes closely related in structure but expressed in different tissues: ACS3 mRNA is highly expressed in the brain and the mRNA for ACS4 is expressed in steroidogenic tissues including adrenal gland, ovary, and testis. To learn more about the potential function of ACS4 in arachidonate metabolism, we have produced knock-out mice for ACS4 gene. ACS4+/- females become pregnant less frequently and produce small litters with extremely low transmission of the disrupted alleles. Striking morphological changes including extremely enlarged uterine filled with numerous proliferative cysts of various size were detected in ACS4+/- females. Furthermore, marked accumulation of prostaglandins were seen in the uterus of heterozygous females. These results indicate that ACS4 is critical for the uterine arachidonate metabolism and heterozygous disruption of its gene lead to impaired pregnancy.

• Proceedings of the KSAR Conference
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• 2004.06a
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• pp.225-225
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• 2004

Acyl-CoA synthetase 4(ACS4) is an arachidonate-preferring enzyme aboundant in steroidogenic tissues and postulated to modulate eicosanoid production. Most of arachidonate present in cells is esterified predominantly in phospholipids. After its release by the action of calcium-dependent phospholipases, arachidonate can be converted to prostaglandins, thromboxanes, and leukotrenes via the cyclooxygenas and lipoxygenase pathways, respectively, depending on the cell type.(omitted)

• Proceedings of the Korean Society of Embryo Transfer Conference
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• 2003.10a
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• pp.96-96
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• 2003

• Journal of Nutrition and Health
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• v.36 no.4
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• pp.376-381
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• 2003

Acyl-CoA synthetase 4 (ACS4) is an arachidonate-preferring enzyme abundant in steroidogenic tissues. We examined ACS4 in rat liver, which contains a variety of pathways that use acyl-CoAs, in order to determine subcellular locations. We demonstrate that ACS4 protein was present most abundantly in the mitochondria and to a much lesser extent in the peroxisomes and microsomes. To determined the dietary effects on the level of ACS4 mRNA, northern blotting was carried out using total RNA from the livers of adult male rats fed various diets. Fasting, high fat diet, and fat-free high sucrose diet increased the hepatic level of ACS4 mRNA approximately 2-fold. Furthermore, the levels of ACS4 mRNA were induced by DEHP[Di- (2-ethylhexyl) phthalate]. These data suggest that ACS4 expression in the liver is regulated with a variety of pathways, including $\beta$-oxidation, hormone, and insulin.