論文 - 黒木 勝久
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Kurogi K., Sakakibara Y., Hashiguchi T., Kakuta Y., Kanekiyo M., Teramoto T., Fukushima T., Bamba T., Matsumoto J., Fukusaki E., Kataoka H., Suiko M.
PNAS Nexus 3 ( 3 ) 2024年3月
担当区分：筆頭著者, 責任著者 記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：PNAS Nexus
Cytosolic sulfotransferases (SULTs) are cytosolic enzymes that catalyze the transfer of sulfonate group to key endogenous compounds, altering the physiological functions of their substrates. SULT enzymes catalyze the O-sulfonation of hydroxy groups or N-sulfonation of amino groups of substrate compounds. In this study, we report the discovery of C-sulfonation of α,β-unsaturated carbonyl groups mediated by a new SULT enzyme, SULT7A1, and human SULT1C4. Enzymatic assays revealed that SULT7A1 is capable of transferring the sulfonate group from 3′-phosphoadenosine 5′-phosphosulfate to the α-carbon of α,β-unsaturated carbonyl-containing compounds, including cyclopentenone prostaglandins as representative endogenous substrates. Structural analyses of SULT7A1 suggest that the C-sulfonation reaction is catalyzed by a novel mechanism mediated by His and Cys residues in the active site. Ligand-activity assays demonstrated that sulfonated 15-deoxy prostaglandin J2 exhibits antagonist activity against the prostaglandin receptor EP2 and the prostacyclin receptor IP. Modification of α,β-unsaturated carbonyl groups via the new prostaglandin-sulfonating enzyme, SULT7A1, may regulate the physiological function of prostaglandins in the gut. Discovery of C-sulfonation of α,β-unsaturated carbonyl groups will broaden the spectrum of potential substrates and physiological functions of SULTs.
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Iwamoto W., Ikeda T., Nishikawa H., Hirano M., Kinoshita H., Ono M., Kurogi K., Sakakibara Y., Suiko M., Yasuda S.
Bioscience, Biotechnology and Biochemistry 88 ( 9 ) 1081 - 1089 2024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：Bioscience, Biotechnology and Biochemistry
Indoxyl sulfate (IS), a uremic toxin, is a physiologically active sulfated metabolite, specifically in kidney failure patients. Our previous studies have shown that IS downregulates phagocytic immune function in a differentiated HL-60 human macrophage cell model. However, it remains unclear whether IS exerts similar effects on macrophage function in other cell types or in lipopolysaccharide (LPS)-sensitive immune cell models. Therefore, this study aimed to investigate the effects of IS on intracellular oxidation levels and phagocytic activity in a differentiated U937 human macrophage cell model, both in the absence and presence of LPS. Our results demonstrated that IS significantly increases intracellular oxidation levels and decreases phagocytic activity, particularly in cells activated by LPS. Furthermore, we found that 2-acetylphenothiazine, an NADH oxidase inhibitor, attenuates the effects of IS in LPS-activated macrophage cells. Representative antioxidants, trolox, α-tocopherol, and ascorbic acid, significantly mitigated the effects of IS on the macrophages responding to LPS.
DOI： 10.1093/bbb/zbae077
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Evolution and multiple functions of sulfonation and cytosolic sulfotransferases across species 査読あり 国際誌
Kurogi K., Suiko M., Sakakibara Y.
Biosci Biotechnol Biochem 88 ( 4 ) 368 - 380 2024年3月
担当区分：筆頭著者, 責任著者 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
Organisms have conversion systems for sulfate ion to take advantage of the chemical features. The use of biologically converted sulfonucleotides varies in an evolutionary manner, with the universal use being that of sulfonate donors. Sulfotransferases have the ability to transfer the sulfonate group of 3'-phosphoadenosine 5'-phosphosulfate to a variety of molecules. Cytosolic sulfotransferases (SULTs) play a role in the metabolism of low-molecular-weight compounds in response to the host organism's living environment. This review will address the diverse functions of the SULT in evolution, including recent findings. In addition to the diversity of vertebrate sulfotransferases, the molecular aspects and recent studies on bacterial and plant sulfotransferases are also addressed.
DOI： 10.1093/bbb/zbae008
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高速液体クロマトグラフィーを用いたアセトアミノフェン O- 硫酸体とチロシン O- 硫酸体の UV 検出による測定法 査読あり
森田千紘、元山優作、谷口玲央真、上田裕人、木下英樹、小野政輝、黒木勝久、榊原陽一、水光正仁、安田伸
東海大学紀要 42 1 - 8 2023年3月
記述言語：日本語 掲載種別：研究論文（大学，研究機関等紀要）
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プロテオミクス基盤技術を活用したブランド豚肉と個体識別の検討 招待あり 査読あり
黒木 勝久, 秋山 克樹, 榊原 陽一
電気泳動 66 ( 2 ) 97 - 102 2022年11月
担当区分：筆頭著者 記述言語：日本語 掲載種別：研究論文（学術雑誌） 出版者・発行元：日本電気泳動学会
黒毛和牛やブランド豚肉を始めとした高付加価値食肉は系統種の交配と飼育条件の工夫により開発される．食肉偽装などの問題もあり，遺伝的・環境的要因を一度に解析できる手法を確立することで，効率的な優良育種とブランド肉の偽装鑑定への応用に期待できる．その一つとして，我々はプロテオミクス基盤技術を活用した解析を行っている．本稿では，豚肉に焦点を当てブランド肉鑑定および優良種豚選抜法への可能性を二次元電気泳動と質量分析計を用いて検討した結果を報告する．プロテオーム解析の結果，ブランド豚肉では解糖系に関するタンパク発現が大きく変動しており，環境要因が糖代謝に与える影響を見出すことが出来たと共に，ブランド豚肉を判別できるマーカータンパク質・ペプチドの候補を見出すことが出来た．さらに，優良育種に用いられるデュロック種と大ヨークシャー種の血清サンプルを用いた解析より，従来の系統的な選抜方法とは異なる新たな個体識別方法への可能性が示された．
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Kurogi K., Cao Y., Segawa K., Sakakibara Y., Suiko M., Uetrecht J., Liu M.C.
Biochemical Pharmacology 204 2022年10月
担当区分：筆頭著者 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
Nevirapine (NVP) is an effective drug for the treatment of HIV infections, but its use is limited by a high incidence of severe skin rash and liver injury. 12-Hydroxynevirapine (12-OH-NVP) is the major metabolite of nevirapine. There is strong evidence that the sulfate of 12-OH-NVP is responsible for the skin rash. While several cytosolic sulfotransferases (SULTs) have been shown to be capable of sulfating 12-OH-NVP, the exact mechanism of sulfation in vivo is unclear. The current study aimed to clarify human SULT(s) and human organs that are capable of sulfating 12-OH-NVP and investigate the metabolic sulfation of 12-OH-NVP using cultured HepG2 human hepatoma cells. Enzymatic assays revealed that of the thirteen human SULTs, SULT1A1 and SULT2A1 displayed strong 12-OH-NVP-sulfating activity. 1-Phenyl-1-hexanol (PHHX), which applied topically prevents the skin rash in rats, inhibited 12-OH-NVP sulfation by SULT1A1 and SULT2A1, implying the involvement of these two enzymes in the sulfation of 12-OH-NVP in vivo. Among five human organ cytosols analyzed, liver cytosol displayed the strongest 12-OH-NVP-sulfating activity, while a low but significant activity was detected with skin cytosol. Cultured HepG2 cells were shown to be capable of sulfating 12-OH-NVP. The effects of genetic polymorphisms of SULT1A1 and SULT2A1 genes on the sulfation of 12-OH-NVP by SULT1A1 and SULT2A1 allozymes were investigated. Two SULT1A1 allozymes, Arg37Asp and Met223Val, showed no detectable 12-OH-NVP-sulfating activity, while a SULT2A1 allozyme, Met57Thr, displayed significantly higher 12-OH-NVP-sulfating activity compared with the wild-type enzyme. Collectively, these results contribute to a better understanding of the involvement of sulfation in NVP-induced skin rash and provide clues to the possible role of SULT genetic polymorphisms in the risk of this adverse reaction.
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Morita C., Tokunaga Y., Ueda Y., Ono M., Kinoshita H., Kurogi K., Sakakibara Y., Suiko M., Liu M.C., Yasuda S.
Journal of Toxicological Sciences 47 ( 10 ) 421 - 428 2022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：Journal of Toxicological Sciences
Acetaminophen (APAP) and p-aminophenol (p-AP) are the analogous simple phenolic compounds that undergo sulfate conjugation (sulfation) by cytosolic sulfotransferases. Sulfation is gener-ally thought to lead to the inactivation and disposal of endogenous as well as xenobiotic compounds. This study aimed to investigate the antioxidative effects of O-sulfated form of APAP and p-AP, i.e., APAPS and p-APS, in comparison with their unsulfated counterparts. Using a 1,1-diphenyl-2-picrylhydrazyl radical scavenging assay, the antioxidant capacity of APAPS was shown to be approximately 126-times low-er than that of APAP. In contrast, p-APS displayed comparable activity as unsulfated p-AP. Similar trends concerning the suppressive effects of these chemicals on cellular O-2 radical generation were found using an activated granulocytic neutrophil cell model. Collectively, these results indicated that, depending on the presence of an additional “active site”, sulfation may not always decrease the antioxidant activities of phenolic compounds.
DOI： 10.2131/jts.47.421
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Yamamoto K., Yamada N., Endo S., Kurogi K., Sakakibara Y., Suiko M.
PLoS ONE 17 ( 8 August ) 2022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：PLoS ONE
Polyphenols in plants are important for defense responses against microorganisms, insect herbivory, and control of feeding. Owing to their antioxidant, anti-cancer, and anti-inflammatory activities, their importance in human nutrition has been acknowledged. However, metabolism of polyphenols derived from mulberry leaves in silkworms (Bombyx mori) remains unclear. Sulfotransferases (SULT) are involved in the metabolism of xenobiotics and endogenous compounds. The purpose of this study is to investigate the metabolic mechanism of polyphenols mediated by B. mori SULT. Here, we identified a novel SULT in silkworms (herein, swSULT ST3). Recombinant swSULT ST3 overexpressed in Escherichia coli effectively sulfated polyphenols present in mulberry leaves. swSULT ST3 showed high specific activity toward genistein among the polyphenols. Genistein-7-sulfate was produced by the activity of swSULT ST3. Higher expression of swSULT ST3 mRNA was observed in the midgut and fat body than in the hemocytes, testis, ovary, and silk gland. Polyphenols inhibited the aldo-keto reductase detoxification of reactive aldehydes from mulberry leaves, and the most noticeable inhibition was observed with genistein. Our results suggest that swSULT ST3 plays a role in the detoxification of polyphenols, including genistein, and contributes to the effects of aldo-keto reductase in the midgut of silkworms. This study provides new insight into the functions of SULTs and the molecular mechanism responsible for host plant selection in lepidopteran insects.
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Acetaminophen 硫酸体の有機合成 査読あり
森田千紘・谷口玲央真・吉田実央・德永祐希・木下英樹 小野政輝・黒木勝久・榊原陽一・水光正仁・安田伸
東海大学紀要 41 39 - 46 2022年3月
記述言語：日本語 掲載種別：研究論文（大学，研究機関等紀要）
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Kurogi K., Manabe Y., Liu M.C., Suiko M., Sakakibara Y.
Bioscience, Biotechnology and Biochemistry 85 ( 10 ) 2113 - 2120 2021年9月
担当区分：筆頭著者, 責任著者 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
Cytosolic sulfotransferase SULT1C subfamily is one of the most flexible gene subfamilies during mammalian evolution. The physiological functions of SULT1C enzymes still remain to be fully understood. In this study, common marmoset (Callithrix jacchus), a promising primate animal model, was used to investigate the functional relevance of the SULT1C subfamily. Gene database search revealed 3 intact SULT1C genes and a pseudogene in its genome. These 4 genes were named SULT1C1, SULT1C2, SULT1C3P, and SULT1C5, according to the sequence homology and gene location. Since SULT1C5 is the orthologous gene for human SULT1C2P, we propose, here, to revisit the designation of human SULT1C2P to SULT1C5P. Purified recombinant SULT1C enzymes showed sulfating activities toward a variety of xenobiotic compounds and thyroid hormones. Kinetic analysis revealed high catalytic activities of SULT1C1 and SULT1C5 for 3,3′-T2. It appears therefore that SULT1C isoforms may play a role in the thyroid hormone metabolism in common marmoset.
DOI： 10.1093/bbb/zbab141
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Effects of genetic polymorphisms on the sulfation of doxorubicin by human SULT1C4 allozymes 査読あり 国際共著
Gohal S.A., Rasool M.I., Bairam A.F., Alatwi E.S., Alherz F.A., Abunnaja M.S., El Daibani A.A., Kurogi K., Liu M.C.
Journal of Biochemistry 170 ( 3 ) 419 - 426 2021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
Doxorubicin is a chemotherapeutic drug widely utilized in cancer treatment. An enzyme critical to doxorubicin metabolism is the cytosolic sulfotransferase (SULT) SULT1C4. This study investigated the functional impact of SULT1C4 single nucleotide polymorphisms (SNPs) on the sulfation of doxorubicin by SULT1C4 allozymes. A comprehensive database search was performed to identify various SULT1C4 SNPs. Ten nonsynonymous SULT1C4 SNPs were selected, and the corresponding cDNAs, packaged in pGEX-2TK expression vector, were generated via site-directed mutagenesis. Respective SULT1C4 allozymes were bacterially expressed and purified by affinity chromatography. Purified SULT1C4 allozymes, in comparison with the wild-type enzyme, were analysed for sulphating activities towards doxorubicin and 4-nitrophenol, a prototype substrate. Results obtained showed clearly differential doxorubicin-sulphating activity of SULT1C4 allozymes, implying differential metabolism of doxorubicin through sulfation in individuals with distinct SULT1C4 genotypes.
DOI： 10.1093/jb/mvab055
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The crystal structure of mouse SULT2A8 reveals the mechanism of 7α-hydroxyl, bile acid sulfation 査読あり
Teramoto T., Nishio T., Kurogi K., Sakakibara Y., Kakuta Y.
Biochemical and Biophysical Research Communications 562 15 - 20 2021年7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 and Biophysical Research Communications
Bile acids play essential roles in facilitating the intestinal absorption of lipophilic nutrients as well as regulation of glucose, lipid, and energy homeostasis via activation of some receptors. Bile acids are cytotoxic, and consequently their concentrations are tightly controlled. A critical pathway for bile acid elimination and detoxification is sulfation. The pattern of bile acid sulfation differs by species. Sulfation preferentially occurs at the 3α-OH of bile acids in humans, but at the 7α-OH in mice. A recent study identified mouse cytosolic sulfotransferase 2A8 (mSULT2A8) as the major hepatic 7α-hydroxyl bile acid-sulfating enzyme. To elucidate the 7α-OH specific sulfation mechanism of mSULT2A8, instead of 3α-OH specific sulfation in humans, we determined a crystal structure of mSULT2A8 in complex with cholic acid, a major bile acid, and 3′-phosphoadenosine-5′-phosphate, the sulfate donor product. Our study shows that bile acid-binding mode of mSULT2A8 and how the enzyme holds the 7α-OH group of bile acids at the catalytic center, revealing that the mechanism underlying 7α-OH specific sulfation. The structure shows the substrate binds to mSULT2A8 in an orientation perpendicular to that of human 3α-hydroxyl bile acid-sulfotransferase (hSULT2A1). The structure of the complex provides new insight into species different bile acid metabolism.
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SULT genetic polymorphisms: physiological, pharmacological and clinical implications 査読あり 国際共著
Kurogi K., Rasool M.I., Alherz F.A., El Daibani A.A., Bairam A.F., Abunnaja M.S., Yasuda S., Wilson L.J., Hui Y., Liu M.C.
Expert Opinion on Drug Metabolism and Toxicology 17 ( 7 ) 767 - 784 2021年7月
担当区分：筆頭著者 記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：Expert Opinion on Drug Metabolism and Toxicology
Introduction: Cytosolic sulfotransferases (SULTs)-mediated sulfation is critically involved in the metabolism of key endogenous compounds, such as catecholamines and thyroid/steroid hormones, as well as a variety of drugs and other xenobiotics. Studies performed in the past three decades have yielded a good understanding about the enzymology of the SULTs and their structural biology, phylogenetic relationships, tissue/organ-specific/developmental expression, as well as the regulation of the SULT gene expression. An emerging area is related to the functional impact of the SULT genetic polymorphisms. Areas covered: The current review aims to summarize our current knowledge about the above-mentioned aspects of the SULT research. An emphasis is on the information concerning the effects of the polymorphisms of the SULT genes on the functional activity of the SULT allozymes and the associated physiological, pharmacological, and clinical implications. Expert opinion: Elucidation of how SULT SNPs may influence the drug-sulfating activity of SULT allozymes will help understand the differential drug metabolism and eventually aid in formulating personalized drug regimens. Moreover, the information concerning the differential sulfating activities of SULT allozymes toward endogenous compounds may allow for the development of strategies for mitigating anomalies in the metabolism of these endogenous compounds in individuals with certain SULT genotypes.
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Impact of Human SULT1E1 Polymorphisms on the Sulfation of 17β-Estradiol, 4-Hydroxytamoxifen, and Diethylstilbestrol by SULT1E1 Allozymes 査読あり
El Daibani AA, Alherz FA, Abunnaja MS, Bairam AF, Rasool MI, Kurogi K, Liu MC
Eur J Drug Metab Pharmacokinet. 46 ( 1 ) 105 - 118 2021年1月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Effects of indole and indoxyl on the intracellular oxidation level and phagocytic activity of differentiated HL-60 human macrophage cells. 査読あり
Tsutsumi S, Tokunaga Y, Shimizu S, Kinoshita H, Ono M, Kurogi K, Sakakibara Y, Suiko M, Liu MC, Yasuda S.
J Toxicol Sci. 45 ( 9 ) 569 - 579 2020年9月
記述言語：英語 掲載種別：研究論文（学術雑誌）
DOI： 10.2131/jts.45.569.
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Functional analysis of novel sulfotransferases in the silkworm Bombyx mori 査読あり
Bairam AF, Kermasha ZW, Liu MC, Kurogi K, Yamamoto K.
Arch Insect Biochem Physiol 104 ( 3 ) e21671 2020年7月
記述言語：英語 掲載種別：研究論文（学術雑誌）
DOI： 10.1002/arch.21671.
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Investigation of the effects of indoxyl sulfate, a uremic toxin, on the intracellular oxidation level and phagocytic activity using an HL-60-differentiated human macrophage cell model 査読あり
Tsutsumi S, Tokunaga Y, Shimizu S, Kinoshita H, Ono M, Kurogi K, Sakakibara Y, Suiko M, Liu MC, Yasuda S.
Biosci Biotechnol Biochem 84 ( 5 ) 1023 - 1029 2020年5月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Effect of SULT2B1 genetic polymorphisms on the sulfation of dehydroepiandrosterone and pregnenolone by SULT2B1b allozymes. 査読あり
Alherz FA, El Daibani AA, Abunnaja MS, Bairam AF, Rasool MI, Sakakibara Y, Suiko M, Kurogi K, Liu MC.
Molecular and Cellular Endocrinology 496 110535 2019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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Impact of SULT1A3/SULT1A4 genetic polymorphisms on the sulfation of phenylephrine and salbutamol by human SULT1A3 allozymes. 査読あり
Bairam AF, Rasool MI, Alherz FA, Abunnaja MS, El Daibani AA, Gohal SA, Alatwi ES, Kurogi K, Liu MC.
Pharmacogenetics and genomics. 29 99 - 105 2019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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レトルト加工および保蔵期間が鶏肉のイミダゾールジペプチド含有量に及ぼす影響 査読あり
神力（長友）はるな，近藤知巳，永濵清子，福井敬一，黒木勝久，水光正仁，榊原陽一
日本食品科学工学会誌 66 210 - 214 2019年6月
記述言語：日本語 掲載種別：研究論文（学術雑誌）
DOI： 10.3136/nskkk.66.210
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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）
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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. 2017年1月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Updated perspectives on the cytosolic sulfotransferases (SULTs) and SULT-mediated sulfation. 査読あり
Suiko M, Kurogi K, Hashiguchi T, Sakakibara Y, Liu MC.
Bioscience, Biotechnology, and Biochemistry. 81 ( 1 ) 63 - 72 2017年1月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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A proteomic approach for the analysis of S-nitrosylated proteins using a fluorescence labeling technique. 査読あり
Yoshimura T, Kurogi K, Liu MC, Suiko M, Sakakibara Y
Journal of Electrophoresis 60 ( 1 ) 5 - 14 2016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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Human Cytosolic Sulfotransferase SULT1A3 Mediates the Sulfation of Dextrorphan. 査読あり
Yamamoto A, Kurogi K, Schiefer IT, Liu MY, Sakakibara Y, Suiko M, Liu MC.
Biological and Pharmaceutical Bulletin 39 ( 9 ) 1432 - 1436 2016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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Sulfation of benzyl alcohol by the human cytosolic sulfotransferases (SULTs): a systematic analysis. 査読あり
Zhang L, Kurogi K, Liu MY, Schnapp AM, Williams FE, Sakakibara Y, Suiko M, Liu MC.
Journal of Applied Toxicology 36 ( 9 ) 1090 - 1094 2016年9月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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A novel procedure for the assessment of the antioxidant capacity of food components 査読あり
Yoshimura T, Harashima M, Kurogi K, Suiko M, Liu MC, Sakakibara Y.
Analytical biochemistry 507 7 - 12 2016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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Identification and Characterization of the Human Cytosolic Sulfotransferases Mediating the Sulfation of Clioquinol and Iodoquinol. 査読あり
Yamamoto A, Debrah-Pinamang M, DiModica NJ, Kurogi K, Naqvi AA, Hui Y, Sakakibara Y, Suiko M, Liu MC.
Drug Metabolism Letters. 10 ( 3 ) 200 - 205 2016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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Identification of the Human SULT Enzymes Involved in the Metabolism of Rotigotine. 査読あり
Jia C, Luo L, Kurogi K, Yu J, Zhou C, Liu MC
Journal of Clinical Pharmacology 56 ( 6 ) 754 - 760 2016年6月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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シイタケおよびその加工品による抗酸化ストレス作用 査読あり
近藤知巳，中島有紀子，渡辺朋子，吉山佳世，内田飛香， 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 63 ( 5 ) 199 - 208 2016年5月
記述言語：日本語 掲載種別：研究論文（学術雑誌）
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Sulfate Conjugation of Daphnetin by the Human Cytosolic Sulfotransferases. 査読あり
Han Z, Xi Y, Luo L, Zhou C, Kurogi K, Sakakibara Y, Suiko M, Liu MC.
Journal of Ethnopharmacology 2016年5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 sulfotransferase SULT1C4 mediates the sulfation of doxorubicin and epirubicin. 査読あり
Luo L, Zhou C, Hui Y, Kurogi K, Sakakibara Y, Suiko M, Liu MC.
Drug metabolism and pharmacokinetics. 31 ( 2 ) 163 - 166 2016年4月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Sulfation of 6-Gingerol by the Human Cytosolic Sulfotransferases: A Systematic Analysis. 査読あり
Luo L, Mei X, Xi Y, Zhou C, Hui Y, Kurogi K, Sakakibara Y, Suiko M, Liu MC.
Planta Medica 82 ( 3 ) 238 - 243 2016年2月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Sulphation of acetaminophen by the human cytosolic sulfotransferases: a systematic analysis 査読あり
Yamamoto A, Liu MY, Kurogi K, Sakakibara Y, Saeki Y, Suiko M, Liu MC
Journal of Biochemistry 158 ( 6 ) 497 - 504 2015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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Sulfation of benzyl alcohol by the human cytosolic sulfotransferases (SULTs): a systematic analysis. 査読あり
Zhang L, Kurogi K, Liu MY, Schnapp AM, Williams FE, Sakakibara Y, Suiko M, Liu MC.
Journal of Applied Toxicology 2015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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Sulfation of 6-hydroxymelatonin, N-acetylserotonin and 4-hydroxyramelteon by the human cytosolic sulfotransferases (SULTs). 査読あり
Luo L, Zhou C, Kurogi K, Sakakibara Y, Suiko M, Liu MC.
Xenobiotica 2015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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タンパク質蛍光標識技術を用いた S-ニトロシル化タンパク質の解析法開発 査読あり
芳村 俊広, 黒木 勝久, 水光 正仁, 榊原 陽一
電気泳動 59 ( 2 ) 123 - 125 2015年10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 afimoxifene, endoxifen, raloxifene, and fulvestrant by the human cytosolic sulfotransferases (SULTs): A systematic analysis. 査読あり
Hui Y, Luo L, Zhang L, Kurogi K, Zhou C, Sakakibara Y, Suiko M, Liu MC.
Journal of Pharmacological Sciences 128 ( 3 ) 144 - 149 2015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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Sulfation of phenylephrine by the human cytosolic sulfotransferases 査読あり
Yamamoto A, Kim J, Liu MY, Kurogi K, Sakakibara Y, Suiko M, Liu MC
Drug metabolism letters 8 ( 2 ) 96 - 100 2014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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Sulfation of opioid drugs by human cytosolic sulfotransferases: Metabolic labeling study and enzymatic analysis. 査読あり
Katsuhisa Kurogi, Andriy Chepak, Michael T. Hanrahan, Ming-Yih Liu, Yoichi Sakakibara, Masahito Suiko, Ming-Cheh Liu
European Journal of Pharmaceutical Sciences 62 ( C ) 40 - 48 2014年5月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Identification of a novel flavonoid glycoside sulfotransferase in Arabidopsis thaliana 査読あり
Hashiguchi, T., Sakakibara, Y., Shimohira, T., Kurogi, K., Yamasaki, M., Nishiyama, K., Akashi, R., Liu, M.C., Suiko, M.
Journal of Biochemistry 155 ( 2 ) 91 - 97 2014年2月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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The use of zebrafish as a model system for investigating the role of the SULTs in the metabolism of endogenous compounds and xenobiotics. 査読あり
Kurogi, K, Liu, T.A., Sakakibara, Y., Suiko, M., Liu, M.C.
Drug Metabolism Reviews 45 ( 4 ) 431 - 440 2013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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Identification and characterization of a novel kaempherol sulfotransferase from Arabidoposis thaliana 査読あり
Hashiguchi, T., Sakakibara, Y., Hara, Y., Shimohira, T., Kurogi, K., Akashi, R., Liu, M.-C., and Suiko, M.
Biochemical and Biophysical Research Communications 434 ( 4 ) 829 - 835 2013年5月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Teramoto, T., Fujikawa, Y., Kawaguchi, Y., Kurogi, K., Soejima, M., Adachi, R., Nakanishi, Y., Mishiro-Sato, E., Liu, M.-C., Sakakibara, Y., Suiko, M., Kimura, M., and Kakuta, Y.
Nature Communications 4 2013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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Ethanol sulfation by the human cytosolic sulfotransferases: A systematic analysis 査読あり
Kurogi, K., Davidson, G., Mohammed, Y.I., Williams, F.E., Liu, M.Y., Sakakibara, Y., Suiko, M., and Liu, M.-C.
Biological & pharmaceutical bulletin. 35 ( 12 ) 2180 - 2185 2012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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Concerted actions of the catechol O-methyltransferase and the cytosolic sulfotransferase SULT1A3 in the metabolism of catecholic drugs 査読あり
Kurogi, K., Alazizi, A., Liu, M.Y., Sakakibara, Y., Suiko, M., Sugahara, T., and Liu, M.-C.
Biochemical Pharmacology 84 ( 9 ) 1186 - 1195 2012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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Sulfation of ractopamine and salbutamol by the human cytosolic sulfotransferases 査読あり
Ko, K.*, Kurogi, K.*, Davidson, G., Liu, M.Y., Sakakibara, Y., Suiko, M., and Liu, M.-C
Journal of Biochemistry 152 ( 3 ) 275 - 283 2012年9月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Sulfation of buprenorphine, pentazaocine, and naloxone by human cytosolic sulfotransferases 査読あり
Kurogi, K., Chen, M., Lee, Y., Shi, B., Yang, T., Liu, M.Y., Sakakibara, Y., Suiko, M., and Liu, M.-C.
Drug Metabolism Letters 6 ( 2 ) 109 - 115 2012年6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 zebrafish SULT1 ST9, SULT3 ST4, and SULT3 ST5 査読あり
Mohammed, Y.I., Kurogi, K., Shaban, A.A., Xu, Z., Liu, M.Y., Williams, F.E., Sakakibara, Y., Suiko, M., Bhuiyan, S., and Liu, M.-C
Aquatic Toxicology 112-113 11 - 18 2012年5月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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A comparative study of the sulfation of bile acids and a bile alcohol by the Zebra danio (Danio rerio) and human cytosolic sulfotransferases (SULTs) 査読あり
Kurogi, K., Krasowski, M.D., Injeti, E., Liu, M.Y., Williams, F.E., Sakakibara, Y., Suiko, M., and Liu, M.-C
The Journal of Steroid Biochemistry and Molecular Biology 127 ( 3-5 ) 307 - 314 2011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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Enzymatic sulfation of tocopherols and tocopherol metabolites by human cytosolic sulfotransferase 査読あり
Hashiguchi, T., Kurogi, K., Sakakibara, Y., Yamasaki, M., Nishiyama, K., Yasuda, S., Liu, M.-C., and Suiko, M
Bioscience, Biotechnology, and Biochemistry 75 ( 10 ) 1951 - 1956 2011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, characterization, and ontogenic study of a catechol O-methyltransferase from zebrafish 査読あり
Alazizi, A., Liu, M.Y., Williams, F.E., Kurogi, K., Sakakibara, Y., Suiko, M., and Liu, M.-C
Aquatic Toxicology 102 ( 1-2 ) 18 - 23 2011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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Mouse cytosolic sulfotransferase SULT2B1b interacts with cytoskeletal proteins via a proline/serine-rich C-terminus 査読あり
Kurogi, K., Sakakibara, Y., Kamemoto, Y., Takahashi, S., Yasuda, S., Liu, M.-C., and Suiko, M
FEBS Journal 277 ( 18 ) 3804 - 3811 2010年9月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Sulfation of drug compounds by the zebrafish cytosolic sulfotransferases (SULTs) 査読あり
Kurogi, K., Dillon, J., Nasser, A., Liu, M.Y., Williams, F.E., Sakakibara, Y., Suiko, M., and Liu, M.-C
Drug Metabolism Letters 4 ( 2 ) 62 - 68 2010年4月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Molecular cloning and characterization of a novel canine sulfotransferase 査読あり
Kurogi, K., Sakakibara, Y., Yasuda, S., Liu, M.-C., and Suiko, M
Animal Cell Technology: Basic & Applied Aspects 16 221 - 229 2010年2月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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A novel hydroxysteroid-sulfating cytosolic sulfotransferase, SULT3 ST3, from zebrafish: Identification, characterization, and ontogenic study 査読あり
Yasuda, S., Burgess, M., Yasuda, T., Liu, M.Y., Bhuiyan, S., Williams, F.E., Kurogi, K., Sakakibara, Y., Suiko, M., and Liu, M.-C.
Drug Metabolism Letters 3 ( 4 ) 217 - 227 2009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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Molecular cloning, expression and characterization of a novel mouse SULT6 cytosolic sulfotransferas 査読あり
Takahashi, S., Sakakibara, Y., Mishiro, E., Kouriki, H., Nobe, R., Kurogi, K., Yasuda, S., Liu, M.-C., and Suiko, M
Journal of Biochemistry 146 ( 3 ) 399 - 405 2009年9月
記述言語：英語 掲載種別：研究論文（学術雑誌）
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Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase. 査読あり
Teramoto, T., Sakakibara, Y., Inada, K., Kurogi, K., Liu, M.-C., Suiko, M., Kimura, M., and Kakuta, Y
FEBS Letters 582 ( 28 ) 3909 - 3914 2008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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Molecular cloning, expression, and characterization of mouse amine N-sulfotransferases 査読あり
Takahashi, S., Sakakibara, Y., Mishiro, E., Kouriki, H., Nobe, R., Kurogi, K., Yasuda, S., Liu, M.-C., and Suiko, M
Biochemical and Biophysical Research Communications 375 ( 4 ) 531 - 535 2008年10月
記述言語：英語 掲載種別：研究論文（学術雑誌）