論文 - 黒木 勝久
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Rasool M., Bairam A., Gohal S., El Daibani A., Alherz F., Abunnaja M., Alatwi E., Kurogi K., Liu M.
Pharmacological Reports 71 ( 2 ) 257 - 265 2019年4月
記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：Pharmacological Reports
© 2018 Institute of Pharmacology, Polish Academy of Sciences Background: Non-opioid and opioid analgesics, as over-the-counter or prescribed medications, are widely used for the management of a diverse array of pathophysiological conditions. Previous studies have demonstrated the involvement of human cytosolic sulfotransferase (SULT) SULT1A1 in the sulfation of acetaminophen, O-desmethylnaproxen (O-DMN), and tapentadol. The current study was designed to investigate the impact of single nucleotide polymorphisms (SNPs) of the human SULT1A1 gene on the sulfation of these analgesic compounds by SULT1A1 allozymes. Methods: Human SULT1A1 genotypes were identified by database search. cDNAs corresponding to nine SULT1A1 nonsynonymous missense coding SNPs (cSNPs) were generated by site-directed mutagenesis. Recombinant wild-type and SULT1A1 allozymes were bacterially expressed and affinity-purified. Purified SULT1A1 allozymes were analyzed for sulfation activity using an established assay procedure. Results: Compared with the wild-type enzyme, SULT1A1 allozymes were shown to display differential sulfating activities toward three analgesic compounds, acetaminophen, O-desmethylnaproxen (O-DMN), and tapentadol, as well as the prototype substrate 4NP. Conclusion: Results obtained indicated clearly the impact of genetic polymorphisms on the drug-sulfation activity of SULT1A1 allozymes. Such information may contribute to a better understanding about the differential metabolism of acetaminophen, O-DMN, and tapentadol in individuals with different SULT1A1 genotypes.
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Kurogi K., Yoshihama M., Williams F., Kenmochi N., Sakakibara Y., Suiko M., Liu M.
Journal of Steroid Biochemistry and Molecular Biology 185 110 - 117 2019年1月
記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：Journal of Steroid Biochemistry and Molecular Biology
© 2018 Elsevier Ltd Steroid sulfatase (STS) plays an important role in the regulation of steroid hormones. Metabolism of steroid hormones in zebrafish has been investigated, but the action of steroid sulfatase remains unknown. In this study, a zebrafish sts was cloned, expressed, purified, and characterized in comparison with the orthologous human enzyme. Enzymatic assays demonstrated that similar to human STS, zebrafish Sts was most active in catalyzing the hydrolysis of estrone-sulfate and estradiol-sulfate, among five steroid sulfates tested as substrates. Kinetic analyses revealed that the Km values of zebrafish Sts and human STS differed with respective substrates, but the catalytic efficiency as reflected by the Vmax/Km appeared comparable, except for DHEA-sulfate with which zebrafish Sts appeared less efficient. While zebrafish Sts was catalytically active at 28 °C, the enzyme appeared more active at 37 °C and with similar Km values to those determined at 28 °C. Assays performed in the presence of different divalent cations showed that the activities of both zebrafish and human STSs were stimulated by Ca2+, Mg2+, and Mn2+, and inhibited by Zn+2 and Fe2+. EMATE and STX64, two known mammalian steroid sulafatase inhibitors, were shown to be capable of inhibiting the activity of zebrafish Sts. Collectively, the results obtained indicated that zebrafish Sts exhibited enzymatic characteristics comparable to the human STS, suggesting that the physiological function of STS may be conserved between zebrafish and humans.
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Abunnaja M., Alherz F., El Daibani A., Bairam A., Rasool M., Gohal S., Kurogi K., Suiko M., Sakakibara Y., Liu M.
Biochemistry and Cell Biology 96 ( 5 ) 655 - 662 2018年10月
記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：Biochemistry and Cell Biology
© 2018 Published by NRC Research Press. The cytosolic sulfotransferase (SULT) SULT2A1 is known to mediate the sulfation of DHEA as well as some other hydroxysteroids such as pregnenolone. The present study was designed to investigate how genetic polymorphisms of the human SULT2A1 gene may affect the sulfation of DHEA and pregnenolone. Online databases were systematically searched to identify human SULT2A1 single nucleotide polymorphisms (SNPs). Of the 98 SULT2A1 non-synonymous coding SNPs identified, seven were selected for further investigation. Site-directed mutagenesis was used to generate cDNAs encoding these seven SULT2A1 allozymes, which were expressed in BL21 Escherichia coli cells and purified by glutathione-Sepharose affinity chromatography. Enzymatic assays revealed that purified SULT2A1 allozymes displayed differential sulfating activity toward both DHEA and pregnenolone. Kinetic analyses showed further differential catalytic efficiency and substrate affinity of the SULT2A1 allozymes, in comparison with wild-type SULT2A1. These findings provided useful information concerning the effects of genetic polymorphisms on the sulfating activity of SULT2A1 allozymes.
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Alherz F., Abunnaja M., El Daibani A., Bairam A., Rasool M., Kurogi K., Sakakibara Y., Suiko M., Liu M.
Journal of Biochemistry 164 ( 3 ) 215 - 221 2018年9月
記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：Journal of Biochemistry
© The Author(s) 2018. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved. Sulphated cholesterol, like its unsulphated counterpart, is known to be biologically active and serves a myriad of biochemical/physiological functions. Of the 13 human cytosolic sulphotransferases (SULTs), SULT2B1b has been reported as the main enzyme responsible for the sulphation of cholesterol. As such, SULT2B1b may play the role as a key regulator of cholesterol metabolism. Variations in the sulphating activity of SULT2B1b may affect the sulphation of cholesterol and, consequently, the related physiological events. This study was designed to evaluate the impact of the genetic polymorphisms on the sulphation of cholesterol by SULT2B1b. Ten recombinant SULT2B1b allozymes were generated, expressed, and purified. Purified SULT2B1b allozymes were shown to display differential cholesterol-sulphating activities, compared with the wild-type enzyme. Kinetic studies revealed further their distinct substrate affinity and catalytic efficiency toward cholesterol. These findings showed clearly the impact of genetic polymorphisms on the cholesterolsulphating activity of SULT2B1b allozymes, which may underscore the differential metabolism of cholesterol in individuals with different SULT2B1b genotypes.
DOI： 10.1093/jb/mvy042
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Effects of Human Sulfotransferase 2A1 Genetic Polymorphisms 3 on the Sulfation of Tibolone 査読あり
Miller E., Zalzala M., Abunnaja M., Kurogi K., Sakakibara Y., Suiko M., Liu M.
European Journal of Drug Metabolism and Pharmacokinetics 43 ( 4 ) 415 - 421 2018年8月
記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：European Journal of Drug Metabolism and Pharmacokinetics
© 2018, Springer International Publishing AG, part of Springer Nature. Background and Objectives: Previous studies have demonstrated the metabolism of tibolone through sulfation, with the cytosolic sulfotransferase (SULT) SULT2A1 as the major responsible enzyme. The current study aimed to investigate how SULT2A1 genetic polymorphisms may affect the dehydroepiandrosterone (DHEA)- and tibolone-sulfating activity of SULT2A1. Methods: Site-directed mutagenesis was employed to generate cDNAs encoding ten different SULT2A1 allozymes. Recombinant SULT2A1 allozymes were expressed in BL21 E. coli cells, and purified using glutathione-sepharose affinity chromatography. An established sulfotransferase assay was used to analyze DHEA- and tibolone-sulfating activity of the purified SULT2A1 allozymes. Results: The nine human SULT2A1 allozymes plus the wild-type SULT2A1 were found to display differential sulfating activity toward DHEA and tibolone. Kinetic analysis revealed that different SULT2A1 allozymes exhibited differential substrate affinity and catalytic efficiency toward the two substrates tested. Conclusion: The results obtained provided useful information concerning the differential metabolism of tibolone through sulfation in individuals with different SULT2A1 genotypes.
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Shimohira T., Kurogi K., Liu M., Suiko M., Sakakibara Y.
Bioscience, Biotechnology and Biochemistry 82 ( 8 ) 1359 - 1365 2018年8月
記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：Bioscience, Biotechnology and Biochemistry
© 2018 Japan society for Bioscience, Biotechnology, and Agrochemistry. Members of the cytosolic sulfotransferase (SULT) SULT2A subfamily are known to be critically involved in the homeostasis of steroids and bile acids. SULT2A8, a 7α-hydroxyl bile acid-preferring mouse SULT, has been identified as the major enzyme responsible for the mouse-specific 7-O-sulfation of bile acids. Interestingly, SULT2A8 lacks a conservative catalytic His residue at position 99th. The catalytic mechanism underlying the SULT2A8-mediated 7-O-sulfation of bile acids thus remained unclear. In this study, we performed a mutational analysis in order to gain insight into this yet-unresolved issue. Results obtained revealed two amino acid residues, His48 and Leu99, that are unique to the mouse SULT2A8, but not other SULTs, are essential for its 7-O-sulfating activity toward bile acids. These findings suggested that substitutions of two amino acids, which might have occurred during the evolution of the mouse SULT2A8 gene, endowed mouse SULT2A8 the capacity to catalyze the 7-O-sulfation of bile acids.
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Bairam A., Rasool M., Alherz F., Abunnaja M., El Daibani A., Kurogi K., Liu M.
Archives of Biochemistry and Biophysics 648 44 - 52 2018年6月
記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：Archives of Biochemistry and Biophysics
© 2018 Elsevier Inc. Sulfoconjugation has been shown to be critically involved in the metabolism of acetaminophen (APAP), morphine, tapentadol and O-desmethyl tramadol (O-DMT). The objective of this study was to investigate the effects of single nucleotide polymorphisms (SNPs) of human SULT1A3 and SULT1A4 genes on the sulfating activity of SULT1A3 allozymes toward these analgesic compounds. Twelve non-synonymous coding SNPs (cSNPs) of SULT1A3/SULT1A4 were investigated, and the corresponding cDNAs were generated by site-directed mutagenesis. SULT1A3 allozymes, bacterially expressed and purified, exhibited differential sulfating activity toward each of the four analgesic compounds tested as substrates. Kinetic analyses of SULT1A3 allozymes further revealed significant differences in binding affinity and catalytic activity toward the four analgesic compounds. Collectively, the results derived from the current study showed clearly the impact of cSNPs of the coding genes, SULT1A3 and SULT1A4, on the sulfating activity of the coded SULT1A3 allozymes toward the tested analgesic compounds. These findings may have implications in the pharmacokinetics as well as the toxicity profiles of these analgesics administered in individuals with distinct SULT1A3 and/or SULT1A4 genotypes.
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Sulfation of catecholamines and serotonin by SULT1A3 allozymes 査読あり
Bairam A., Rasool M., Alherz F., Abunnaja M., El Daibani A., Gohal S., Kurogi K., Sakakibara Y., Suiko M., Liu M.
Biochemical Pharmacology 151 104 - 113 2018年5月
記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：Biochemical Pharmacology
© 2018 Elsevier Inc. Previous studies have demonstrated the involvement of sulfoconjugation in the metabolism of catecholamines and serotonin. The current study aimed to clarify the effects of single nucleotide polymorphisms (SNPs) of human SULT1A3 and SULT1A4 genes on the enzymatic characteristics of the sulfation of dopamine, epinephrine, norepinephrine and serotonin by SULT1A3 allozymes. Following a comprehensive search of different SULT1A3 and SULT1A4 genotypes, twelve non-synonymous (missense) coding SNPs (cSNPs) of SULT1A3/SULT1A4 were identified. cDNAs encoding the corresponding SULT1A3 allozymes, packaged in pGEX-2T vector were generated by site-directed mutagenesis. SULT1A3 allozymes were expressed, and purified. Purified SULT1A3 allozymes exhibited differential sulfating activity toward catecholamines and serotonin. Kinetic analyses demonstrated differences in both substrate affinity and catalytic efficiency of the SULT1A3 allozymes. Collectively, these findings provide useful information relevant to the differential metabolism of dopamine, epinephrine, norepinephrine and serotonin through sulfoconjugation in individuals having different SULT1A3/SULT1A4 genotypes.
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Radical scavenging effects of 1-naphthol, 2-naphthol, and their sulfate-conjugates 査読あり
Sugahara S, Fukuhara K, Tokunaga Y, Tsutsumi S, Ueda Y, Ono M, Kurogi K, Sakakibara Y, Suiko M, Liu MC, Yasuda S
The Journal of Toxicological Sciences. 43 ( 3 ) 213 - 221 2018年3月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Human Cytosolic Sulphotransferase SULT1C3: genomic analysis and functional characterization of splice variant SULT1C3a and SULT1C3d 査読あり
Kurogi K, Shimohira T, Kouriki-Nagatomo H, Zhang G, Miller ER, Sakakibara Y, Suiko M, Liu MC
Journal of Biochemistry 162 ( 6 ) 403 - 414 2017年12月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Identification and characterization of 5α-cyprinol-sulfating cytosolic sulfotransferases (Sults) in the zebrafish (Danio rerio) 査読あり
Kurogi K, Yoshihama M, Horton A, Schiefer IT, Krasowski MD, Hagey LR, Williams FE, Sakakibara Y, Kenmochi N, Suiko M, Liu MC
The Journal of Steroid Biochemistry and Molecular Biology. 174 120 - 127 2017年11月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Δ4-3-ketosteroids as a new class of substrates for the cytosolic sulfotransferases 査読あり
Hashiguchi T, Kurogi K, Shimohira T, Teramoto T, Liu MC, Suiko M, Sakakibara Y
Biochimica et Biophysica Acta 1861 ( 11PtA ) 2883 - 2890 2017年11月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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On the Molecular Basis Underlying the Metabolism of Tapentadol Through Sulfation 査読あり
Bairam AF, Rasool MI, Kurogi K, Liu MC
European Journal of Drug Metabolism and Pharmacokinetics 42 ( 5 ) 793 - 800 2017年10月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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On the sulfation of O-desmethyltramadol by human cytosolic sulfotransferases 査読あり
Rasool MI, Bairam AF, Kurogi K, Liu MC
Pharmacological Reports 69 ( 5 ) 953 - 958 2017年10月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Identification and characterization of the zebrafish glutathione S-transferase Pi-1 査読あり
Abunnaja MS, Kurogi K, Mohammed YI, Sakakibara Y, Suiko M, Hassoun EA, Liu MC
Journal of Biochemical and Molecular Toxicology 31 ( 10 ) e21948 - e21948 2017年10月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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食品成分の抗酸化能の複合的評価について 査読あり
近藤知巳，上橋朋佳，渡辺朋子，河野朝美，黒木勝久， 福井敬一，水光正仁，榊原陽一
日本食品科学工学会誌 64 ( 9 ) 457 - 463 2017年9月
記述言語：日本語 掲載種別：研究論文（学術雑誌）
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Sulfation of vitamin D3 -related compounds-identification and characterization of the responsible human cytosolic sulfotransferases 査読あり
Kurogi K, Sakakibara Y, Suiko M, Liu MC
FEBS letters 591 ( 16 ) 2417 - 2425 2017年8月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1 査読あり
Tanaka S, Nishiyori T, Kojo H, Otsubo R, Tsuruta M, Kurogi K, Liu MC, Suiko M, Sakakibara Y, Kakuta Y
Scientific Reports 7 ( 1 ) e8776 - e8776 2017年8月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Regioselective production of sulfated polyphenols using human cytosolic sulfotransferase-expressing Escherichia coli cells 査読あり
Shimohira T, Kurogi K, Hashiguchi T, Liu MC, Suiko M, Sakakibara Y
Journal of Bioscience and Bioengineering. 124 ( 1 ) 84 - 90 2017年7月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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A reappraisal of the 6-O-desmethylnaproxen-sulfating activity of the human cytosolic sulfotransferases 査読あり
Alherz FA, Almarghalani DA, Hussein NA, Kurogi K, Liu MC
Canadian Journal of Physiology and Pharmacology 95 ( 6 ) 647 - 651 2017年6月
記述言語：英語 掲載種別：研究論文（学術雑誌）