論文 - 榊原 陽一
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Genistein induced apoptotic cell death in adult t-cell leukemia cells through estrogen receptors 査読あり
Yamasaki M., Mukai A., Ohba M., Mine Y., Sakakibara Y., Suiko M., Morishita K., Nishiyama K.
Bioscience, Biotechnology and Biochemistry 74 ( 10 ) 2113 - 2115 2010年11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
Adult T-cell leukemia (ATL) occurs in human T-lymphotropic virus type I-infected individuals and is endemic to the southwestern area of Kyushu in Japan. Here, we found that nM levels of genistein and 17-estradiol had cytotoxic effects on ATL cells and activated caspase-3. The estrogen receptor antagonist ICI182780 negated the cytotoxic effect of genistein. In addition, G protein-coupled estrogen receptor agonist G-1 also had a cytotoxic effect on ATL cells. This is the first report suggesting that estrogen receptors are a molecular target for ATL therapy.
DOI： 10.1271/bbb.100359
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Genistein induced apoptotic cell death in adult T-cell leukemia cells through estrogen receptors. 査読あり
Yamasaki M, Mukai A, Ohba M, Mine Y, Sakakibara Y, Suiko M, Morishita K, Nishiyama K.
Biosci. Biotechnol. Biochem. 74 ( 10 ) 2113 - 2115 2010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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Hui Y., Hui Y., Yasuda T., Yasuda S., Liu M., Sakakibara Y., Suiko M., Wall K., Liu M.
Biological and Pharmaceutical Bulletin 33 ( 9 ) 1633 - 1637 2010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：Biological and Pharmaceutical Bulletin
Prolonged exposure to high level of estrogen is a known risk factor for breast carcinogenesis. It has been suggested recently that nitrative stress may be an etiologic factor for breast carcinogenesis. Since sulfation plays a major role in the homeostasis of estrogens and their metabolites, we attempted in the present study to find out whether nitrative stress may affect the homeostasis of estrogens through sulfation. Metabolic labeling experiments revealed that the amount of sulfated 17β-estradiol or 4-methoxyestradiol decreased dramatically in MCF- 10A mammary epithelial cells incubated in the presence of 3-morpholinosydnonimine (SIN-1) or diethylenetriamine NONOate (DETA NONOate), two nitric oxide donors commonly used to simulate nitrative stress conditions. In searching for the mechanism underlying the decrease of the sulfation of 17β-estradiol and 4- methoxyestradiol, we demonstrated in an in vitro nitration experiment, that the human cytosolic sulfotransferase isoform 1E1 (SULT1E1), a major estrogen-sulfating enzyme, lost its estrogen-sulfating activity proportionately to the degree of nitration on tyrosine residues. Moreover, cell lysates prepared from MCF-10A cells treated with SIN-1 or DETA NONOate also showed much lower 4-methoxyestradiol-sulfating activities, compared with those determined with cell lysate prepared from control MCF-10A cells. © 2010 Pharmaceutical Society of Japan.
DOI： 10.1248/bpb.33.1633
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Inhibitory effects of nitrative stress on the sulfation of 17beta-estradiol and 4-methoxyestradiol by human MCF 10A mammary epithelial cells. 査読あり
Hui Y, Yasuda T, Yasuda S, Liu MY, Sakakibara Y, Suiko M, Wall KA, Liu MC.
Biol. Pharm. Bull. 33 ( 9 ) 1633 - 1637 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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Kurogi K., Sakakibara Y., Kamemoto Y., Takahashi S., Yasuda S., Liu M., 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） 出版者・発行元：FEBS Journal
Cytosolic sulfotransferase (SULT) SULT2B1b had previously been characterized as a cholesterol sulfotransferase. Like human SULT2B1, mouse SULT2B1b contains a unique, 31 amino acid C-terminal sequence with a proline/serine-rich region, which is not found in members of other SULT families. To gain insight into the functional relevance of this proline/serine-rich region, we constructed a truncated mouse SULT2B1b lacking the 31 C-terminal amino acids, and compared it with the wild-type enzyme. Enzymatic characterization indicated that the catalytic activity was not significantly affected by the absence of those C-terminal residues. Glutathione S-transferase pulldown assays showed that several proteins interacted with mouse SULT2B1b specifically through this C-terminal proline/serine-rich region. Peptide mass fingerprinting revealed that of the five SULT2B1b-binding proteins analyzed, three were cytoskeletal proteins and two were cytoskeleton-binding molecular chaperones. Furthermore, wild-type mouse SULT2B1b, but not the truncated enzyme, was associated with the cytoskeleton in experiments with a cytoskeleton-stabilizing buffer. Collectively, these results suggested that the unique, extended proline/serine-rich C-terminus of mouse SULT2B1b is important for its interaction with cytoskeletal proteins. Such an interaction may allow the enzyme to move along microfilaments such as actin filaments, and catalyze the sulfation of hydroxysteroids, such as cholesterol and pregnenolone, at specific intracellular locations. Structured digital abstract : Sult2B1b (uniprotkb:) physically interacts () with Myosin-Ic (uniprotkb:), Alpha-actinin-1 (uniprotkb:), Alpha-actinin-4 (uniprotkb:), HSP 90-beta (uniprotkb:), Hsc70, (uniprotkb:), Beta-actin (uniprotkb:) and Gamma-actin (uniprotkb:) by pull down. © 2010 FEBS.
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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 MC, Suiko M.
FEBS J. 277 ( 18 ) 3804 - 3811 2010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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Zebrafish as a Model for the Study of the Phase II Cytosolic Sulfotransferases. 招待あり 査読あり
Liu TA, Bhuiyan S, Liu MY, Sugahara T, Sakakibara Y, Suiko M, Yasuda S, Kakuta Y, Kimura M, Williams FE, Liu MC.
Curr Drug Metab. 11 ( 6 ) 538 - 546 2010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 of A Novel Biomarker for Oxidative Stress Induced by Hydrogen Peroxide in Primary Human Hepatocytes Using The 2-nitrobenzenesulfenyl Chloride Isotope Labeling Method. 査読あり
Takami, Y., Uto, H., Tamai, T., Sato, Y., Ishida, Y., Morinaga, H., Sakakibara, Y., Moriuchi, A., Oketani, M., Ido, A., Nakajima, T., Okanoue, T., Tsubouchi, H.
Hepatol. Res. 40 438 - 445 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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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., Liu, M.-C.
Drug Metab. Lett. 4 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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Shirasugi I., Shirasugi I., Kamada M., Matsui T., Sakakibara Y., Sakakibara Y., Liu M., Suiko M., Suiko M.
Bioscience, Biotechnology and Biochemistry 74 ( 3 ) 579 - 582 2010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：Bioscience, Biotechnology and Biochemistry
Sulforaphane is a compound widely present in consumed vegetables, particularly broccoli. Previous studies have demonstrated that sulforaphane has many physiological effects including anti-cancer, anti-oxidation, and detoxification. In this study, we found that sulforaphane inhibited melanogenesis and tyrosinase expression. The inhibitory effect of 5μM sulforaphane on melanogenesis was determined to be equivalent to that of 100μM arbutin. In addition, sulforaphane induced phosphorylated extracellular signal-regulated kinase (ERK) and inhibited phosphorylated p38. It has been reported that the phosphorylated mitogenactivated protein (MAP) kinase family (ERK and p38) controls tyrosinase expression. Our data indicate that sulforaphane inhibited melanogenesis and tyrosinase expression by affecting the phosphorylated MAP kinase family. These findings indicate that sulforaphane might be an effective skin-whitening agent.
DOI： 10.1271/bbb.90778
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Sulforaphane Inhibited Melanin Synthesis by Regulating Tyrosinase Gene Expression in B16 Mouse Melanoma Cells. 査読あり
Shirasugi, I., Kamada, M., Matsui, T., Sakakibara, Y., Liu, M.-C., Suiko, M.
Biosci. Biotechnol. Biochem. 74 579 - 582 2010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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Molecular Cloning and Characterization of a Novel Canine Sulfotransferase
Kurogi, K., Sakakibara, Y., Yasuda, S., Liu, M.-C., Suiko, M.
Animal Cell Technology: Basic & Applied Aspects 16 221 - 229 2010年1月
記述言語：英語 掲載種別：研究論文（国際会議プロシーディングス）
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Sulfation of drug compounds by the zebrafish cytosolic sulfotransferases (SULTS) 査読あり
Kurogi K., Kurogi K., Dillon J., Nasser A., Liu M., Williams F., Sakakibara Y., Suiko M., Liu M.
Drug Metabolism Letters 4 ( 2 ) 62 - 68 2010年
記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：Drug Metabolism Letters
To establish the zebrafish as a model to investigate drug metabolism through sulfation, we had previous cloned, expressed, and purified fourteen distinct zebrafish cytosolic sulfotransferases (SULTs). In the present study, we carried a systematic analysis of the sulfating activities of these fourteen zebrafish SULTs toward a panel of drug compounds. Results showed that four of the fourteen zebrafish SULTs showed no detectable activities toward any of the tested drugs. Among the other ten zebrafish SULTs, three SULT1 enzymes (SULT1 ST1, SULT1 ST2, and SULT1 ST3) displayed considerably stronger activities than the others toward the majority of the drug compounds tested. Specifically, SULT1 ST1, SULT1 ST2, and SULT1 ST3 showed the highest specific activities, at 26.9, 29.3, and 31.5 nmol/min/mg, toward aesculetin, 4-methylembelliferone, and dobutamine, respectively. To further investigate the sulfation of tested drugs by the responsible zebrafish SULT enzymes, the kinetics of the sulfation reactions were analyzed. Kinetic constants determined indicated that the sulfation of these drugs by the SULT enzymes tested is likely to be physiologically relevant. A metabolic labeling experiment using cultured zebrafish liver cells and HepG2 human hepatoma cells was performed. Results showed that zebrafish liver cells displayed a similar pattern of sulfation of the drugs tested as that of HepG2 cells, implying that human and zebrafish liver cells may share considerable similarities with regard to their constituent drugsulfating SULT enzymes. © 2010 Bentham Science Publishers Ltd.
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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., Liu, M.-C.
Drug Metab. Lett. 3 217 - 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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Yasuda S., Burgess M., Yasuda T., Liu M., Bhuiyan S., Williams F., Kurogi K., Sakakibara Y., Suiko M., Liu M., Liu M.
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） 出版者・発行元：Drug Metabolism Letters
To establish the zebrafish as a model for investigating the drug metabolism through sulfation, we had embarked on establishing a complete repertoire of the zebrafish Phase II cytosolic sulfotransferases (SULTs). By searching the expressed sequence tag database, a zebrafish cDNA encoding a putative cytosolic sulfotransferase (SULT) was identified. Based on the sequence analysis, this zebrafish SULT was found to belong to the SULT3 gene family. The recombinant protein of the zebrafish SULT, designated SULT3 ST3, was expressed in and purified from BL21 (DE3) Escherichia coli cells transformed with the pGEX-2TK expression vector harboring SULT3 ST3 cDNA. Upon enzymatic characterization, purified SULT3 ST3 displayed sulfating activity toward hydroxysteroids, particularly pregnenolone and dehydroepiandrosterone (DHEA), as well as several drugs among various endogenous and xenobiotic compounds tested as substrates. The pH-dependence and kinetic constants of this enzyme with DHEA were determined. The regulatory effects of various divalent metal cations on the DHEA-sulfating activity of SULT3 ST3 were quantitatively evaluated. A reverse transcription-polymerase chain reaction (RT-PCR) analysis revealed developmental stage-dependent expression of SULT3 ST3 during embryonic development and throughout the larval stage onto maturity. Collectively, these results suggest a possible involvement of the newly discovered SULT3 ST3 in the metabolism of hydroxysteroids and xenobiotics including drugs in zebrafish. © 2009 Bentham Science Publishers Ltd.
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Yamasaki M., Omi Y., Fujii N., Ozaki A., Nakama A., Sakakibara Y., Suiko M., Nishiyama K.
Bioscience, Biotechnology and Biochemistry 73 ( 10 ) 2217 - 2221 2009年11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
Cruciferous vegetables and their isothiocyanates are promising foods and agents for cancer prevention. We focus here on the effects of mustard oil (SMO) in a variety of the Japanese radish, Shibori Daikon (Raphanus sativus), on the proliferation of 3Y1 rat fibroblasts and the H-ras-transformed derivative, HR-3Y1-2. SMO (1.6 μ, g/ml) inhibited the proliferation of HR-3Y1-2, but not 3Y1 after 24h after treatment. A cell cycle analysis showed that SMO induced G2/M arrest after 6 h, although this effect was not observed 24 h after the treatment. SMO transiently decreased the cellular reduced glutathione level accompanied with up-regulation of the intracellular reactive oxygen species 2-3 h post-treatment. Glutathione ethyl ester and N- acetyl-L-cysteine prevented the growth inhibitory effect of SMO. This mustard oil extract consisted of 95.6% 4-methylthio-3-butenyl isothiocyanate and 4.4% 4-methylthiobutyl isothiocyanate. SMO selectively inhibited H-ras-transformed 3Y1 cells associated with transient oxidative stress via reduced glutathione (GSH) depletion.
DOI： 10.1271/bbb.90322
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Mustard Oil in "Shibori Daikon" a Variety of Japanese Radish, Selectively Inhibits the Proliferation of H-ras-Transformed 3Y1 Cells. 査読あり
Yamasaki, M., Omi, Y., Fujii, N., Ozaki, A., Nakama, A., Sakakibara, Y., Suiko, M., Nishiyama, K.
Biosci. Biotechnol. Biochem. 73 2217 - 2221 2009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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Molecular Cloning, Expression and Characterization of A Novel Mouse SULT6 Cytosolic Sulfotransferase 査読あり
Takahashi Saki, Sakakibara Yoichi, Mishiro Emi, KOURIKI Haruna, NOBE Rika, KUROGI Katsuhisa, YASUDA Shin, LIU Ming-Cheh, SUIKO Masahito
The 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） 出版者・発行元：Japanese Biochemical Society
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On the similar spatial arrangement of active site residues in PAPS-dependent and phenolic sulfate-utilizing sulfotransferases. 査読あり
Teramoto, T., Adachi, R., Sakakibara, Y., Liu, M.-C., Suiko, M., Kimura, M.,Kakuta, Y.
FEBS Lett. 583 3091 - 3094 2009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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A target-specific approach for the identification of tyrosine-sulfated hemostatic proteins 査読あり
Liu T., Liu T., Yasuda S., Williams F., Liu M., Suiko M., Sakakibara Y., Yang Y., Liu M.
Analytical Biochemistry 390 ( 1 ) 88 - 90 2009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：Analytical Biochemistry
A simple methodology for the identification of hemostatic proteins that are subjected to posttranslational tyrosine sulfation was developed. The procedure involves sequence analysis of members of the three hemostatic pathways using the Sulfinator prediction algorithm, followed by [35S]sulfate labeling of cultured HepG2 human hepatoma cells, immunoprecipitation of targeted [35S]sulfate-labeled hemostatic proteins, and tyrosine O-[35S]sulfate analysis of immunoprecipitated proteins. Three new tyrosine-sulfated hemostatic proteins-protein S, prekallikrein, and plasminogen-were identified. Such a target-specific approach will allow investigation of tyrosine-sulfated proteins of other biochemical/physiological pathways/processes and contribute to a better understanding of the functional role of posttranslational tyrosine sulfation. © 2009 Elsevier Inc. All rights reserved.