• Journal of the Korean Society of Food Science and Nutrition
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• v.18 no.1
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• pp.93-100
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• 1989

The effect of each azalea(Rhodoendron mucronulatum) pollen extract on phase I enzyme(aniline hydroxylase)was studied in this experiment. Serum aminotransferases were not changed in mice injected each azalea pollen extract, respectively compared to control group. The hepatic micros mal aniline hydroxylase activities in the presence of each azalea pollen extract were not affected in vitro. After treatment with azalea pollen water extract, hepatic microsomal aniline hydroxylase activity was increased with dose-dependent manner as compared to control group. The increment of hepatic microsmal aniline hydroxylase activity was more powerful by the treatment of water extract. As mice received aniline after pollen butanol and water extract-pretreatment once a day for 5 days, the blood and liver levels of aniline were decreased significantly.

• Biomolecules & Therapeutics
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• v.17 no.2
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• pp.188-198
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• 2009

This work was conducted to investigate the effect of bisphenol A (BPA) on estradiol (E2) 2-and 4-hydroxylase activities in the liver, kidney and lung tissues of male and female rats. After intraperitoneal administration of BPA to male and female rats for 4 days at 0, 10, and 50 mg/kg, the conversion of the substrate for hepatic and extra-hepatic enzyme activities was measured by GC/MSD. The result showed decreases of body and organ weights at 50 mg/kg BPA of male and female rats. Male hepatic E2 2-hydroxylase activity was inhibited by 68% at 10 mg/kg and by 82% at 50 mg/kg BPA. Female hepatic E2 2-hydroxylase activity was decreased by 46% at 10 mg/kg and by 56% at 50 mg/kg to the control. E2 4-hydroxylase was inhibited by 57 and 57% at 10 mg/kg and 54 and 78% at 50 mg/kg in liver of female and male, respectively. The urinary excretion rate of 2-hydroxyestradiol (2-OHE), androsterone and testosterone in urine of female rats with 50 mg/kg BPA were decreased significantly. The results showed that 50 mg/kg BPA was decreased E2 2-and 4-hydroxylase activities in liver, but not in other tissues. The urinary excretion rates of 2-OHE, androsterone and testosterone were also decreased. In liver, estrogenic enzyme activity were higher in male than female. These results suggest that BPA can disrupt estrogen metabolism by suppressing E2 2-and 4-hydroxylase activities in the liver of male and female rats.

• Clinical and Experimental Reproductive Medicine
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• v.42 no.2
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• pp.72-76
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• 2015

$17{\alpha}$-hydroxylase and 17,20-lyase are enzymes encoded by the CYP17A1 gene and are required for the synthesis of sex steroids and cortisol. In $17{\alpha}$-hydroxylase deficiency, there are low blood levels of estrogens, androgens, and cortisol, and resultant compensatory increases in adrenocorticotrophic hormone that stimulate the production of 11-deoxycorticosterone and corticosterone. In turn, the excessive levels of mineralocorticoids lead to volume expansion and hypertension. Females with $17{\alpha}$-hydroxylase deficiency are characterized by primary amenorrhea and delayed puberty, with accompanying hypertension. Affected males usually have female external genitalia, a blind vagina, and intra-abdominal testes. The treatment of this disorder is centered on glucocorticoid and sex steroid replacement. In patients with $17{\alpha}$-hydroxylase deficiency who are being raised as females, estrogen should be supplemented, while genetically female patients with a uterus should also receive progesterone supplementation. Here, we report a case of a 21-year-old female with $17{\alpha}$-hydroxylase deficiency who had received inadequate treatment for a prolonged period of time. We also include a brief review of the recent literature on this disorder.

• Preventive Nutrition and Food Science
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• v.13 no.2
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• pp.61-65
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• 2008

To evaluate the effect of ground cherry extract on the activity of aniline hydroxylase, we gave ground cherry extract in doses of 100, 200 or 400 mg/kg i.p to mice for 1, 2 or 4 days. The aniline hydroxylase activity in the group treated with ground cherry extract increased in a dose dependant manner in all experimental groups compared with the control group, and was significantly higher in the group treated with ground cherry extract at a dose of 200 mg/kg, which also exhibited a time dependant increase over 4 days. Enzyzme kinetic analysis was performed for hepatic aniline hydroxylase activity in the group treated with 200 mg/kg for 4 days. There was no change of the Km values for aniline hydroxylase between the experimental group and the control group, but the Vmax values for aniline hydroxylase was 21% lower in the experimental group compared with the control. The experimental group also showed lower lipid peroxide and reduced glutathione content, and there were no significant difference in serum alanine aminotransferase activity between the experimental group and the control. Aniline was injected into both the experimental group mice treated with ground cherry extract at a dose of 200 mg/kg for 4 days and the control group, and then the level of blood aniline was assayed at 1hr. The level of blood aniline was lower in the experimental than the control group. This study suggests that ground cherry extract induces hepatic aniline hydroxylase activity and might accelerate the scavenging system of reactive oxygen species. It is likely that ground cherry extract influences the metabolism of xenobiotics by activating AH activity substituted for CYP2E1.

• Microbiology and Biotechnology Letters
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• v.26 no.4
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• pp.365-368
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• 1998

The aklavinone 11-hydroxylase which was overexpressed using T7 promoter in E. coli could be detected in SDS-PAGE only in insoluble precipitate without any detectable enzyme activity. The insoluble enzyme was solubilized in 6M guanidine$.$HCl solution and their refolding ability was tested under various conditions. When the enzymatic activity was checked by the bioconversion experiment, stepwise dialysis against 6M, 3M, 1M guanidine$.$HCl and finally 100 mM potassium phosphate buffer of the solubilized protein gave the best bioconversion efficiency. The aklavinone 11-hydroxylase showed its enzymatic activity in the reaction buffer containing NADPH with vigorous shaking. The enzymatic activity was lost during partial purification and regained by the addition of crude extract of S. lividans in the reaction mixture. This effect was confirmed to due to some low-molecular weight component(s) in the crude extract, because the addition of dialyzed crude extract could not recover the enzymatic activity.

• Journal of Microbiology and Biotechnology
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• v.16 no.9
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• pp.1468-1471
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• 2006

The last step in L-carnitine biosynthesis in eukaryotic organisms is mediated by ${\gamma}$-butyrobetaine hydroxylase (EC1.14.11.1), a dioxygenase that converts ${\gamma}$-butyrobetaine to L-carnitine. This enzyme was previously identified from rat liver and humans, and the peptide sequence of human ${\gamma}$-butyrobetaine hydroxylase was used to search the Neurospora crassa genome database, which led to an identification of an open reading frame (ORF) consisting of 1,407 bp encoding a polypeptide of 468 amino acids. When this protein was expressed in Saccharomyces cerevisiae, the crude cell-free extract exhibited ${\gamma}$-butyrobetaine hydroxylase activity.

• Biotechnology and Bioprocess Engineering:BBE
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• v.5 no.1
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• pp.61-64
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• 2000

A series of 5-oxaproline peptide derivatives was synthesized and evaluated for its ability to inhibit the prolyl 4-hydroxylase in vitro. Structure-activity studies show that the 5-oxaproline sequences, prepared by the 1,3-dipolar cycloaddition of the C-methoxycarbonyl-N-mannosyl nitrone in the presence of the ethylene, are more active than the corresponding proline derivatives. Prolyl 4-hydroxylase belongs to a family of $Fe^{2+}-dependent$ dioxygenase, which catalyzes the formation of 4-hydroxyproline in collagens by the hydroxylation of proline residues in -Gly-Xaa-Pro-Gly- of procollagen chains. In this paper we discover the more selective N-Cbz-Gly-Phe-Pro-Gly-OEt $(K_m\;=\;520\;{\mu}M)$ sequences which are showed stronger binding than others in vitro. Therefore, we set out to investigate constrained tetrapeptide that was designed to mimic the proline structure of pep tides for the development of prolyl 4-hydroxylase inhibitor. From this result, we found that the most potent inhibitor is N-Dansyl-Gly-Phe-5-oxaPro-Gly-OEt $(K_i\;=\;1.6\;{\mu}M)$. This has prompted attempts to develop drugs which inhibit collagen synthesis. Prolyl 4-hydroxylase would seem a particularly suitable target for antifibrotic therapy.

• Animal cells and systems
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• v.9 no.1
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• pp.19-25
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• 2005

This study was conducted to determine the effect of dietary salt on the synthesis of glucocorticoids in the adrenal cortex of mice. Mice had ad libitum access to 3% sodium chloride as the only drinking fluid (high salt diet) for either 4 days or 4 weeks. Adrenocortical expression of cytochrome P450 11beta-hydroxylase, a major regulatory enzyme in the biosynthesis of glucocorticoids, was examined by immunohistochemistry and western blot analysis. Ultrastructure of adrenocortical cell and plasma level of corticosterone were analyzed as well. Size and density of lipid droplets in the cortical cell were increased by high salt diet. Four days of high salt diet decreased P450 11beta-hydroxylase in the adrenal cortex, but 4 weeks increased it. Plasma level of corticosterone changed in parallel with the Cortical level of P450 11 beta-hydroxylase. These results suggest that high salt diet may modulate the biosynthesis of glucocorticoids, at least partly, via regulating the expression of P450 11beta-hydroxylase in adrenocortical cells.

• Horticultural Science & Technology
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• v.29 no.3
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• pp.267-272
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• 2011

Several reports indicated that astaxanthin and zeaxanthin have more active anticancer activity than pro-vitamin A carotenes. ${\beta}$-carotene hydroxylase is a key enzyme to synthesize zeaxanthin and astaxanthin in carotenoids biosynthesis pathway. We isolated the ChyB gene encoding ${\beta}$-carotene hydroxylase from tomato leaves. The ChyB gene (1.5Kbp) fragment was cloned into the binary vector and designated to pIG121-ChyB-tom. Agrobacterium-mediated infiltration was used for transient assay in Nicotiana benthamiana. Leaf samples were collected 0, 1, 2, 3 days after infiltration (DAI). RT-PCR result showed that the expression of ${\beta}$-carotene hydroxylase transcripts was not detected in control (0DAI), but its expression was detected after 1 DPI and increased later on. When the activity of ${\beta}$-carotene hydroxylase was measured, the 1,1-diphenyl-pricryl hydrazyl (DPPH) radical scavenging activity (27%) at 2 DAI was significantly higher than that (21%) at 0 DAI. These results indicated that anti-oxidant activity dramatically increased at 2 DAI in tobacco leaves was due to over expression of tomato ${\beta}$-carotene hydroxylase. These results can be the foundation to develop tomato cultivars with high oxy-carotenoids content using the ChyB gene transformation.

• The Korean Journal of Pharmacology
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• v.27 no.1
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• pp.1-5
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• 1991

We studied changes in the hypothalamic norepinephrine(NE) metabolism in streptozotocin (STZ)-induced diabetic rats by measuring basal NE levels, turnover rate of NE, and in vivo tyrosine hydroxylase activities. Basal NE level did not change significantly upto 4 weeks after the establishment of diabetes with STZ(60 mg/kg, iv). But turnover rate of NE decreased to 62% of control rate(P<0.01), and in vivo tyrosine hydroxylase activities decreased to 32% of control level(P<0.05) at one week of diabetes. From these results, we concluded that, of the three parameters measured, in vive tyrosine hydroxylase activity is the most sensitive index of altered hypothalamic NE metabloism in STZ-induced diabetic rats.