Details of the Researcher

PHOTO

Tomoaki Ida
Section
Graduate School of Medicine
Job title
Specially Appointed Professor(Research)
Degree
e-Rad No.
70570406

Research History 4

  • 2025/01 - Present
    Tohoku University Graduate School of Medicine

  • 2023/05 - 2024/12
    Osaka Metropolitan University

  • 2013/06 - 2023/04
    東北大学大学院 医学系研究科 助教

  • 2012/01 - 2013/05
    Kumamoto University

Education 3

  • Osaka Prefecture University Graduate School of Science

    2006/04 - 2010/03

  • Osaka Prefecture University Graduate School of Science

    2004/04 - 2006/03

  • Osaka Prefecture University

    2000/04 - 2004/03

Research Interests 5

  • supersulfides

  • 8-Nitro-cGMP

  • 質量分析装置

  • メタボローム解析

  • 活性イオウ分子種

Research Areas 3

  • Life sciences / Functional biochemistry /

  • Life sciences / Food sciences /

  • Life sciences / Pharmaceuticals - chemistry and drug development /

Awards 8

  1. 学術奨励賞

    2025/05 日本酸化ストレス学会

  2. 若手優秀発表賞

    2023/01 第22回分子予防環境医学研究会

  3. 石田・海老名記念「北斗医学賞」

    2018 公益財団法人仙台微生物学研究所

  4. 若手優秀発表賞

    2018 分子環境予防医学研究会

  5. 学術奨励賞

    2016 日本酸化ストレス学会

  6. 生体防御学会奨励賞

    2015 日本生体防御学会学術総会

  7. 鈴木紘一メモリアル賞

    2012 日本生化学会大会

  8. Travel award

    2012 日本NO学会学

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Papers 97

  1. RNA and chondroitin sulfate—BACE1 inhibitory components in protease-digested whitebait (Shirasu): Potential for Alzheimer's disease prevention in mice

    Takahiro Katsuki, Ayaka Kinno, Tomoaki Ida, Shingo Kasamatsu, Hidenobu Sumitani, Hideshi Ihara

    NFS Journal 100273-100273 2026/05

    Publisher: Elsevier BV

    DOI: 10.1016/j.nfs.2026.100273  

    ISSN: 2352-3646

  2. Sulfide:quinone oxidoreductase drives mitochondrial supersulfide metabolism to regulate bioenergetics and longevity in eukaryotes

    Jia Yao, Tetsuro Matsunaga, Akira Nishimura, Meg Shieh, Tomoaki Ida, Minkyung Jung, Seiryo Ogata, Tsuyoshi Takata, Uladzimir Barayeu, Hozumi Motohashi, Masanobu Morita, Takaaki Akaike

    2026/04/07

    Publisher: openRxiv

    DOI: 10.64898/2026.04.05.716515  

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    Sulfide:quinone oxidoreductase (SQR) is a critical enzyme that maintains sulfur metabolism by oxidizing sulfide to supersulfides, currently defined as sulfur metabolites with six valence electrons and no charge that are covalently catenated with other sulfur atoms and excludes disulfides. While SQR is known to contribute to mitochondrial electron transport, its physiological impact on systemic energy metabolism and longevity remains largely undefined. In this study, we investigated the role of SQR in mitochondrial bioenergetics and aging using SQR-deficient Schizosaccharomyces pombe ( Δhmt2 ) and a mitochondria-selective SQR-deficient ( Sqrdl ΔN/ΔN ) mice model. Functional analysis demonstrated that Δhmt2 grew normally in glucose but not in glycerol, indicating impaired mitochondrial respiration. It showed reduced membrane potential, ATP, and lifespan. Consistent with the yeast findings, Sqrdl ΔN/ΔN mice exhibited accumulated levels of hydrogen sulfide and persulfides, and demonstrated impaired mitochondrial energy metabolism. Furthermore, supersulfide donor supplementation selectively conferred lifespan extension in wild-type yeast, but not in SQR-deficient strain, and similarly improved mitochondrial function exclusively in wild-type mouse embryonic fibroblasts, with no benefit observed in SQR-mutant counterparts. Together, our findings demonstrate that mitochondrial SQR plays an essential role in sulfur respiration, critically supporting mitochondrial function and organismal longevity across eukaryotes.

  3. Sulfide:quinone oxidoreductase drives mitochondrial supersulfide metabolism to regulate bioenergetics and longevity in eukaryotes

    Jia Yao, Tetsuro Matsunaga, Akira Nishimura, Meg Shieh, Tomoaki Ida, Minkyung Jung, Seiryo Ogata, Tsuyoshi Takata, Uladzimir Barayeu, Hozumi Motohashi, Masanobu Morita, Takaaki Akaike

    2026/04/07

    Publisher: openRxiv

    DOI: 10.64898/2026.04.05.716515  

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    Sulfide:quinone oxidoreductase (SQR) is a critical enzyme that maintains sulfur metabolism by oxidizing sulfide to supersulfides, currently defined as sulfur metabolites with six valence electrons and no charge that are covalently catenated with other sulfur atoms and excludes disulfides. While SQR is known to contribute to mitochondrial electron transport, its physiological impact on systemic energy metabolism and longevity remains largely undefined. In this study, we investigated the role of SQR in mitochondrial bioenergetics and aging using SQR-deficient Schizosaccharomyces pombe ( Δhmt2 ) and a mitochondria-selective SQR-deficient ( Sqrdl ΔN/ΔN ) mice model. Functional analysis demonstrated that Δhmt2 grew normally in glucose but not in glycerol, indicating impaired mitochondrial respiration. It showed reduced membrane potential, ATP, and lifespan. Consistent with the yeast findings, Sqrdl ΔN/ΔN mice exhibited accumulated levels of hydrogen sulfide and persulfides, and demonstrated impaired mitochondrial energy metabolism. Furthermore, supersulfide donor supplementation selectively conferred lifespan extension in wild-type yeast, but not in SQR-deficient strain, and similarly improved mitochondrial function exclusively in wild-type mouse embryonic fibroblasts, with no benefit observed in SQR-mutant counterparts. Together, our findings demonstrate that mitochondrial SQR plays an essential role in sulfur respiration, critically supporting mitochondrial function and organismal longevity across eukaryotes.

  4. Formation of a reducing microenvironment and regulation of protein supersulfidation by gut microbial supersulfides. International-journal Peer-reviewed

    Jun Uchiyama, Yoshimi Shimizu, Takamitsu Unoki, Shingo Kasamatsu, Tomoaki Ida, Hideshi Ihara, Yun-Gi Kim, Koji Hase, Yuri Miura, Tomohiko Maehama, Maiko Kusano, Keitaro Umezawa, Masahiro Akiyama

    Redox biology 92 104123-104123 2026/03/11

    DOI: 10.1016/j.redox.2026.104123  

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    Supersulfides, sulfur species containing catenated sulfur atoms, are potent reducing agents produced by diverse organisms. Although their intracellular functions are increasingly recognized, the ecological and physiological importance of gut microbial supersulfides remains poorly understood. In this study, we explored two complementary aspects of gut microbiota-derived supersulfide. First, by assessing the reducing activity, we found that bacterial supersulfides contribute to the enhancement of the extracellular reducing capacity. In particular, Dorea longicatena and Enterocloster bolteae exhibit strong cystine-dependent supersulfide production, which is associated with protection against oxidative stress. Second, beyond their ecological roles, supersulfides influence protein supersulfidation, which is a reversible post-translational modification. Supersulfidated proteins have been detected across multiple commensal taxa with species-specific profiles. This modification is redox-sensitive and modulated by extracellular supersulfides. Members of the Lactobacillaceae family are particularly susceptible to exogenous supersulfides. Supersulfidation involves proteins linked to core microbial processes, including bile acid metabolism, suggesting their potential role in tuning bacterial functions. Together, these findings suggest that microbial supersulfides act as dual regulators: (i) contributing to a protective reducing milieu and (ii) modulating bacterial protein function through supersulfidation. By highlighting post-translational control in gut bacteria and their sensitivity to the local redox environment, this work broadens the current models of microbial redox biology and provides a basis for linking bacterial sulfur metabolism with gut ecosystem stability and host-microbe interactions.

  5. Dynamic transformation of the sulfur metabolome during natto fermentation: Supersulfide omics study Peer-reviewed

    Tomoaki Ida, Shingo Kasamatsu, Mahiro Kuryu, Haruka Nitta, Wakana Nagamura, Hina Yoshida, Ayaka Kinno, Aoi Morishita, Takaaki Akaike, Hideshi Ihara

    Nitric Oxide 160 14-23 2026/02

    Publisher: Elsevier BV

    DOI: 10.1016/j.niox.2025.11.001  

    ISSN: 1089-8603

  6. Role of Sulfide Quinone Oxidoreductase and Supersulfides in Hepatic Ischemia-Reperfusion Injury in Mice. International-journal

    Shinnosuke Takamori, Kazuhiro Shirozu, Eizo Marutani, Tsuyoshi Takata, Yukie Mizuta, Takahito Kawano, Masaharu Murata, Tomoaki Ida, Tetsuro Matsunaga, Takaaki Akaike, Ken Yamaura, Tomohiko Akahoshi

    Antioxidants (Basel, Switzerland) 15 (1) 2026/01/12

    DOI: 10.3390/antiox15010094  

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    Hepatic ischemia-reperfusion injury (IRI) is a critical clinical condition associated with liver transplantation and acute liver injury. This study investigated the role of sulfide quinone oxidoreductase (SQOR) and its downstream product, supersulfides, in hepatic IRI. C57BL/6NJ mice were subjected to 45 min of partial hepatic ischemia, followed by reperfusion lasting 4 h. Control of shRNA mediated knockdown of SQOR expressing adeno-associated viral vectors were administered 3 weeks prior to liver ischemia. In the shRNA-mediated knockdown of SQOR group, the hydro-trisulfide donor sodium trisulfide was administered daily for 1 week prior to the induction of liver ischemia. SQOR played a crucial protective role during hepatic IRI by facilitating electron transport to the mitochondrial respiratory chain and maintaining the oxidized and reduced nicotinamide adenine dinucleotide ratio. Administration of sodium trisulfide, exhibited protective effects against hepatic IRI. Sodium trisulfide restored the oxidized and reduced nicotinamide adenine dinucleotide ratio, reduced oxidative stress, and preserved the expression of key enzymes involved in the sulfide oxidation pathway. SQOR and supersulfides contribute to hepatic protection against IRI, likely through their potent antioxidative and redox-regulating functions, and highlight sodium trisulfide as a potential therapeutic agent.

  7. Mitochondria regulate the cell fate decisions of megakaryocyte-erythroid progenitors. International-journal

    Eunkyu Sung, Shohei Murakami, Masanobu Morita, Tomoaki Ida, Takaaki Akaike, Hozumi Motohashi

    Stem cell reports 20 (12) 102720-102720 2025/12/09

    DOI: 10.1016/j.stemcr.2025.102720  

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    Recent studies highlight the critical role of mitochondria in hematopoiesis, especially in stem cell function and erythroid maturation. To explore mitochondrial contributions to cell lineage commitment of hematopoietic progenitors, we utilized Cars2-mutant mice, an ideal model for this purpose. CARS2, a mitochondrial isoform of cysteinyl-tRNA synthetase, has cysteine persulfide synthase (CPERS) activity. Our new mouse model, with reduced CPERS activity, showed that the Cars2 mutation led to mitochondrial inhibition and anemia by suppressing erythroid commitment in megakaryocyte-erythroid progenitors (MEPs). This suppression was reproduced using mitochondrial electron transport chain inhibitors. We identified two distinct MEP populations based on the mitochondrial content: mitochondria-rich MEPs favored erythroid differentiation, while the mitochondria-poor MEPs favored megakaryocyte differentiation. These findings reveal critical contributions of mitochondria to the MEP lineage selection, acting as a "mitochondrial navigation" for lineage commitment.

  8. Growth inhibitory factor/metallothionein-3 is a sulfane sulfur-binding protein. International-journal

    Yasuhiro Shinkai, Yunjie Ding, Toru Matsui, George Devitt, Masahiro Akiyama, Tang-Long Shen, Motohiro Nishida, Tomoaki Ida, Takaaki Akaike, Sumeet Mahajan, Jon M Fukuto, Yasuteru Shigeta, Yoshito Kumagai

    eLife 12 2025/11/14

    DOI: 10.7554/eLife.92120  

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    Cysteine-bound sulfane sulfur atoms in proteins have received much attention as key factors in cellular redox homeostasis. However, the role of sulfane sulfur in zinc regulation has been underinvestigated. In this study, we identified growth inhibitory factor (GIF)/metallothionein-3 (MT-3) as a sulfane sulfur-binding protein from mouse brain. We also report here that cysteine-bound sulfane sulfur atoms serve as ligands to hold and release zinc ions in GIF/MT-3 with an unexpected C-S-S-Zn structure. Oxidation of such a zinc/persulfide cluster in Zn7GIF/MT-3 results in the release of zinc ions, and intramolecular tetrasulfide bridges in apo-GIF/MT-3 efficiently undergo S-S bond cleavage by thioredoxin to regenerate Zn7GIF/MT-3. Three-dimensional molecular modeling confirmed the critical role of the persulfide group in the thermostability and Zn-binding affinity of GIF/MT-3. The present discovery raises the fascinating possibility that the function of other Zn-binding proteins is controlled by sulfane sulfur.

  9. Supersulfide controls intestinal inflammation by suppressing CD4+ T cell proliferation Peer-reviewed

    Shunichi Tayama, Yuya Kitamura, Kyoga Hiraide, Hibiki Suzuki, Jing Li, Ziying Yang, Ryoji Mitsuwaka, Akihisa Kawajiri, Kosuke Sato, Feng Gao, Taku Nakai, Yuko Okuyama, Tadahisa Numakura, Mitsuhiro Yamada, Tomoaki Ida, Masanobu Morita, Takeshi Kawabe, Takaaki Akaike, Naoto Ishii

    Frontiers in Immunology 16 2025/04/15

    Publisher: Frontiers Media SA

    DOI: 10.3389/fimmu.2025.1506580  

    eISSN: 1664-3224

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    Inflammatory bowel disease (IBD) is characterized by chronic intestinal inflammation where CD4+ T lymphocytes play an essential role. Accumulating evidence suggests that immune responses driven by CD4+ T cells are critically regulated by various metabolic pathways including oxidative phosphorylation and glycolysis. Here we show that CARS2/CPERS-dependent supersulfide metabolism restrains CD4+ T cell proliferation in a cell-intrinsic manner. Under steady state, Cars2+/- mice exhibited spontaneous accumulation of effector/memory CD4+ T cells in the colon with age. In lymphopenic conditions, Cars2+/- CD4+ T cells showed enhanced cell cycle entry with reduced expression of a cell cycle inhibitor Trp53 and triggered an exacerbated form of colitis, the response being rescued by treatment with a supersulfide donor glutathione trisulfide (GSSSG). Furthermore, re-analysis of publicly available gene datasets of human colonic CD4+ T lymphocytes revealed that downregulation of CARS2 was associated with pathogenesis of IBD, and indeed, addition of GSSSG inhibited human CD4+ T cell proliferation in vitro. Together these observations reveal that CARS2/CPERS-dependent supersulfide metabolism is essential for homeostasis of intestinal effector/memory CD4+ T cells, and further suggest that dysregulation of the same metabolic pathway can lead to development of gut inflammation both in mice and humans.

  10. Serendipitous Discovery of Photolytic Thiosulfoxide Formation: Application for Visible-Light-Inducible Manipulation of Supersulfide Level in Biological Systems

    Mitsuyasu Kawaguchi, Katsutoshi Yoshino, Tomoaki Ida, Hibiki Moriyama, Naoya Ieda, Yuhei Ohta, Shingo Kasamatsu, Hideshi Ihara, Hidehiko Nakagawa

    Journal of the American Chemical Society 147 (15) 12627-12634 2025/04/01

    Publisher: American Chemical Society (ACS)

    DOI: 10.1021/jacs.5c00196  

    ISSN: 0002-7863

    eISSN: 1520-5126

  11. Supersulfides contribute to joint homeostasis and bone regeneration. International-journal

    Miki Maemura, Masanobu Morita, Seiryo Ogata, Yoichi Miyamoto, Tomoaki Ida, Kazuhiro Shibusaka, Soichiro Negishi, Masahiro Hosonuma, Taku Saito, Jun Yoshitake, Tsuyoshi Takata, Tetsuro Matsunaga, Eikan Mishima, Uladzimir Barayeu, Takaaki Akaike, Fumiko Yano

    Redox biology 81 103545-103545 2025/02/11

    DOI: 10.1016/j.redox.2025.103545  

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    The physiological functions of supersulfides, inorganic and organic sulfides with sulfur catenation, have been extensively studied. Their synthesis is mainly mediated by mitochondrial cysteinyl-tRNA synthetase (CARS2) that functions as a principal cysteine persulfide synthase. This study aimed to investigate the role of supersulfides in joint homeostasis and bone regeneration. Using Cars2AINK/+ mutant mice, in which the KIIK motif of CARS2 essential for supersulfide production was replaced with AINK, we evaluated the role of supersulfides in fracture healing and cartilage homeostasis during osteoarthritis (OA). Tibial fracture surgery was performed on the wild-type (Cars2+/+) and Cars2AINK/+ mice littermates. Bulk RNA-seq analysis for the osteochondral regeneration in the fracture model showed increased inflammatory markers and reduced osteogenic factors, indicative of impaired bone regeneration, in Cars2AINK/+ mice. Destabilization of the medial meniscus (DMM) surgery was performed to produce the mouse OA model. Histological analyses with Osteoarthritis Research Society International and synovitis scores revealed accelerated OA progression in Cars2AINK/+ mice compared with that in Cars2+/+ mice. To assess the effects of supersulfides on OA progression, glutathione trisulfide (GSSSG) or saline was periodically injected into the mouse knee joints after the DMM surgery. Thus, supersulfides derived from CARS2 and GSSSG exogenously administered significantly inhibited inflammation and lipid peroxidation of the joint cartilage, possibly through suppression of ferroptosis, during OA development. This study represents a significant advancement in understanding anti-inflammatory and anti-oxidant functions of supersulfides in skeletal tissues and may have a clinical relevance for the bone healing and OA therapeutics.

  12. Non-thermal atmospheric pressure plasma-irradiated cysteine protects cardiac ischemia/reperfusion injury by preserving supersulfides Peer-reviewed

    Akiyuki Nishimura, Tomohiro Tanaka, Kakeru Shimoda, Tomoaki Ida, Shota Sasaki, Keitaro Umezawa, Hiromi Imamura, Yasuteru Urano, Fumito Ichinose, Toshiro Kaneko, Takaaki Akaike, Motohiro Nishida

    Redox Biology 79 103445-103445 2025/02

    Publisher: Elsevier BV

    DOI: 10.1016/j.redox.2024.103445  

    ISSN: 2213-2317

  13. Supersulfide formation in the sinus mucosa of chronic rhinosinusitis. International-journal

    Jun Suzuki, Tomotaka Hemmi, Tomoaki Ida, Seiryo Ogata, Jun Yoshitake, Tetsuro Matsunaga, Tomoyasu Ishida, Yuki Numano, Yusuke Kusano, Ryoukichi Ikeda, Kazuhiro Nomura, Mitsuru Sugawara, Nobuo Ohta, Takaaki Akaike, Yukio Katori

    Laryngoscope Investigative Otolaryngology 9 (4) e1261 2024/08

    DOI: 10.1002/lio2.1261  

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    OBJECTIVES: Disruption of the oxidative stress defense system is involved in developing various diseases. Sulfur compounds such as glutathione (GSH) and cysteine (CysSH) are representative antioxidants in the body. Recently, supersulfides, including reactive persulfide and polysulfide species, have gained attention as potent antioxidants regulating oxidative stress and redox signaling. However, their involvement in the pathogenesis of chronic rhinosinusitis (CRS) remains unclear. METHODS: To clarify the changes in sulfur compounds within the sinus mucosa of each CRS subtype, we measured sulfur compound levels in the sinus mucosa of control individuals (n = 9), patients with eosinophilic CRS (ECRS) (n = 13), and those with non-ECRS (nECRS) (n = 11) who underwent sinus surgery using mass spectrometry. RESULTS: GSH and CysSH levels were significantly reduced, and the glutathione disulfide (GSSG)/GSH ratio, an oxidative stress indicator, was increased in patients with ECRS. Despite the absence of notable variations in supersulfides, patients with ECRS and nECRS exhibited a significant reduction in glutathione trisulfide (GSSSG), which serves as the precursor for supersulfides. CONCLUSIONS: This study is the first quantitative assessment of supersulfides in normal and inflamed sinus mucosa, suggesting that sulfur compounds contribute to the pathogenesis of CRS. LEVEL OF EVIDENCE: N/A.

  14. Deciphering pathophysiological mechanisms underlying cystathionine beta-synthase-deficient homocystinuria using targeted metabolomics, liver proteomics, sphingolipidomics and analysis of mitochondrial function. International-journal

    Tomas Majtan, Thomas Olsen, Jitka Sokolova, Jakub Krijt, Michaela Křížková, Tomoaki Ida, Tamás Ditrói, Hana Hansikova, Ondrej Vit, Jiri Petrak, Ladislav Kuchař, Warren D Kruger, Péter Nagy, Takaaki Akaike, Viktor Kožich

    Redox biology 73 103222-103222 2024/06/04

    DOI: 10.1016/j.redox.2024.103222  

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    BACKGROUND: Cystathionine β-synthase (CBS)-deficient homocystinuria (HCU) is an inherited disorder of sulfur amino acid metabolism with varying severity and organ complications, and a limited knowledge about underlying pathophysiological processes. Here we aimed at getting an in-depth insight into disease mechanisms using a transgenic mouse model of HCU (I278T). METHODS: We assessed metabolic, proteomic and sphingolipidomic changes, and mitochondrial function in tissues and body fluids of I278T mice and WT controls. Furthermore, we evaluated the efficacy of methionine-restricted diet (MRD) in I278T mice. RESULTS: In WT mice, we observed a distinct tissue/body fluid compartmentalization of metabolites with up to six-orders of magnitude differences in concentrations among various organs. The I278T mice exhibited the anticipated metabolic imbalance with signs of an increased production of hydrogen sulfide and disturbed persulfidation of free aminothiols. HCU resulted in a significant dysregulation of liver proteome affecting biological oxidations, conjugation of compounds, and metabolism of amino acids, vitamins, cofactors and lipids. Liver sphingolipidomics indicated upregulation of the pro-proliferative sphingosine-1-phosphate signaling pathway. Liver mitochondrial function of HCU mice did not seem to be impaired compared to controls. MRD in I278T mice improved metabolic balance in all tissues and substantially reduced dysregulation of liver proteome. CONCLUSION: The study highlights distinct tissue compartmentalization of sulfur-related metabolites in normal mice, extensive metabolome, proteome and sphingolipidome disruptions in I278T mice, and the efficacy of MRD to alleviate some of the HCU-related biochemical abnormalities.

  15. 慢性腎臓病の早期診断法確立を目指した硫黄代謝物に基づく呼気オミックス

    逸見 佳宣, 緒方 星陵, 井田 智章, 三枝 大輔, 三島 英換, 高橋 信行, 魏 范研, 赤池 孝章, 佐藤 恵美子

    日本腎臓学会誌 66 (4) 632-632 2024/06

    Publisher: (一社)日本腎臓学会

    ISSN: 0385-2385

    eISSN: 1884-0728

  16. Glutathione supersulphide regulates T-cell receptor signalling

    Yusaku Sasaki, Tadahisa Numakura, Mitsuhiro Yamada, Hisatoshi Sugiura, Tetsuro Matsunaga, Tomoaki Ida, Masanobu Morita, Ayumi Suzuki, Shuichiro Matsumoto, Madoka Kawaguchi, Takeshi Kawabe, Shunichi Tayama, Yuko Okuyama, Tsuyoshi Takata, Kenji Inaba, Satoshi Watanabe, Manami Suzuki, Hirohito Sano, Yorihiko Kyogoku, Rie Tanaka, Ayumi Mitsune, Tomohiro Ichikawa, Naoya Fujino, Tsutomu Tamada, Naoto Ishii, Masakazu Ichinose, Takaaki Akaike, Hozumi Motohashi

    2024/05/02

    Publisher: openRxiv

    DOI: 10.1101/2024.04.30.591985  

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    Abstract Immunometabolism regulates functions and fates of immune cells including T cells. Supersulphides, which are universal metabolites containing catenated sulphur atoms, have various physiological functions based on their unique redox properties. Here we found that activation of T-cell receptor (TCR) signalling was accompanied by supersulphide decrease, which suggests a regulatory contribution of sulphur metabolism to immune function. Consistently, inhibiting supersulphide synthesis facilitated TCR activation and exacerbated allergen-induced type 2 inflammation in mice. Supplementation with glutathione trisulphide (GSSSG), a major endogenous supersulphide, suppressed TCR signalling in naïve CD4 + T cells and their differentiation and effectively alleviated the inflammation. Docking simulation revealed interaction of GSSSG with CD3ε chain in the TCR/CD3 complex, which was supported by mass spectrometry detection of persulphidated glutathionylation at a functionally important CXXC motif of CD3ε chain. This study identified a new post-translational modification with supersulfides and demonstrated a critical contribution of sulphur metabolism to TCR signalling regulation.

  17. Longevity control by supersulfide-mediated mitochondrial respiration and regulation of protein quality. International-journal

    Akira Nishimura, Sunghyeon Yoon, Tetsuro Matsunaga, Tomoaki Ida, Minkyung Jung, Seiryo Ogata, Masanobu Morita, Jun Yoshitake, Yuka Unno, Uladzimir Barayeu, Tsuyoshi Takata, Hiroshi Takagi, Hozumi Motohashi, Albert van der Vliet, Takaaki Akaike

    Redox biology 69 103018-103018 2024/01/03

    DOI: 10.1016/j.redox.2023.103018  

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    Supersulfides, which are defined as sulfur species with catenated sulfur atoms, are increasingly being investigated in biology. We recently identified pyridoxal phosphate (PLP)-dependent biosynthesis of cysteine persulfide (CysSSH) and related supersulfides by cysteinyl-tRNA synthetase (CARS). Here, we investigated the physiological role of CysSSH in budding yeast (Saccharomyces cerevisiae) by generating a PLP-binding site mutation K109A in CRS1 (the yeast ortholog of CARS), which decreased the synthesis of CysSSH and related supersulfides and also led to reduced chronological aging, effects that were associated with an increased endoplasmic reticulum stress response and impaired mitochondrial bioenergetics. Reduced chronological aging in the K109A mutant could be rescued by using exogenous supersulfide donors. Our findings indicate important roles for CARS in the production and metabolism of supersulfides-to mediate mitochondrial function and to regulate longevity.

  18. Quantitative profiling of supersulfides naturally occurring in dietary meats and beans. International-journal

    Shingo Kasamatsu, Ayaka Kinno, Chiharu Miura, Jun-Ichi Hishiyama, Kensuke Fukui, Shoji Kure, Kazunobu Tsumura, Tomoaki Ida, Tetsuro Matsunaga, Takaaki Akaike, Hideshi Ihara

    Analytical biochemistry 685 115392-115392 2023/11/13

    DOI: 10.1016/j.ab.2023.115392  

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    Sulfur is essential in the inception of life and crucial for maintaining human health. This mineral is primarily supplied through the intake of proteins and is used for synthesizing various sulfur-containing biomolecules. Recent research has highlighted the biological significance of endogenous supersulfides, which include reactive persulfide species and sulfur catenated residues in thiol and proteins. Ingestion of exogenous sulfur compounds is essential for endogenous supersulfide production. However, the content and composition of supersulfides in foods remain unclear. This study investigated the supersulfide profiles of protein-rich foods, including edible animal meat and beans. Quantification of the supersulfide content revealed that natto, chicken liver, and bean sprouts contained abundant supersulfides. In general, the supersulfide content in beans and their derivatives was higher than that in animal meat. The highest proportion (2.15 %) was detected in natto, a traditional Japanese fermented soybean dish. These results suggest that the abundance of supersulfides, especially in foods like natto and bean sprouts, may contribute to their health-promoting properties. Our findings may have significant biological implications and warrant developing novel dietary intervention for the human health-promoting effects of dietary supersulfides abundantly present in protein-rich foods such as natto and bean sprouts.

  19. Untargeted polysulfide omics analysis of alternations in polysulfide production during the germination of broccoli sprouts

    Shingo Kasamatsu, Takuma Owaki, Somei Komae, Ayaka Kinno, Tomoaki Ida, Takaaki Akaike, Hideshi Ihara

    Redox Biology 102875-102875 2023/09

    Publisher: Elsevier BV

    DOI: 10.1016/j.redox.2023.102875  

    ISSN: 2213-2317

  20. Supersulfide catalysis for nitric oxide and aldehyde metabolism. International-journal

    Shingo Kasamatsu, Akira Nishimura, Md Morshedul Alam, Masanobu Morita, Kakeru Shimoda, Tetsuro Matsunaga, Minkyung Jung, Seiryo Ogata, Uladzimir Barayeu, Tomoaki Ida, Motohiro Nishida, Akiyuki Nishimura, Hozumi Motohashi, Takaaki Akaike

    Science advances 9 (33) eadg8631 2023/08/18

    DOI: 10.1126/sciadv.adg8631  

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    Abundant formation of endogenous supersulfides, which include reactive persulfide species and sulfur catenated residues in thiols and proteins (supersulfidation), has been observed. We found here that supersulfides catalyze S-nitrosoglutathione (GSNO) metabolism via glutathione-dependent electron transfer from aldehydes by exploiting alcohol dehydrogenase 5 (ADH5). ADH5 is a highly conserved bifunctional enzyme serving as GSNO reductase (GSNOR) that down-regulates NO signaling and formaldehyde dehydrogenase (FDH) that detoxifies formaldehyde in the form of glutathione hemithioacetal. C174S mutation significantly reduced the supersulfidation of ADH5 and almost abolished GSNOR activity but spared FDH activity. Notably, Adh5C174S/C174S mice manifested improved cardiac functions possibly because of GSNOR elimination and consequent increased NO bioavailability. Therefore, we successfully separated dual functions (GSNOR and FDH) of ADH5 (mediated by the supersulfide catalysis) through the biochemical analysis for supersulfides in vitro and characterizing in vivo phenotypes of the GSNOR-deficient organisms that we established herein. Supersulfides in ADH5 thus constitute a substantial catalytic center for GSNO metabolism mediating electron transfer from aldehydes.

  21. Supersulphides provide airway protection in viral and chronic lung diseases. International-journal

    Tetsuro Matsunaga, Hirohito Sano, Katsuya Takita, Masanobu Morita, Shun Yamanaka, Tomohiro Ichikawa, Tadahisa Numakura, Tomoaki Ida, Minkyung Jung, Seiryo Ogata, Sunghyeon Yoon, Naoya Fujino, Yorihiko Kyogoku, Yusaku Sasaki, Akira Koarai, Tsutomu Tamada, Atsuhiko Toyama, Takakazu Nakabayashi, Lisa Kageyama, Shigeru Kyuwa, Kenji Inaba, Satoshi Watanabe, Péter Nagy, Tomohiro Sawa, Hiroyuki Oshiumi, Masakazu Ichinose, Mitsuhiro Yamada, Hisatoshi Sugiura, Fan-Yan Wei, Hozumi Motohashi, Takaaki Akaike

    Nature communications 14 (1) 4476-4476 2023/07/25

    DOI: 10.1038/s41467-023-40182-4  

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    Supersulphides are inorganic and organic sulphides with sulphur catenation with diverse physiological functions. Their synthesis is mainly mediated by mitochondrial cysteinyl-tRNA synthetase (CARS2) that functions as a principal cysteine persulphide synthase (CPERS). Here, we identify protective functions of supersulphides in viral airway infections (influenza and COVID-19), in aged lungs and in chronic lung diseases, including chronic obstructive pulmonary disease (COPD), idiopathic pulmonary fibrosis (IPF). We develop a method for breath supersulphur-omics and demonstrate that levels of exhaled supersulphides increase in people with COVID-19 infection and in a hamster model of SARS-CoV-2 infection. Lung damage and subsequent lethality that result from oxidative stress and inflammation in mouse models of COPD, IPF, and ageing were mitigated by endogenous supersulphides production by CARS2/CPERS or exogenous administration of the supersulphide donor glutathione trisulphide. We revealed a protective role of supersulphides in airways with various viral or chronic insults and demonstrated the potential of targeting supersulphides in lung disease.

  22. Synthesis of Sulfides and Persulfides Is Not Impeded by Disruption of Three Canonical Enzymes in Sulfur Metabolism. International-journal

    Qamarul Hafiz Zainol Abidin, Tomoaki Ida, Masanobu Morita, Tetsuro Matsunaga, Akira Nishimura, Minkyung Jung, Naim Hassan, Tsuyoshi Takata, Isao Ishii, Warren Kruger, Rui Wang, Hozumi Motohashi, Masato Tsutsui, Takaaki Akaike

    Antioxidants (Basel, Switzerland) 12 (4) 2023/04/03

    DOI: 10.3390/antiox12040868  

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    Reactive sulfur species, or persulfides and polysulfides, such as cysteine hydropersulfide and glutathione persulfide, are endogenously produced in abundance in both prokaryotes and eukaryotes, including mammals. Various forms of reactive persulfides occur in both low-molecular-weight and protein-bound thiols. The chemical properties and great supply of these molecular species suggest a pivotal role for reactive persulfides/polysulfides in different cellular regulatory processes (e.g., energy metabolism and redox signaling). We demonstrated earlier that cysteinyl-tRNA synthetase (CARS) is a new cysteine persulfide synthase (CPERS) and is responsible for the in vivo production of most reactive persulfides (polysulfides). Some researchers continue to suggest that 3-mercaptopyruvate sulfurtransferase (3-MST), cystathionine β-synthase (CBS), and cystathionine γ-lyase (CSE) may also produce hydrogen sulfide and persulfides that may be generated during the transfer of sulfur from 3-mercaptopyruvate to the cysteine residues of 3-MST or direct synthesis from cysteine by CBS/CSE, respectively. We thus used integrated sulfur metabolome analysis, which we recently developed, with 3-MST knockout (KO) mice and CBS/CSE/3-MST triple-KO mice, to elucidate the possible contribution of 3-MST, CBS, and CSE to the production of reactive persulfides in vivo. We therefore quantified various sulfide metabolites in organs derived from these mutant mice and their wild-type littermates via this sulfur metabolome, which clearly revealed no significant difference between mutant mice and wild-type mice in terms of reactive persulfide production. This result indicates that 3-MST, CBS, and CSE are not major sources of endogenous reactive persulfide production; rather, CARS/CPERS is the principal enzyme that is actually involved in and even primarily responsible for the biosynthesis of reactive persulfides and polysulfides in vivo in mammals.

  23. Polysulfide metabolizing enzymes influence SqrR-mediated sulfide-induced transcription by impacting intracellular polysulfide dynamics Peer-reviewed

    Takayuki Shimizu, Tomoaki Ida, Giuliano T Antelo, Yuta Ihara, Joseph N Fakhoury, Shinji Masuda, David P Giedroc, Takaaki Akaike, Daiana A Capdevila, Tatsuru Masuda

    PNAS Nexus 2023/02/10

    DOI: 10.1093/pnasnexus/pgad048  

  24. Cysteine hydropersulfide reduces lipid peroxidation and protects against myocardial ischaemia-reperfusion injury - Are endogenous persulfides mediators of ischaemic preconditioning? International-journal

    Kayleigh Griffiths, Tomoaki Ida, Masanobu Morita, Reece J Lamb, Jordan J Lee, Michael P Frenneaux, Jon M Fukuto, Takaaki Akaike, Martin Feelisch, Melanie Madhani

    Redox biology 60 102605-102605 2023/01/10

    DOI: 10.1016/j.redox.2023.102605  

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    Earlier studies revealed the presence of cysteine persulfide (CysSSH) and related polysulfide species in various mammalian tissues. CysSSH has both antioxidant and oxidant properties, modulates redox-dependent signal transduction and has been shown to mitigate oxidative stress. However, its functional relevance in the setting of myocardial ischaemia-reperfusion injury (IRI) remains unknown. The present study was undertaken to (1) study the dynamics of production and consumption of persulfides under normoxic and hypoxic conditions in the heart, and (2) determine whether exogenous administration of the CysSSH donor, cysteine trisulfide (Cys-SSS-Cys) at the onset of reperfusion rescues functional impairment and myocardial damage by interfering with lipid peroxidation. Utilising a well-established ex vivo Langendorff murine model, we here demonstrate that endogenous tissue concentrations of CysSSH are upregulated when oxygen supply is compromised (global myocardial ischaemia) and rapidly restored to baseline levels upon reperfusion, suggestive of active regulation. In a separate set of experiments, exogenous administration of Cys-SSS-Cys for 10 min at the onset of reperfusion was found to decrease malondialdehyde (MDA) concentrations, formation of 4-hydroxynonenal (4-HNE) protein adducts and rescue the heart from injury. Cys-SSS-Cys also restored post-ischaemic cardiac function, improving both coronary flow and left ventricular developed pressure (LVDP). Taken together, these results support the notion that endogenous CysSSH plays an important role as a "redox preconditioning" agent to combat the oxidative insult in myocardial IRI.

  25. 8-Nitro-cGMP suppresses mineralization by mouse osteoblasts.

    Kotaro Kaneko, Yoichi Miyamoto, Tomoaki Ida, Masanobu Morita, Kentaro Yoshimura, Kei Nagasaki, Kazuki Toba, Risa Sugisaki, Hozumi Motohashi, Takaaki Akaike, Daichi Chikazu, Ryutaro Kamijo

    Journal of clinical biochemistry and nutrition 71 (3) 191-197 2022/11

    DOI: 10.3164/jcbn.21-129  

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    Nitric oxide and reactive oxygen species regulate bone remodeling, which occurs via bone formation and resorption by osteoblasts and osteoclasts, respectively. Recently, we found that 8-nitro-cGMP, a second messenger of nitric oxide and reactive oxygen species, promotes osteoclastogenesis. Here, we investigated the formation and function of 8-nitro-cGMP in osteoblasts. Mouse calvarial osteoblasts were found to produce 8-nitro-cGMP, which was augmented by tumor necrosis factor-α (10 ng/ml) and interleukin-1β (1 ng/ml). These cytokines suppressed osteoblastic differentiation in a NO synthase activity-dependent manner. Exogenous 8-nitro-cGMP (30 μmol/L) suppressed expression of osteoblastic phenotypes, including mineralization, in clear contrast to the enhancement of mineralization by osteoblasts induced by 8-bromo-cGMP, a cell membrane-permeable analog of cGMP. It is known that reactive sulfur species denitrates and degrades 8-nitro-cGMP. Mitochondrial cysteinyl-tRNA synthetase plays a crucial role in the endogenous production of RSS. The expression of osteoblastic phenotypes was suppressed by not only exogenous 8-nitro-cGMP but also by silencing of the Cars2 gene, indicating a role of endogenous 8-nitro-cGMP in suppressing the expression of osteoblastic phenotypes. These results suggest that 8-nitro-cGMP is a negative regulator of osteoblastic differentiation.

  26. Regulation of nitric oxide/reactive oxygen species redox signaling by nNOS splicing variants. International-journal

    Shingo Kasamatsu, Hiroyasu Tsutsuki, Tomoaki Ida, Tomohiro Sawa, Yasuo Watanabe, Takaaki Akaike, Hideshi Ihara

    Nitric oxide : biology and chemistry 120 44-52 2022/03/01

    DOI: 10.1016/j.niox.2022.01.004  

    ISSN: 1089-8603

    eISSN: 1089-8611

  27. GRIM‐19 is a target of mycobacterial Zn 2+ metalloprotease 1 and indispensable for NLRP3 inflammasome activation

    Tomomi Kurane, Tetsuro Matsunaga, Tomoaki Ida, Kazuko Sawada, Akira Nishimura, Masayuki Fukui, Masayuki Umemura, Masaaki Nakayama, Naoya Ohara, Sohkichi Matsumoto, Takaaki Akaike, Goro Matsuzaki, Giichi Takaesu

    The FASEB Journal 36 (1) 2022/01

    Publisher: Wiley

    DOI: 10.1096/fj.202101074rr  

    ISSN: 0892-6638

    eISSN: 1530-6860

  28. Sulfide catabolism ameliorates hypoxic brain injury

    Eizo Marutani, Masanobu Morita, Shuichi Hirai, Shinichi Kai, Robert M.H. Grange, Yusuke Miyazaki, Fumiaki Nagashima, Lisa Traeger, Aurora Magliocca, Tomoaki Ida, Tetsuro Matsunaga, Daniel R. Flicker, Benjamin Corman, Naohiro Mori, Yumiko Yamazaki, Annabelle Batten, Rebecca Li, Tomohiro Tanaka, Takamitsu Ikeda, Akito Nakagawa, Dmitriy N. Atochin, Hideshi Ihara, Benjamin A. Olenchock, Xinggui Shen, Motohiro Nishida, Kenjiro Hanaoka, Christopher G. Kevil, Ming Xian, Donald B. Bloch, Takaaki Akaike, Allyson G. Hindle, Hozumi Motohashi, Fumito Ichinose

    Nature Communications 12 (1) 2021/12

    DOI: 10.1038/s41467-021-23363-x  

    eISSN: 2041-1723

  29. Reprogrammed transsulfuration promotes basal-like breast tumor progression via realigning cellular cysteine persulfidation. International-journal

    Katalin Erdélyi, Tamás Ditrói, Henrik J Johansson, Ágnes Czikora, Noémi Balog, Laxmi Silwal-Pandit, Tomoaki Ida, Judit Olasz, Dorottya Hajdú, Zoltán Mátrai, Orsolya Csuka, Koji Uchida, József Tóvári, Olav Engebraten, Takaaki Akaike, Anne-Lise Børresen Dale, Miklós Kásler, Janne Lehtiö, Péter Nagy

    Proceedings of the National Academy of Sciences of the United States of America 118 (45) 2021/11/09

    DOI: 10.1073/pnas.2100050118  

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    Basal-like breast cancer (BLBC) is the most aggressive subtype of breast tumors with poor prognosis and limited molecular-targeted therapy options. We show that BLBC cells have a high Cys demand and reprogrammed Cys metabolism. Patient-derived BLBC tumors from four different cohorts exhibited elevated expression of the transsulfuration enzyme cystathione β-synthetase (CBS). CBS silencing (shCBS) made BLBC cells less invasive, proliferate slower, more vulnerable to oxidative stress and cystine (CySSCy) deprivation, prone to ferroptosis, and less responsive to HIF1-α activation under hypoxia. shCBS xenograft tumors grew slower than controls and exhibited impaired angiogenesis and larger necrotic areas. Sulfur metabolite profiling suggested that realigned sulfide/persulfide-inducing functions of CBS are important in BLBC tumor progression. Supporting this, the exclusion of serine, a substrate of CBS for producing Cys but not for producing sulfide/persulfide, did not exacerbate CySSCy deprivation-induced ferroptosis in shCBS BLBC cells. Impaired Tyr phosphorylation was detected in shCBS cells and xenografts, likely due to persulfidation-inhibited phosphatase functions. Overexpression of cystathione γ-lyase (CSE), which can also contribute to cellular sulfide/persulfide production, compensated for the loss of CBS activities, and treatment of shCBS xenografts with a CSE inhibitor further blocked tumor growth. Glutathione and protein-Cys levels were not diminished in shCBS cells or xenografts, but levels of Cys persulfidation and the persulfide-catabolizing enzyme ETHE1 were suppressed. Finally, expression of enzymes of the oxidizing Cys catabolism pathway was diminished, but expression of the persulfide-producing CARS2 was elevated in human BLBC tumors. Hence, the persulfide-producing pathways are major targetable determinants of BLBC pathology that could be therapeutically exploited.

  30. Methods in sulfide and persulfide research

    Tsuyoshi Takata, Minkyung Jung, Tetsuro Matsunaga, Tomoaki Ida, Masanobu Morita, Hozumi Motohashi, Xinggui Shen, Christopher G. Kevil, Jon M. Fukuto, Takaaki Akaike

    Nitric Oxide 116 47-64 2021/11

    Publisher: Elsevier BV

    DOI: 10.1016/j.niox.2021.09.002  

    ISSN: 1089-8603

    eISSN: 1089-8611

  31. High-Precision Sulfur Metabolomics Innovated by a New Specific Probe for Trapping Reactive Sulfur Species

    Shingo Kasamatsu, Tomoaki Ida, Taisei Koga, Kosho Asada, Hozumi Motohashi, Hideshi Ihara, Takaaki Akaike

    Antioxidants and Redox Signaling 34 (18) 1407-1419 2021/06/20

    DOI: 10.1089/ars.2020.8073  

    ISSN: 1523-0864

    eISSN: 1557-7716

  32. On-tissue polysulfide visualization by surface-enhanced Raman spectroscopy benefits patients with ovarian cancer to predict post-operative chemosensitivity

    Kazufumi Honda, Takako Hishiki, Sohei Yamamoto, Takehiro Yamamoto, Nami Miura, Akiko Kubo, Mai Itoh, Wei Yu Chen, Masashi Takano, Tomoyuki Yoshikawa, Takahiro Kasamatsu, Shinichiro Sonoda, Hirotoshi Yoshizawa, Seigo Nakamura, Yuichiro Itai, Megumi Shiota, Daisuke Koike, Masayuki Naya, Noriyo Hayakawa, Yoshiko Naito, Tomomi Matsuura, Keiko Iwaisako, Toshihiko Masui, Shinji Uemoto, Kengo Nagashima, Yoshinori Hashimoto, Tomohiro Sakuma, Osamu Matsubara, Wilber Huang, Tomoaki Ida, Takaaki Akaike, Yohei Masugi, Michiie Sakamoto, Tomoyasu Kato, Yoshinori Ino, Hiroshi Yoshida, Hitoshi Tsuda, Nobuyoshi Hiraoka, Yasuaki Kabe, Makoto Suematsu

    Redox Biology 41 2021/05

    DOI: 10.1016/j.redox.2021.101926  

    ISSN: 2213-2317

  33. Loss of cell wall integrity genes cpxA and mrcB causes flocculation in Escherichia coli

    Keita Sugawara, Hayato Toyoda, Mami Kimura, Shunsuke Hayasaka, Hiromi Saito, Hiroshi Kobayashi, Kunio Ihara, Tomoaki Ida, Takaaki Akaike, Eiji Ando, Mamoru Hyodo, Yoshihiro Hayakawa, Shin Hamamoto, Nobuyuki Uozumi

    Biochemical Journal 478 (1) 41-59 2021/01

    DOI: 10.1042/BCJ20200723  

    ISSN: 0264-6021

    eISSN: 1470-8728

  34. Measuring Reactive Sulfur Species and Thiol Oxidation States: Challenges and Cautions in Relation to Alkylation-Based Protocols International-journal Peer-reviewed

    Péter Nagy, Éva Dóka, Tomoaki Ida, Takaaki Akaike

    Antioxidants and Redox Signaling 33 (16) 1174-1189 2020/12/01

    DOI: 10.1089/ars.2020.8077  

    ISSN: 1523-0864

    eISSN: 1557-7716

  35. 8-Nitro-cGMP modulates exocytosis in adrenal chromaffin cells International-journal Peer-reviewed

    Hiroyasu Tsutsuki, Shingo Kasamatsu, Kohei Kunieda, Tomoaki Ida, Tomohiro Sawa, Nobuyuki Sasakawa, Takaaki Akaike, Hideshi Ihara

    Biochemical and Biophysical Research Communications 526 (1) 225-230 2020/05/21

    DOI: 10.1016/j.bbrc.2020.03.045  

    ISSN: 0006-291X

    eISSN: 1090-2104

  36. Control of protein function through oxidation and reduction of persulfidated states International-journal Peer-reviewed

    Dóka, T. Ida, M. Dagnell, Y. Abiko, N. C. Luong, N. Balog, T. Takata, B. Espinosa, A. Nishimura, Q. Cheng, Y. Funato, H. Miki, J. M. Fukuto, J. R. Prigge, E. E. Schmidt, E. S.J. Arnér, Y. Kumagai, T. Akaike, P. Nagy

    Science Advances 6 (1) eaax8358 2020/01/01

    DOI: 10.1126/sciadv.aax8358  

    eISSN: 2375-2548

  37. Long-lasting blood pressure lowering effects of nitrite are NO-independent and mediated by hydrogen peroxide, persulfides, and oxidation of protein kinase G1α redox signalling Peer-reviewed

    Martin Feelisch, Takaaki Akaike, Kayleigh Griffiths, Tomoaki Ida, Oleksandra Prysyazhna, Joanna J. Goodwin, Nicholas D. Gollop, Bernadette O. Fernandez, Magdalena Minnion, Miriam M. Cortese-Krott, Alessandra Borgognone, Rosie M. Hayes, Philip Eaton, Michael P. Frenneaux, Melanie Madhani

    Cardiovascular Research 116 (1) 51-62 2020/01/01

    DOI: 10.1093/cvr/cvz202  

    ISSN: 0008-6363

    eISSN: 1755-3245

  38. Mitochondrial cysteinyl-tRNA synthetase is expressed via alternative transcriptional initiation regulated by energy metabolism in yeast cells Peer-reviewed

    Akira Nishimura, Ryo Nasuno, Yuki Yoshikawa, Minkyung Jung, Tomoaki Ida, Tetsuro Matsunaga, Masanobu Morita, Hiroshi Takagi, Hozumi Motohashi, Takaaki Akaike

    Journal of Biological Chemistry 294 (37) 13781-13788 2019/09/13

    DOI: 10.1074/jbc.RA119.009203  

    ISSN: 0021-9258

    eISSN: 1083-351X

  39. Data-Driven Identification of Hydrogen Sulfide Scavengers

    Chun tao Yang, Yingying Wang, Eizo Marutani, Tomoaki Ida, Xiang Ni, Shi Xu, Wei Chen, Hui Zhang, Takaaki Akaike, Fumito Ichinose, Ming Xian

    Angewandte Chemie - International Edition 58 (32) 10898-10902 2019/08/05

    DOI: 10.1002/anie.201905580  

    ISSN: 1433-7851

    eISSN: 1521-3773

  40. Titelbild: Data‐Driven Identification of Hydrogen Sulfide Scavengers (Angew. Chem. 32/2019) Peer-reviewed

    Chun-tao Yang, Yingying Wang, Eizo Marutani, Tomoaki Ida, Xiang Ni, Shi Xu, Wei Chen, Hui Zhang, Takaaki Akaike, Fumito Ichinose, Ming Xian

    Angewandte Chemie 131 (32) 10877 2019/08

    Publisher: Wiley

    DOI: 10.1002/ange.201908294  

  41. Environmental electrophile-mediated toxicity in mice lacking Nrf2, CSE, or both Peer-reviewed

    Masahiro Akiyama, Takamitsu Unoki, Yasuhiro Shinkai, Isao Ishii, Tomoaki Ida, Takaaki Akaike, Masayuki Yamamoto, Yoshito Kumagai

    Environmental Health Perspectives 127 (6) 67002 2019/06

    DOI: 10.1289/EHP4949  

    ISSN: 0091-6765

    eISSN: 1552-9924

  42. The Uptake and Release of Polysulfur Cysteine Species by Cells: Physiological and Toxicological Implications Peer-reviewed

    Joseph Lin, Masahiro Akiyama, Iris Bica, Faith T. Long, Catherine F. Henderson, Robert N. Goddu, Valeria Suarez, Blaine Baker, Tomoaki Ida, Yasuhiro Shinkai, Peter Nagy, Takaaki Akaike, Jon M. Fukuto, Yoshito Kumagai

    Chemical Research in Toxicology 32 (3) 447-455 2019/03/18

    DOI: 10.1021/acs.chemrestox.8b00340  

    ISSN: 0893-228X

    eISSN: 1520-5010

  43. The Uptake and Release of Polysulfur Cysteine Species by Cells: Physiological and Toxicological Implications International-journal Peer-reviewed

    Lin, Joseph, Akiyama, Masahiro, Bica, Iris, Long, Faith T, Henderson, Catherine F, Goddu, Robert N, Suarez, Valeria, Baker, Blaine, Ida, Tomoaki, Shinkai, Yasuhiro, Nagy, Peter, Akaike, Takaaki, Fukuto, Jon M, Kumagai, Yoshito

    Chemical research in toxicology 32 (3:::SI) 447-455 2019/02

    Publisher: AMER CHEMICAL SOC

    DOI: 10.1021/acs.chemrestox.8b00340  

    ISSN: 1520-5010

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    Hydropersulfides and related polysulfides have recently become topics of significant interest due to their physiological prevalence and proposed biological functions. Currently, examination of the effects of hydropersulfide treatment on cells is difficult due to their lack of inherent stability with respect to disproportionation. Herein, it is reported that the treatment of a variety of cell types with cysteine trisulfide (also known as thiocystine; Cys-SSS-Cys), results in an increase in intracellular hydropersulfide levels (e.g., cysteine hydropersulfide; Cys-SSH, and glutathione hydropersulfide; GSSH). Thus, Cys-SSS-Cys represents a possible pharmacological agent for examining the effects of hydropersulfides on cell function/viability. It has also been found that cells with increased intracellular hydropersulfide levels can export Cys-SSH into the extracellular media. Interestingly, the Cys-SSH is the major hydropersulfide exported by cells, although GSSH is the predominant intracellular species. The possible implications of cellular export are discussed.

  44. Polysulfide stabilization by tyrosine and hydroxyphenyl-containing derivatives that is important for a reactive sulfur metabolomics analysis Peer-reviewed

    Hisyam Abdul Hamid, Akira Tanaka, Tomoaki Ida, Akira Nishimura, Tetsuro Matsunaga, Shigemoto Fujii, Masanobu Morita, Tomohiro Sawa, Jon M. Fukuto, Péter Nagy, Ryouhei Tsutsumi, Hozumi Motohashi, Hideshi Ihara, Takaaki Akaike

    Redox Biology 21 101096 2019/02

    DOI: 10.1016/j.redox.2019.101096  

    ISSN: 2213-2317

  45. The reaction of hydrogen sulfide with disulfides: formation of a stable trisulfide and implications for biological systems Peer-reviewed

    Christopher L. Bianco, Takaaki Akaike, Tomoaki Ida, Peter Nagy, Virag Bogdandi, John P. Toscano, Yoshito Kumagai, Catherine F. Henderson, Robert N. Goddu, Joseph Lin, Jon M. Fukuto

    British Journal of Pharmacology 176 (4) 671-683 2019/02

    DOI: 10.1111/bph.14372  

    ISSN: 0007-1188

    eISSN: 1476-5381

  46. Speciation of reactive sulfur species and their reactions with alkylating agents: do we have any clue about what is present inside the cell? Peer-reviewed

    Virág Bogdándi, Tomoaki Ida, Thomas R. Sutton, Christopher Bianco, Tamás Ditrói, Grielof Koster, Hillary A. Henthorn, Magda Minnion, John P. Toscano, Albert van der Vliet, Michael D. Pluth, Martin Feelisch, Jon M. Fukuto, Takaaki Akaike, Péter Nagy

    British Journal of Pharmacology 176 (4) 646-670 2019/02

    DOI: 10.1111/bph.14394  

    ISSN: 0007-1188

    eISSN: 1476-5381

  47. Oxidation of PKGIα mediates an endogenous adaptation to pulmonary hypertension Peer-reviewed

    Olena Rudyk, Alice Rowan, Oleksandra Prysyazhna, Susanne Krasemann, Kristin Hartmann, Min Zhang, Ajay M. Shah, Clemens Ruppert, Astrid Weiss, Ralph T. Schermuly, Tomoaki Ida, Takaaki Akaike, Lan Zhao, Philip Eaton

    Proceedings of the National Academy of Sciences of the United States of America 116 (26) 13016-13025 2019

    DOI: 10.1073/pnas.1904064116  

    ISSN: 0027-8424

    eISSN: 1091-6490

  48. Reactive Persulfides from Salmonella Typhimurium Downregulate Autophagy-Mediated Innate Immunity in Macrophages by Inhibiting Electrophilic Signaling Peer-reviewed

    Shahzada Khan, Shigemoto Fujii, Tetsuro Matsunaga, Akira Nishimura, Katsuhiko Ono, Tomoaki Ida, Khandaker Ahtesham Ahmed, Tatsuya Okamoto, Hiroyasu Tsutsuki, Tomohiro Sawa, Takaaki Akaike

    Cell Chemical Biology 25 (11) 1403-1413.e4 2018/11/15

    DOI: 10.1016/j.chembiol.2018.08.007  

    ISSN: 2451-9456

    eISSN: 2451-9448

  49. Biological hydropersulfides and related polysulfides – a new concept and perspective in redox biology Peer-reviewed

    Jon M. Fukuto, Louis J. Ignarro, Peter Nagy, David A. Wink, Christopher G. Kevil, Martin Feelisch, Miriam M. Cortese-Krott, Christopher L. Bianco, Yoshito Kumagai, Adrian J. Hobbs, Joseph Lin, Tomoaki Ida, Takaaki Akaike

    FEBS Letters 592 (12) 2140-2152 2018/06

    Publisher: Wiley Blackwell

    DOI: 10.1002/1873-3468.13090  

    ISSN: 0014-5793

    eISSN: 1873-3468

  50. Bright and dark sides of KEAP1-NRF2 system in carcinogenesis Peer-reviewed

    Motohashi Hozumi, Ida Tomoaki, Alam Md. Morshedul, Kitamura Hiroshi, Akaike Takaaki

    FREE RADICAL BIOLOGY AND MEDICINE 120 S18 2018/05/20

    DOI: 10.1016/j.freeradbiomed.2018.04.078  

    ISSN: 0891-5849

  51. Cysteine perthiosulfenic acid (Cys-SSOH): A novel intermediate in thiol-based redox signaling? Peer-reviewed

    David E. Heppner, Milena Hristova, Tomoaki Ida, Ana Mijuskovic, Christopher M. Dustin, Virág Bogdándi, Jon M. Fukuto, Tobias P. Dick, Péter Nagy, Jianing Li, Takaaki Akaike, Albert van der Vliet

    Redox Biology 14 379-385 2018/04

    Publisher: Elsevier B.V.

    DOI: 10.1016/j.redox.2017.10.006  

    ISSN: 2213-2317

  52. Important role of endothelial caveolin-1 in the protective role of endothelium-dependent hyperpolarization against Nitric oxide-mediated nitrative stress in microcirculation in mice Peer-reviewed

    Hiroki Saito, Shigeo Godo, Saori Sato, Akiyo Ito, Yosuke Ikumi, Shuhei Tanaka, Tomoaki Ida, Shigemoto Fujii, Takaaki Akaike, Hiroaki Shimokawa

    Journal of Cardiovascular Pharmacology 71 (2) 113-126 2018/02/01

    Publisher: Lippincott Williams and Wilkins

    DOI: 10.1097/FJC.0000000000000552  

    ISSN: 0160-2446

    eISSN: 1533-4023

  53. Involvement of nitric oxide/reactive oxygen species signaling via 8-nitro-cGMP formation in 1-methyl-4-phenylpyridinium ion-induced neurotoxicity in PC12 cells and rat cerebellar granule neurons International-journal Peer-reviewed

    Kumiko Masuda, Hiroyasu Tsutsuki, Shingo Kasamatsu, Tomoaki Ida, Tsuyoshi Takata, Kikuya Sugiura, Motohiro Nishida, Yasuo Watanabe, Tomohiro Sawa, Takaaki Akaike, Hideshi Ihara

    Biochemical and Biophysical Research Communications 495 (3) 2165-2170 2018/01/15

    DOI: 10.1016/j.bbrc.2017.12.088  

    ISSN: 0006-291X

    eISSN: 1090-2104

  54. Reactive Cysteine Persulphides: Occurrence, Biosynthesis, Antioxidant Activity, Methodologies, and Bacterial Persulphide Signalling Peer-reviewed

    Tomohiro Sawa, Katsuhiko Ono, Hiroyasu Tsutsuki, Tianli Zhang, Tomoaki Ida, Motohiro Nishida, Takaaki Akaike

    Advances in Microbial Physiology 72 1-28 2018/01/01

    DOI: 10.1016/bs.ampbs.2018.01.002  

    ISSN: 0065-2911

  55. Production of reactive persulfide species in chronic obstructive pulmonary disease Peer-reviewed

    Tadahisa Numakura, Hisatoshi Sugiura, Takaaki Akaike, Tomoaki Ida, Shigemoto Fujii, Akira Koarai, Mitsuhiro Yamada, Katsuhiro Onodera, Yuichiro Hashimoto, Rie Tanaka, Kei Sato, Yutaka Shishikura, Taizou Hirano, Satoru Yanagisawa, Naoya Fujino, Tatsuma Okazaki, Tsutomu Tamada, Yasushi Hoshikawa, Yoshinori Okada, Masakazu Ichinose

    Thorax 72 (12) 1074-1083 2017/12/01

    DOI: 10.1136/thoraxjnl-2016-209359  

    ISSN: 0040-6376

    eISSN: 1468-3296

  56. Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics International-journal Peer-reviewed

    Takaaki Akaike, Tomoaki Ida, Fan Yan Wei, Motohiro Nishida, Yoshito Kumagai, Md Morshedul Alam, Hideshi Ihara, Tomohiro Sawa, Tetsuro Matsunaga, Shingo Kasamatsu, Akiyuki Nishimura, Masanobu Morita, Kazuhito Tomizawa, Akira Nishimura, Satoshi Watanabe, Kenji Inaba, Hiroshi Shima, Nobuhiro Tanuma, Minkyung Jung, Shigemoto Fujii, Yasuo Watanabe, Masaki Ohmuraya, Péter Nagy, Martin Feelisch, Jon M. Fukuto, Hozumi Motohashi

    Nature Communications 8 (1) 1177-1177 2017/12/01

    DOI: 10.1038/s41467-017-01311-y  

    eISSN: 2041-1723

  57. Cysteine Hydropersulfide Production Catalyzed by Cysteinyl-tRNA Synthetases Peer-reviewed

    Tomoaki Ida, Akira Nishimura, Masanobu Morita, Hozumi Motohashi, Takaaki Akaike

    FREE RADICAL BIOLOGY AND MEDICINE 112 189-190 2017/11

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    ISSN: 1882-4110

  13. Discovery of supersulfide biosynthesis highly conserved among all organisms

    井田智章, JUNG Minkyung, 松永哲郎, 守田匡伸, 緒方星陵, 高田剛, 海野雄加, 本橋ほづみ, 赤池孝章

    日本細菌学雑誌(Web) 78 (1) 2023

    ISSN: 1882-4110

  14. 新型コロナウイルス感染に関わる呼気・空間オミックス解析

    朝光世志, 緒方星稜, 井田智章, 松永哲郎, JUNG Minkyung, 高田剛, 守田匡伸, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 76th 2023

  15. 脂肪細胞が担う超硫黄分子貯蔵庫としての役割

    海野雄加, 松永哲郎, 井田智章, ジョン ミンギョン, 高田剛, 守田匡伸, 緒方星陵, 本橋ほづみ, 吉沢道人, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 76th 2023

  16. Inhibition of SARS-CoV-2 by supersulfide and its antti-viral effect

    JUNG Minkyung, 松永哲郎, 井田智章, 高田剛, 守田匡伸, 赤池孝章

    日本生体防御学会学術総会講演抄録集 33rd 2022

  17. Elucidation of metabolic mechanism of supersulfur molecule S8 in adipocytes

    海野雄加, 井田智章, 高田剛, 松永哲郎, 守田匡伸, JUNG Minkyung, 吉沢道人, 赤池孝章

    日本生体防御学会学術総会講演抄録集 33rd 2022

  18. Supersulfide activation and infection protection by NADPH oxidoreductase

    高田剛, 井田智章, 松永哲郎, 守田匡伸, JUNG Minkyung, 土屋幸弘, 渡邊泰男, 本橋ほづみ, 吉沢道人, 住本英樹, 赤池孝章

    日本生体防御学会学術総会講演抄録集 33rd 2022

  19. Supersulfides regulate immune responses by binding to TCR/CD3ε-CXXC

    守田匡伸, 山田充啓, 佐々木優作, 井田智章, 松永哲郎, 高田剛, 渡部聡, 稲葉謙次, 石井直人, 杉浦久敏, 本橋ほづみ, 赤池孝章

    日本生体防御学会学術総会講演抄録集 33rd 2022

  20. Breath omics analysis and host defense reserach

    井田智章, 高田剛, 松永哲郎, 守田匡伸, JUNG Minkyung, 本橋ほづみ, 赤池孝章

    日本生体防御学会学術総会講演抄録集 33rd 2022

  21. Aminoacyl-tRNA synthetaseによる超硫黄分子合成機構の解明

    ジョン ミンギョン, 井田智章, 西村明, 松永哲郎, 守田匡伸, 高田剛, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 95th 2022

  22. 呼気オミックスと個別化医療

    アカイケ タカアキ, マツナガ テツロウ, イダ トモアキ, タカタ ツヨシ, モリタ マサノブ, モトハシ ホズミ

    4 (13) 1223-1226 2021/12

    Publisher: 北隆館

    ISSN: 2434-3625

  23. Breathomics and personalized medicine

    赤池孝章, 松永哲郎, 井田智章, 高田剛, JUNG Minkyung, 守田匡伸, 本橋ほづみ

    月刊Precision Medicine 4 (13) 2021

    ISSN: 2434-3625

  24. 新興感染症菌Helicobacter cinaediの骨髄内の潜伏感染と細胞内寄生性の分子機構の解明

    松永 哲郎, 西村 明, 守田 匡伸, 井田 智章, 津々木 博康, 澤 智裕, 河村 好章, 赤池 孝章

    日本細菌学雑誌 74 (1) 104-104 2019/03

    Publisher: 日本細菌学会

    ISSN: 0021-4930

  25. 活性パースルフィドによる硫化水素キノン酸化還元酵素(SQR)を介したミトコンドリア膜電位形成機構の解明

    松永哲郎, 守田匡伸, 西村明, 井田智章, 本橋ほづみ, 赤池孝章

    日本NO学会学術集会プログラム抄録集 19th 2019

  26. タンパク質・核酸の分子修飾 II.細胞質/オルガネラでの分子修飾 酸化還元状態 SH(ポリスルフィド)酸化

    西村明, 井田智章, 赤池孝章

    生体の科学 69 (5) 448‐449-449 2018/10/15

    Publisher: (公財)金原一郎記念医学医療振興財団

    DOI: 10.11477/mf.2425200872  

    ISSN: 0370-9531

    eISSN: 1883-5503

  27. 【レドックス疾患学 酸素・窒素・硫黄活性種はどう作用するのか、どこまで健康・疾患と関わるのか?】 (第3章)レドックスの検出手法、応用など 活性イオウメタボローム イオウ代謝物とレドックスバイオマーカー

    井田 智章, 西村 明, 守田 匡伸

    実験医学 36 (5) 865-873 2018/03

    Publisher: (株)羊土社

    ISSN: 0288-5514

  28. 新興感染症菌Helicobacter cinaediの骨髄内における潜伏感染と細胞内寄生性の解析

    松永哲郎, 西村明, 守田匡伸, 藤井重元, 井田智章, 澤智裕, 河村好章, 赤池孝章

    日本細菌学雑誌(Web) 73 (1) 117(J‐STAGE)-117 2018/02

    Publisher: 日本細菌学会

    ISSN: 1882-4110

  29. 新興感染症菌Helicobacter cinaediの骨髄内における潜伏感染と細胞内寄生性の解析

    松永 哲郎, 西村 明, 守田 匡伸, 藤井 重元, 井田 智章, 澤 智裕, 河村 好章, 赤池 孝章

    日本細菌学雑誌 73 (1) 117-117 2018/02

    Publisher: 日本細菌学会

    ISSN: 0021-4930

  30. NRF2依存性がんの代謝制御とその特徴

    本橋ほづみ, 井田智章, ALAM Md.Morshedul, 北村大志, 赤池孝章

    日本分子腫瘍マーカー研究会プログラム・講演抄録 38th 2018

  31. 活性イオウ分子種によるミトコンドリア膜電位形成機構の解明

    松永哲郎, 守田匡伸, 西村明, 井田智章, 藤井重元, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 91st 2018

  32. ニトロソグルタチオン代謝酵素アルコールデヒドロゲナーゼ5のタンパク質ポリスルフィド化による活性制御機構

    藤井重元, 笠松真吾, MORSHEDUL Alam Md., 井田智章, 守田匡伸, 居原秀, 西村明, 松永哲郎, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 71st 2018

  33. タンパク質・核酸の分子修飾 II.細胞質/オルガネラでの分子修飾 酸化還元状態 ポリスルフィド化

    西村明, 井田智章, 赤池孝章

    生体の科学 69 (5) 2018

    ISSN: 0370-9531

  34. 新規蛍光プローブを用いた活性パースルフィド分子種のイメージング解析

    松永哲郎, 梅澤啓太郎, 神谷真子, 井田智章, 藤井重元, 渡邊泰男, XIAN Ming, 浦野泰照, 赤池孝章

    日本細菌学雑誌(Web) 72 (1) 98(J‐STAGE)-98 2017/02

    Publisher: 日本細菌学会

    ISSN: 1882-4110

  35. システイニルtRNA合成酵素によるミトコンドリア機能制御の解明

    松永哲郎, 井田智章, 魏范研, 澤智裕, 守田匡伸, 西村明, 笠松真吾, 田沼延公, 藤井重元, 島礼, 居原秀, 西田基宏, 西田基宏, 富澤一仁, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 70th 2017

  36. 硫化水素代謝酵素sulfide quinone reductaseの生体における機能解析

    守田匡伸, 松永哲郎, 井田智章, 西村明, 笠松真吾, 藤井重元, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 70th 2017

  37. 酵母におけるシステインパースルフィド合成経路とその生理的役割の解明

    西村明, 那須野亮, 松永哲郎, 井田智章, 笠松真吾, 守田匡伸, 藤井重元, 高木博史, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 70th 2017

  38. イオウ呼吸とイオウストレス:新しいエネルギー代謝とレドックス病態の提案

    赤池孝章, 西村明, 井田智章, 松永哲郎, 守田匡伸, 藤井重元, 本橋ほづみ

    日本酸化ストレス学会学術集会プログラム・抄録集 70th 2017

  39. イオウ呼吸とイオウ毒性(生命進化のイオウパラドックス):ヒトの新しいエネルギー代謝と解毒代謝経路の発見

    赤池孝章, 西村明, 井田智章, 松永哲郎, 守田匡伸, 本橋ほづみ

    衛生薬学・環境トキシコロジー講演要旨集 2017 2017

    ISSN: 0919-2115

  40. ニトロソグルタチオン還元酵素(GSNOR)選択的欠損マウスの開発

    松永哲郎, 西村明, 笠松真吾, ALAM Morshedul, 井田智章, 守田匡伸, 居原秀, 藤井重元, 下田翔, 西田基宏, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 90th 2017

  41. メチル水銀の新たな毒性メカニズム

    西村明, 西村明幸, 笠松真吾, 居原秀, 松永哲郎, 井田智章, 守田匡伸, 藤井重元, 熊谷嘉人, 本橋ほづみ, 西田基宏, 赤池孝章

    東北公衆衛生学会講演集 66th 2017

    ISSN: 0915-549X

  42. 親電子性物質による活性イオウ分子種依存性レドックスシグナルの破綻

    北村篤志, 笠松真吾, 西村明, 井田智章, 西田基宏, 熊谷嘉人, 赤池孝章, 居原秀

    日本生化学会大会(Web) 90th 2017

  43. システインtRNA合成酵素によるミトコンドリア形態および機能の制御

    松永哲郎, 井田智章, 魏范研, 西村明幸, 守田匡伸, 藤井重元, 西田基宏, 西田基宏, 富澤一仁, 本橋ほづみ, 赤池孝章

    日本NO学会学術集会プログラム抄録集 17th 2017

  44. 酵母におけるシステインパースルフィド合成経路と生理的役割の解明

    西村明, 那須野亮, 松永哲郎, 井田智章, 笠松真吾, 守田匡伸, 藤井重元, 高木博史, 赤池孝章

    日本NO学会学術集会プログラム抄録集 17th 2017

  45. 細菌性アミノアシルtRNA合成酵素のパースルフィド産生能に関する研究

    赤司壮一郎, 赤司壮一郎, 西村明, 井田智章, 守田匡伸, 松永哲郎, 笠松真吾, 藤井重元, 西田基宏, 西田基宏, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 70th 2017

  46. アルコールデヒドロゲナーゼ5の酵素活性制御におけるタンパク質ポリスルフィド化機能

    井田智章, 笠松真吾, ALAM Md.Morshedul, 守田匡伸, 居原秀, 西村明, 松永哲郎, 藤井重元, 本橋ほづみ, 赤池孝章

    日本NO学会学術集会プログラム抄録集 17th 2017

  47. アルコールデヒドロゲナーゼ5タンパク質ポリスルフィド化の酵素活性制御機能

    JUNG Minkyung, 西村明, 笠松真吾, ALAM Md. Morshedul, 井田智章, 松永哲郎, 藤井重元, 居原秀, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 70th 2017

  48. アルコールデヒドロゲナーゼ5タンパク質ポリスルフィド化の酵素活性制御機能

    ABDULA Chazia Gluamo, 笠松真吾, 西村明, ALAM Md. Morshedul, 井田智章, 松永哲郎, 藤井重元, 居原秀, 本橋ほづみ, 赤池孝章

    日本細菌学雑誌(Web) 72 (1) 2017

    ISSN: 1882-4110

  49. アミノアシル-tRNA合成酵素のシステインパースルフィド産生能の検討

    薗部武, 工藤梨沙, 西村明, 井田智章, 赤司壮一郎, JUNG Minkyung, 守田匡伸, 松永哲郎, 笠松真吾, 藤井重元, 居原秀, 赤池孝章

    日本細菌学雑誌(Web) 72 (1) 2017

    ISSN: 1882-4110

  50. 大腸菌におけるシステインパースルフィド生成機構

    井田智章, 居原秀, 守田匡伸, 笠松真吾, 松永哲郎, 西村明, 藤井重元, 澤智裕, 赤池孝章

    日本細菌学雑誌(Web) 72 (1) 2017

    ISSN: 1882-4110

  51. 細菌のイオウ呼吸はすべての生物種に保存されている:ほ乳類における新しいエネルギー代謝経路・イオウ呼吸の発見

    赤池孝章, 井田智章, 松永哲郎, 守田匡伸, 笠松真吾, 西村明, 藤井重元, 居原秀, JUNG Minkyung, 赤司壮一郎, 澤智裕, 本橋ほづみ

    日本細菌学雑誌(Web) 72 (1) 2017

    ISSN: 1882-4110

  52. 8-ニトロ-cGMPとタンパク質poly-S-グアニル化による親電子シグナルの可逆的制御

    赤司壮一郎, 笠松真吾, JUNG Minkyung, 松永哲郎, 井田智章, 藤井重元, 澤智裕, 熊谷嘉人, 本橋ほづみ, 赤池孝章

    日本細菌学雑誌(Web) 72 (1) 2017

    ISSN: 1882-4110

  53. 8-ニトロ-cGMPを介した細菌感染防御機構と硫化水素による制御

    笠松真吾, 藤井重元, 松永哲郎, SHAHZADA Khan, 井田智章, 小野勝彦, 澤智裕, 赤池孝章

    日本細菌学雑誌(Web) 72 (1) 2017

    ISSN: 1882-4110

  54. 酵母におけるシステインパースルフィドの生理的役割の解明

    西村明, 那須野亮, 松永哲郎, 井田智章, 笠松真吾, 守田匡伸, 藤井重元, 高木博史, 赤池孝章

    日本細菌学雑誌(Web) 72 (1) 2017

    ISSN: 1882-4110

  55. タンパク質ポリサルファ化の分子メカニズムの解明

    井田 智章, 魏 研范, 笠松 真吾, 守田 匡伸, 松永 哲郎, 居原 秀, 富澤 一仁, 熊谷 嘉人, 澤 智裕, 本橋 ほづみ, 赤池 孝章

    日本生化学会大会プログラム・講演要旨集 89回 [1T14-06(1P 2016/09

    Publisher: (公社)日本生化学会

  56. 健常者における新興感染症菌Helicobacter cinaedi感染スクリーニングと感染疫学研究

    松永 哲郎, 藤井 重元, 井田 智章, 津々木 博康, 澤 智裕, 河村 好章, 赤池 孝章

    日本細菌学雑誌 71 (1) 105-105 2016/02

    Publisher: 日本細菌学会

    ISSN: 0021-4930

  57. 新しい活性パースルフィド産生系の発見

    JUNG Minkyung, 井田智章, 居原秀, 魏范研, 富澤一仁, 笠松真吾, 松永哲郎, 藤井重元, 澤智裕, 赤池孝章

    臨床フリーラジカル会議 32nd 2016

  58. システインtRNA合成酵素によるシステインパースルフィド生成とミトコンドリア機能制御

    井田智章, 魏范研, 富澤一仁, 守田匡伸, 居原秀, 松永哲郎, 笠松真吾, 澤智裕, 藤井重元, 赤池孝章

    日本生体防御学会学術総会講演抄録集 27th 2016

  59. 喘息における呼気凝縮液中の活性イオウ分子種に関する検討

    小野寺克洋, 杉浦久敏, 沼倉忠久, 佐藤慶, 井田智章, 赤池孝章, 一ノ瀬正和

    アレルギー 65 (4/5) 2016

    ISSN: 0021-4884

  60. 生体内ポリサルファー代謝とレドックス制御機能

    藤井重元, 澤智裕, 井田智章, 笠松真吾, 松永哲郎, 守田匡伸, 赤池孝章

    日本生化学会大会(Web) 89th 2016

  61. Ethylmalonic encephalopathy1(ETHE1)による活性イオウ分子種の制御メカニズム

    JUNG Minkyung, 松永哲郎, 笠松真吾, 北村大志, 小野勝彦, 井田智章, 澤智裕, 藤井重元, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 89th 2016

  62. 酵母をモデル生物とした活性イオウ分子種:システインパースルフィドの生理的役割の解明

    西村明, 那須野亮, 松永哲郎, 井田智章, 笠松真吾, 守田匡伸, 藤井重元, 高木博史, 赤池孝章

    日本生化学会大会(Web) 89th 2016

  63. タンパク質ポリサルファ化によるアルコールデヒドロゲナーゼ5の新規酵素活性制御機構

    笠松真吾, ALAM Md. Morshedul, 井田智章, 松永哲郎, 藤井重元, 居原秀, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 69th 2016

  64. 8-NO2-cGMPは骨の伸長を促進する内因性シグナル分子である

    金子児太郎, 金子児太郎, 星野真理江, 星野真理江, 宮本洋一, 赤池孝章, 井田智章, 藤井重元, 近津大地, 馬場一美, 上條竜太郎

    日本酸化ストレス学会学術集会プログラム・抄録集 69th 2016

  65. 活性イオウ分子種の新しい解析法の構築

    HISYAM Abdul Hamid, HISYAM Abdul Hamid, 井田智章, 笠松真吾, 居原秀, 土屋幸弘, 渡邊泰男, 澤智裕, 藤井重元, 赤池孝章

    日本生化学会大会(Web) 89th 2016

  66. CARS2欠損細胞株の作製とポリサルファ化およびミトコンドリア生合成におけるCARS2の機能解析

    守田匡伸, 井田智章, 松永哲郎, 笠松真吾, 藤井重元, 赤池孝章

    日本生化学会大会(Web) 89th 2016

  67. 新しいシステインパースルフィド合成酵素の発見とパースルフィドによるミトコンドリア機能制御機構の解明

    井田智章, 魏范研, 松永哲郎, 西田基宏, 澤智裕, 西村明幸, 守田匡伸, 笠松真吾, 居原秀, 藤井重元, 熊谷嘉人, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 69th 2016

  68. 酵母における活性イオウ分子種:システインパースルフィドの産生とその生理的役割

    西村明, 那須野亮, 松永哲郎, 井田智章, 笠松真吾, 守田匡伸, 藤井重元, 高木博史, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 69th 2016

  69. 活性イオウ分子種によるミトコンドリア機能制御

    赤池孝章, 井田智章

    日本酸化ストレス学会学術集会プログラム・抄録集 69th 2016

  70. 活性イオウ分子種の新規検出法の開発

    HAMID Hisyam Abdul, HAMID Hisyam Abdul, 井田智章, 笠松真吾, 居原秀, 土屋幸弘, 渡邊泰男, 澤智裕, 藤井重元, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 69th 2016

  71. 8-Nitro-cGMPは成長板軟骨で産生される骨伸長因子である

    宮本洋一, 金子児太郎, 金子児太郎, 星野真理江, 赤池孝章, 井田智章, 藤井重元, 馬場一美, 近津大地, 上條竜太郎

    日本酸化ストレス学会学術集会プログラム・抄録集 69th 2016

  72. 8-nitro-cGMPによるメチル水銀毒性の調節機構

    藪川啓司, 石崎健勝, 北村篤志, 笠松真吾, 津々木博康, 井田智章, 藤井重元, 澤智裕, 赤池孝章, 居原秀

    日本酸化ストレス学会学術集会プログラム・抄録集 69th 2016

  73. ヒトCARS2 KO細胞株を用いたタンパク質ポリサルファ化およびミトコンドリア生合成におけるCARS2の機能解析

    守田匡伸, 井田智章, 松永哲郎, 笠松真吾, 藤井重元, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 69th 2016

  74. Helicobacter cinaediの持続感染と動脈硬化促進メカニズム

    松永哲郎, 藤井重元, 井田智章, 小野勝彦, 津々木博康, 澤智裕, 河村好章, 赤池孝章

    日本生体防御学会学術総会講演抄録集 27th 2016

  75. Ethylmalonic encephalopathy 1(ETHE1)による活性イオウ分子種の制御機構

    JUNG Minkyung, 松永哲郎, 井田智章, 笠松真吾, 北村大志, 小野勝彦, 藤井重元, 澤智裕, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 69th 2016

  76. アルコールデヒドロゲナーゼ5の酵素活性制御におけるタンパク質ポリサルファ化の機能

    笠松真吾, MORSHEDUL Alam Md., 井田智章, 松永哲朗, 藤井重元, 居原秀, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 89th 2016

  77. 細菌における新規シグナル伝達物質8-ニトロ-cGMPの生成とその制御機構の解明

    松永哲郎, 井田智章, 小野勝彦, 津々木博康, 藤井重元, 居原秀, 澤智裕, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 69th 2016

  78. 細菌における新規シグナル伝達物質8-ニトロ-cGMPの生成と制御

    松永哲郎, 井田智章, 小野勝彦, 津々木博康, 藤井重元, 澤智裕, 赤池孝章

    日本生化学会大会(Web) 89th 2016

  79. 活性イオウ分子種によるメチル水銀毒性制御機構

    北村篤志, 笠松真吾, 津々木博康, 井田智章, 藤井重元, 澤智裕, 赤池孝章, 居原秀

    日本分子生物学会年会プログラム・要旨集(Web) 39th 2016

  80. 活性イオウ含有分子の再発見とその生物活性

    井田智章, 松永哲郎, 藤井重元, 澤智裕, 赤池孝章

    日本薬理学雑誌 147 (5) 2016

    ISSN: 0015-5691

  81. タンパク質ポリサルファ化の分子メカニズムの解明

    井田 智章, 居原 秀, 魏 范研, 富澤 一仁, 長尾 翌手可, 鈴木 勉, 熊谷 嘉人, 澤 智裕, 笠松 真吾, 本橋 ほづみ, 赤池 孝章

    日本生化学会大会・日本分子生物学会年会合同大会講演要旨集 88回・38回 [3T21p-03(3P0211)] 2015/12

    Publisher: (公社)日本生化学会

  82. 呼吸器疾患の分子病態に迫る 活性イオウ分子による酸化・ニトロ化ストレス制御

    笠松真吾, 井田智章, 藤井重元, 赤池孝章

    Respir Med Res 3 (2) 70-75 2015/04/01

    Publisher: 先端医学社

    ISSN: 2187-8560

  83. 【活性イオウ分子種の生理機能に迫る チオールバイオロジーの新たなステージ】 RSSによる抗酸化・レドックスシグナル制御

    井田 智章, 藤井 重元, 赤池 孝章

    細胞工学 34 (4) 354-357 2015/03

    Publisher: (株)学研メディカル秀潤社

    ISSN: 0287-3796

  84. Helicobacter cinaedi感染による動脈硬化促進作用と感染疫学解析

    松永哲郎, 藤井重元, 井田智章, 河村好章, 赤池孝章

    日本細菌学雑誌 70 (1) 2015

    ISSN: 0021-4930

  85. 活性イオウ分子の親電子シグナル制御異常に起因する有機水銀の新規毒性発現機構の解明

    笠松真吾, 津々木博康, 居原秀, 井田智章, 藤井重元, 澤智裕, 赤池孝章

    日本衛生学雑誌 70 (Supplement) 2015

    ISSN: 0021-5082

  86. 活性システインパースルフィドによる8-ニトロ-cGMP制御機構

    井田智章, 居原秀, 澤智裕, 津々木博康, 笠松真吾, 松永哲郎, 赤司壮一郎, 有本博一, 藤井重元, 赤池孝章

    日本生体防御学会学術総会講演抄録集 26th 2015

  87. HPLC-蛍光検出法によるシステインパースルフィドの新しい定量システムの構築

    ジョン ミンギョン, 井田智章, 笠松真吾, 松永哲郎, 土屋幸弘, 渡邊泰男, 藤井重元, 赤池孝章

    日本NO学会学術集会プログラム抄録集 15th 2015

  88. タンパク質ポリサルファ化を介したアルコールデヒドロゲナーゼ5の酵素活性制御機構

    笠松真吾, ALAM Md. Morshedul, 井田智章, 松永哲郎, 藤井重元, 居原秀, 赤池孝章, 本橋ほづみ

    日本生化学会大会(Web) 88th 2015

  89. 活性イオウ分子種のメタボローム解析法の新たな展開

    JUNG Minkyung, 井田智章, 笠松真吾, 居原秀, 藤井重元, 赤池孝章

    日本生化学会大会(Web) 88th 2015

  90. タンパク質S-ポリチオール化による親電子シグナル制御

    赤司壮一郎, 笠松真吾, JUNG Minkyung, 松永哲郎, 井田智章, 藤井重元, 本橋ほづみ, 澤智裕, 熊谷嘉人, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 68th 2015

  91. タンパク質S-ポリチオール化によるアルコールデヒドロゲナーゼ5の活性制御機構

    藤井重元, MORSHEDUL Alam Md., 井田智章, 松永哲郎, 笠松真吾, 居原秀, 赤池孝章, 本橋ほづみ

    日本NO学会学術集会プログラム抄録集 15th 2015

  92. 活性イオウ分子のNO・活性酸素シグナル制御異常に起因する有機水銀の新規毒性発現機構の解析

    笠松真吾, 笠松真吾, 居原秀, 津々木博康, 津々木博康, 石崎健勝, 井田智章, 藤井重元, 澤智裕, 熊谷嘉人, 赤池孝章

    日本NO学会学術集会プログラム抄録集 15th 2015

  93. 加齢に伴うタンパク質中システインパーサルファイドの変動

    藪川啓司, 津々木博康, 井田智章, 笠松真吾, 赤池孝章, 居原秀

    日本NO学会学術集会プログラム抄録集 15th 2015

  94. アルコールデヒドロゲナーゼ5の活性発現におけるタンパク質S-ポリチオール化の役割

    藤井重元, MD.MORSHEDUL Alam, 井田智章, 松永哲郎, 笠松真吾, 居原秀, 赤池孝章, 本橋ほづみ

    日本酸化ストレス学会学術集会プログラム・抄録集 68th 2015

  95. タンパク質S-ポリチオール化を介する親電子シグナルの制御メカニズム

    赤司壮一郎, 笠松真吾, ジョン ミンギョン, 松永哲郎, 井田智章, 藤井重元, 澤智裕, 熊谷嘉人, 本橋ほづみ, 赤池孝章

    日本NO学会学術集会プログラム抄録集 15th 2015

  96. 有機水銀の神経毒性発現における8-ニトロ-cGMPの役割と活性イオウ分子による制御

    藤井重元, 笠松真吾, 居原秀, 津々木博康, 石崎健勝, 井田智章, 澤智裕, 熊谷嘉人, 赤池孝章

    日本生化学会大会(Web) 88th 2015

  97. 新規活性イオウ分子過硫化水素(HSSH)の生体内生成の検出と生成機序の解明

    松永哲郎, 井田智章, 藤井重元, 渡邊泰男, 澤智裕, 本橋ほづみ, XIAN Ming, 赤池孝章

    日本生化学会大会(Web) 88th 2015

  98. タンパク質poly-S-グアニル化を介した親電子シグナルの可逆的制御

    赤司壮一郎, 笠松真吾, ジョン ミンギョン, 松永哲郎, 井田智章, 藤井重元, 澤智裕, 熊谷嘉人, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 88th 2015

  99. 【炎症-全体像を知り慢性疾患を制御する 炎症シグナル、免疫細胞のダイナミズムからがん・糖尿病などの発症機序と治療標的まで】 (第3章)炎症の慢性化と収束を制御するメディエーター フリーラジカル制御系 硫化水素・活性イオウ分子と炎症

    藤井 重元, 井田 智章, 澤 智裕, 赤池 孝章

    実験医学 32 (17) 2803-2809 2014/11

    Publisher: (株)羊土社

    ISSN: 0288-5514

  100. 生体防御における転写因子Nrf2とグルタチオン依存性ホルムアルデヒド脱水素酵素Adh3による協調作用

    後藤 まき, 北村 大志, 井田 智章, 澤 智裕, 赤池 孝章, 長谷場 健, 秋元 敏雄, 山本 照子, 野, 山本 雅之, 本橋 ほづみ

    日本生化学会大会プログラム・講演要旨集 87回 [4T09p-06] 2014/10

    Publisher: (公社)日本生化学会

  101. 活性酸素と炎症

    井田 智章, 赤池 孝章, 澤 智裕, 藤井 重元

    感染・炎症・免疫 44 (2) 104-109 2014/07

    Publisher: 鳥居薬品(株)

    ISSN: 0387-1010

  102. 新興感染症菌Helicobacter cinaedi感染による動脈硬化の促進作用

    松永哲郎, 岡本竜哉, 藤井重元, 井田智章, 澤智裕, 河村好章, 赤池孝章

    日本細菌学雑誌 69 (1) 2014

    ISSN: 0021-4930

  103. 新興感染症菌Helicobacter cinaedi感染による動脈硬化促進作用についての検討

    松永哲郎, 藤井重元, 岡本竜哉, 井田智章, 澤智裕, 河村好章, 赤池孝章

    東北公衆衛生学会講演集 63rd 2014

    ISSN: 0915-549X

  104. 新興感染症菌Helicobacter cinaedi感染による動脈硬化の促進作用

    松永哲郎, 岡本竜哉, 藤井重元, 井田智章, 澤智裕, 河村好章, 赤池孝章

    日本生体防御学会学術総会講演抄録集 25th 2014

  105. 8-ニトロ-cGMPを介した感染防御機構と細菌が産生する硫化水素による抑制

    松永哲郎, 赤司壮一郎, ジョン ミンキョン, 伊藤千秋, 井田智章, 藤井重元, 澤智裕, 有本博一, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 67th 2014

  106. 8-ニトロ-cGMPによる感染防御機構と細菌由来硫化水素による抑制

    松永哲郎, 赤司壮一郎, JUNG Minkyung, 伊藤千秋, 井田智章, 藤井重元, 澤智裕, 有本博一, 赤池孝章

    日本NO学会学術集会プログラム抄録集 14th 2014

  107. 細菌における新規シグナル伝達物質8-ニトロ-cGMPの生成とその機能

    松永哲郎, 藤井重元, 井田智章, ジョン ミンキョン, 赤司壮一郎, 津々木博康, 居原秀, 澤智裕, 澤智裕, 赤池孝章

    日本生化学会大会(Web) 87th 2014

  108. 感染・炎症・免疫

    井田智章, 赤池孝章, 澤 智裕, 藤井重元

    活性酸素と炎症. (44) 16-21 2014

  109. 【酸化ストレスとその防御】 活性酸素シグナルの調節機構 ROS毒性説から脱却した新たな概念

    居原 秀, 井田 智章, 赤池 孝章

    FRAGRANCE JOURNAL 41 (2) 75-80 2013/02

    Publisher: フレグランスジャーナル社

    ISSN: 0288-9803

  110. 【活性酸素・ガス状分子による恒常性制御と疾患 酸化ストレス応答と低酸素センシングの最新知見からがん、免疫、代謝・呼吸・循環異常、神経変性との関わりまで】 (第4章)活性酸素・ガス状分子研究の最先端技法 硫化水素と硫化水素シグナル関連物質の検出・定量

    居原 秀, 井田 智章

    実験医学 30 (17) 2884-2889 2012/11

    Publisher: (株)羊土社

    ISSN: 0288-5514

  111. NO/活性酸素および硫化水素の2次メッセンジャーの同定と機能解析

    井田智章, 笠松真吾, 國枝恒兵, 池田善和, 藤井重元, 澤智裕, 澤智裕, 居原秀, 赤池孝章

    日本NO学会学術集会プログラム抄録集 12th 2012

  112. 動物細胞,組織における新規のスルフヒドリル化cGMP(8-SH-cGMP)の産生

    國枝恒兵, 笠松真吾, 井田智章, 徳弘桃子, 池田善和, 澤智裕, 赤池孝章, 居原秀

    日本生化学会大会(Web) 85th 2012

  113. 神経系における新規cGMP誘導体8-SH-cGMPの検出

    笠松真吾, 國枝恒兵, 井田智章, 澤智裕, 池田善和, 赤池孝章, 居原秀

    日本生化学会大会(Web) 85th 2012

Show all ︎Show first 5

Books and Other Publications 9

  1. レッドクス疾患学

    井田智章, 西村 明, 守田匡伸

    羊土社 2018/03

  2. ポリスルフィド化

    西村 明, 井田智章, 赤池孝章

    生体の科学 2018

  3. SH(ポリスルフィド)の酸化

    西村 明, 井田智章, 赤池孝章

    生体の科学 2018

  4. 活性イオウ含有分子の再発見とその生物活性

    井田 智章, 松永 哲郎, 藤井 重元, 澤 智裕, 赤池 孝章

    日本薬理学雑誌 2016

  5. 特集 呼吸器疾患の分子病態に迫る

    笠松 真吾, 井田 智章, 藤井 重元

    2015/04

  6. 特集 活性イオウ分子種の生理機能に迫る : チオールバイオロジーの新たなステージ

    井田智章, 藤井重元, 赤池孝章

    細胞工学 学研メディカル秀潤社 2015

  7. 炎症の慢性化と収束を制御するメディエーター

    藤井重元, 井田智章, 澤 智裕, 赤池孝章

    実験医学 2014

  8. 活性酸素と炎症

    井田智章, 赤池孝章, 澤 智裕, 藤井重元

    感染・炎症・免疫 2014

  9. 活性酸素シグナルの調節機構?ROS毒性説から脱却した新たな概念

    居原秀, 井田智章, 赤池孝章

    Fragrance Journal 2013

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Presentations 176

  1. Supersulfides regulate immune response via T cell receptor signaling

    守田匡伸, 山田充啓, 佐々木優作, 井田智章, 松永哲郎, 稲葉謙次, 石井直人, 杉浦久敏, 本橋ほづみ, 赤池孝章

    日本細菌学雑誌(Web) 2022

  2. Infection defense through supersulfides production by NADPH oxidase and nitric oxide synthase

    高田剛, 井田智章, 松永哲郎, 守田匡伸, 土屋幸弘, 渡邊泰男, 本橋ほづみ, 吉沢道人, 住本英樹, 赤池孝章

    日本細菌学雑誌(Web) 2022

  3. Longevity regulation by supersulfide in yeast

    JUNG Minkyung, 西村明, 井田智章, 松永哲郎, 守田匡伸, 高木博史, 本橋ほづみ, 赤池孝章

    日本細菌学雑誌(Web) 2022

  4. Supersulfide metabolism regulated by rhodanese in bacteria and mitochondria

    海野雄加, 松永哲郎, 守田匡伸, JUNG Minkyung, 高田剛, 井田智章, 吉沢道人, 本橋ほづみ, 赤池孝章

    日本細菌学雑誌(Web) 2022

  5. Supersulfide biosynthesis pathway mediated by aminoacyl-tRNA synthetase in E. coli

    井田智章, JUNG Minkyung, 西村明, 松永哲郎, 守田匡伸, 高田剛, 本橋ほづみ, 赤池孝章

    日本細菌学雑誌(Web) 2022

  6. Cross-species conservation and generation of knockout mice of sulfurtransferase, Rhodanese

    佐藤聡, 守田匡伸, JUNG Minkyung, 松永哲郎, 高田剛, 井田智章, 本橋ほづみ, 赤池孝章

    日本細菌学雑誌(Web) 2022

  7. Breath omics and pathogen monitoring

    井田智章, 赤池孝章

    日本細菌学雑誌(Web) 2022

  8. Latent infection of Helicobacter cinaedi in bone marrow sustained by super sulfide

    松永哲郎, 吉田真彰, 西村明, 守田匡伸, 井田智章, 津々木博康, 澤智裕, 本橋ほづみ, 河村好章, 赤池孝章

    日本細菌学雑誌(Web) 2021

  9. アルコールデヒドロゲナーゼ5(ADH5)のニトロソグルタチオン還元酵素(GSNOR)反応の選択的欠損マウスの開発

    松永哲郎, 笠松真吾, 西村明, 井田智章, 守田匡伸, 居原秀, 下田翔, 西田基宏, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2021

  10. 超硫黄分子種によるミトコンドリアエネルギー代謝機構の解明

    松永哲郎, 守田匡伸, 井田智章, 高田剛, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2021

  11. Host defense mechanism by nitric oxide and supersulfides in Salmonella infection

    松永哲郎, 高田剛, 井田智章, 筒井正人, 守田匡伸, 澤智裕, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2021

  12. S-sulfhydryl化タンパク質解析を志向したhydropersulfideラベル化蛍光プローブの開発

    山口遥己, 川口充康, 井田智章, 松永哲郎, 家田直弥, 赤池孝章, 中川秀彦

    日本病院薬剤師会東海ブロック・日本薬学会東海支部合同学術大会講演要旨集 2021

  13. T細胞受容体(TCR)/CD3複合体を標的とした超硫黄分子による免疫応答制御

    守田匡伸, 山田充啓, 佐々木優作, 井田智章, 松永哲郎, 高田剛, 渡部聡, 稲葉謙次, 石井直人, 杉浦久敏, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2021

  14. Discovery of reactive sulfur biosynthesis pathway mediated by aminoacyl-tRNA synthetase in bacteria

    井田智章, JUNG Minkyung, 松永哲郎, 西村明, 守田匡伸, 高田剛, 本橋ほづみ, 赤池孝章

    日本細菌学雑誌(Web) 2021

  15. Host defense mechanism by nitric oxide and super sulfide in Salmonella infection

    吉田真彰, 松永哲郎, 高田剛, 井田智章, 筒井正人, 守田匡伸, 澤智裕, 赤池孝章

    日本細菌学雑誌(Web) 2021

  16. NADPHオキシダーゼおよび一酸化窒素合成酵素による超硫黄活性化メカニズム

    高田剛, 井田智章, 松永哲郎, 守田匡伸, JUNG Minkyung, 土屋幸弘, 渡邊泰男, 本橋ほづみ, 住本英樹, 赤池孝章

    日本生化学会大会(Web) 2021

  17. 造血幹細胞における超硫黄分子の役割

    村上昌平, ZHAO Mingyue, 守田匡伸, 松永哲郎, 井田智章, 赤池孝章, 本橋ほづみ

    日本生化学会大会(Web) 2021

  18. 新規アルキル化試薬N-iodoacetyl tyrosine methyl esterを用いた超硫黄メタボローム・プロテオーム解析系の構築

    笠松真吾, 井田智章, 古賀大聖, 浅田康勝, 本橋ほづみ, 赤池孝章, 居原秀

    日本生化学会大会(Web) 2021

  19. 超硫黄化タンパク質の特異的検出法:新規超硫黄ビオチンスイッチ法

    JUNG Minkyung, 笠松真吾, 井田智章, 松永哲郎, 守田匡伸, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2021

  20. 超硫黄代謝物解析と呼気オミックスへの展開

    井田智章, 松永哲郎, 高田剛, 守田匡伸, JUNG Minkyung, 澤智裕, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2021

  21. Supersulfides regulate immune response via T cell receptor (TCR) signaling

    守田匡伸, 山田充啓, 佐々木優作, 井田智章, 松永哲郎, 高田剛, 渡部聡, 稲葉謙次, 石井直人, 杉浦久敏, 本橋ほづみ, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2021

  22. Supersulfide host defense and its omics development

    井田智章, 松永哲郎, 高田剛, 守田匡伸, JUNG Minkyung, 澤智裕, 本橋ほづみ, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2021

  23. Development of preventive and therapeutic drug for novel coronavirus infectious disease by supersulfide

    JUNG Minkyung, 松永哲郎, 守田匡伸, 井田智章, 高田剛, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2021

  24. A molecular mechanism of IL-β inhibition by mycobacterial effector protein

    藏根友美, 高江洲義一, 高江洲義一, 松永哲郎, 井田智章, 澤田和子, 梅村正幸, 梅村正幸, 赤池孝章, 松崎吾朗, 松崎吾朗

    日本生体防御学会学術総会講演抄録集 2021

  25. Mechanism of supersulfides activation by NADPH oxidase and nitric oxide synthase in host defense

    高田剛, 井田智章, 松永哲郎, 守田匡伸, JUNG Minkyung, 土屋幸弘, 渡邊泰男, 本橋ほづみ, 住本英樹, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2021

  26. NO合成酵素およびNADPHオキシダーゼによる超硫黄種活性化機構の解明

    高田剛, 井田智章, 松永哲郎, 守田匡伸, JUNG Minkyung, 土屋幸弘, 渡邊泰男, 本橋ほづみ, 住本英樹, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2021

  27. 硫化水素キノン酸化還元酵素(SQR)を介した超硫黄分子による種横断的なミトコンドリア硫黄呼吸

    守田匡伸, 西村明, 井田智章, 松永哲郎, 高田剛, ジョン ミンキョン, 田中智弘, 西田基宏, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2021

  28. 超硫黄による新型コロナウイルス感染症(COVID-19)の予防・治療法の開発

    ジョン ミンキョン, 松永哲郎, 守田匡伸, 井田智章, 高田剛, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2021

  29. システインパースルフィド合成酵素の酵素反応機構とその機能解析

    井田智章, 守田匡伸, 松永哲郎, JUNG Minkyung, 高田剛, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2021

  30. Reactive sulfur species protection against influenza virus-induced pneumonia

    守田匡伸, 滝田克也, 佐野寛仁, 杉浦久敏, 市川朋宏, 沼倉忠久, 井田智章, 山田充啓, 京極自彦, 松永哲郎, 本橋ほづみ, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2020

  31. Development of prevention and therapeutics for novel coronavirus infections by reactive sulfur species

    松永哲郎, 井田智章, 高田剛, JUNG Minkyung, 澤智裕, 守田匡伸, 本橋ほづみ, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2020

  32. 硫化水素キノン酸化還元酵素(SQR)を介したミトコンドリアエネルギー代謝機構の解明

    松永哲郎, 守田匡伸, 西村明, 井田智章, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2020

  33. Mechanism of protein translation-coupled cysteine persulfide biosynthesis in bacteria

    松永哲郎, 井田智章, 西村明, JUNG Minkyung, 守田匡伸, 澤智裕, 居原秀, 本橋ほづみ, 本橋ほづみ, 赤池孝章

    日本細菌学雑誌(Web) 2020

  34. 硫化水素キノン酸化還元酵素(SQR)による硫化水素の解毒機構と生理機能の解明

    松永哲郎, 守田匡伸, 西村明, 井田智章, 本橋ほづみ, 赤池孝章

    日本衛生学雑誌(Web) 2020

  35. Development of breath omics for SARS-CoV-2 infection

    井田智章, 高田剛, 守田匡伸, 松永哲郎, JUNG Minkyung, 澤智裕, 杉浦久敏, 本橋ほづみ, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2020

  36. Reactive sulfur metabolism mediated by nitric oxide synthase and NADPH oxidase and its host defense mechanism

    高田剛, 井田智章, 松永哲郎, 守田匡伸, 土屋幸弘, 渡邊泰男, 住本英樹, 本橋ほづみ, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2020

  37. NADPHオキシダーゼおよび一酸化窒素合成酵素による新規活性硫黄代謝メカニズムの解明

    高田剛, 井田智章, 松永哲郎, 守田匡伸, 土屋幸弘, 渡邊泰男, 住本英樹, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2020

  38. Reactive sulfur remodeling by by NADPH oxidase and host defense mechanism

    井田智章, 松永哲郎, 守田匡伸, 高田剛, 本橋ほづみ, 住本英樹, 赤池孝章

    日本細菌学雑誌(Web) 2020

  39. Novel redox signaling by plasma irradiation regulates cardiac homeostasis

    田中智弘, 田中智弘, 田中智弘, 佐々木渉太, 金子俊郎, 井田智章, 赤池孝章, 西田基宏, 西田基宏, 西田基宏

    応用物理学会秋季学術講演会講演予稿集(CD-ROM) 2020

  40. Inhibition of SARS-CoV2 cysteine proteases by selenium-containing compounds

    羽深友哉, 外山喬士, JUNG Minkyung, 井田智章, 守田匡伸, 有澤美枝子, 赤池孝章, 斎藤芳郎

    衛生薬学・環境トキシコロジー講演要旨集 2020

  41. A molecular mechanism of IL-1β inhibition by mycobacterial effector protein

    高江洲義一, 高江洲義一, 藏根友美, 澤田和子, 西村明, 松永哲郎, 井田智章, 梅村正幸, 梅村正幸, 赤池孝章, 松崎吾朗, 松崎吾朗

    日本生体防御学会学術総会講演抄録集 2020

  42. ミトコンドリア・イオウ呼吸選択的sulfide-quinone oxidoreductase欠損マウスの開発および機能解析

    守田匡伸, 井田智章, 松永哲郎, 田中智弘, 西田基宏, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2020

  43. 酵母における活性イオウ分子による寿命制御

    JUNG Minkyung, 西村明, 井田智章, 守田匡伸, 松永哲郎, 高木博史, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2020

  44. 新規システインパースルフィド合成酵素の同定と酵素反応機構の解明

    井田智章, 西村明, 守田匡伸, JUNG Minkyung, 松永哲郎, 居原秀, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2020

  45. 活性イオウ分子種特異的新規アルキル化試薬の合成

    笠松真吾, 井田智章, 浅田康勝, 古賀大聖, 坂本拓斗, 赤池孝章, 居原秀

    日本酸化ストレス学会学術集会プログラム・抄録集 2020

  46. プラズマ照射による新規レドックスシグナル形成とその生理学的意義の解明

    田中智弘, 佐々木渉太, 金子俊郎, 井田智章, 赤池孝章, 西田基宏, 西田基宏, 西田基宏

    日本酸化ストレス学会学術集会プログラム・抄録集 2020

  47. 新規アルキル化剤を用いた活性イオウ分子種の網羅的検出

    浅田康勝, 笠松真吾, 古賀大聖, 坂本拓斗, 井田智章, 赤池孝章, 居原秀

    日本酸化ストレス学会学術集会プログラム・抄録集 2020

  48. 活性パースルフィドによる硫化水素キノン酸化還元酵素(SQR)を介したミトコンドリア膜電位形成機構の解明

    松永哲郎, 守田匡伸, 西村明, 井田智章, 本橋ほづみ, 赤池孝章

    日本NO学会学術集会プログラム抄録集 2019/06/01

  49. 新興感染症菌Helicobacter cinaediの骨髄内の潜伏感染と細胞内寄生性の分子機構の解明

    松永 哲郎, 西村 明, 守田 匡伸, 井田 智章, 津々木 博康, 澤 智裕, 河村 好章, 赤池 孝章

    日本細菌学雑誌 2019/03

  50. Metabolic Features of NRF2-addicted Cancer Cells

    Motohashi Hozumi, Ida Tomoaki, Morshedul Alam, Kitamura Hiroshi, Akaike Takaaki

    Japan Journal of Molecular Tumor Marker Research 2019

  51. Latent infection and intracellular parasitism in bone marrow by Helicobacter cinaedi

    松永哲郎, 西村明, 守田匡伸, 井田智章, 津々木博康, 澤智裕, 河村好章, 赤池孝章

    日本細菌学雑誌(Web) 2019

  52. 硫化水素キノン酸化還元酵素(SQR)によるミトコンドリアにおけるイオウ依存型エネルギー代謝機構の解明

    松永哲郎, 守田匡伸, 西村明, 井田智章, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2019

  53. Biosynthesis pathway of reactive persulfides in photosynthetic bacteria

    JUNG Minkyung, 雨宮大雅, 井田智章, 解良康太, 西村明, 本橋ほづみ, 魚住信之, 赤池孝章

    日本細菌学雑誌(Web) 2019

  54. Biosynthesis pathway and physiological functions of reactive persulfides in yeast

    西村明, 高木博史, 井田智章, 守田匡伸, 松永哲郎, 本橋ほづみ, 赤池孝章

    日本細菌学雑誌(Web) 2019

  55. Novel cysteine persulfide synthase ubiquitously expressed among all organisms

    井田智章, 守田匡伸, 松永哲郎, 西村明, 居原秀, 澤智裕, 本橋ほづみ, 赤池孝章

    日本細菌学雑誌(Web) 2019

  56. 活性パースルフィドの種横断的な生理機能の解明

    西村明, 井田智章, 守田匡伸, 松永哲郎, 高木博史, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2019

  57. ゲノム編集によるミトコンドリア/イオウ呼吸選択的硫化水素キノン酸化還元酵素(SQR)欠損マウスの開発

    守田匡伸, 井田智章, 田中智弘, 松永哲郎, 西村明, 西田基宏, 本橋ほづみ, 赤池孝章

    日本NO学会学術集会プログラム抄録集 2019

  58. 活性イオウ分子によるエネルギー代謝制御

    守田匡伸, 井田智章, 西村明, 田中智弘, 松永哲郎, 西田基宏, 本橋ほづみ, 赤池孝章

    がんと代謝研究会プログラム&抄録集 2019

  59. 種横断的な活性パースルフィド産生経路とその生理的意義の解明

    西村明, 井田智章, 守田匡伸, 松永哲郎, 高木博史, 本橋ほづみ, 赤池孝章

    日本NO学会学術集会プログラム抄録集 2019

  60. ミトコンドリア選択的硫化水素キノン還元酵素(SQR)欠損マウスは致死性のエネルギー代謝不全を示す

    守田匡伸, 松永哲郎, ABIDIN Qamarul Hafiz Zainol, 井田智章, 田中智弘, 西村明, 西田基宏, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2019

  61. 活性イオウ安定化と高精度イオウ代謝解析法の確立

    井田智章, 松永哲郎, 西村明, 守田匡伸, 居原秀, 澤智裕, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2019

  62. 活性イオウ構造保護を目的とした新規アルキル化剤の作製

    田中アキラ, 井田智章, 赤池孝章, 居原秀

    日本酸化ストレス学会学術集会プログラム・抄録集 2019

  63. ミトコンドリア・イオウ呼吸選択的硫化水素キノン酸化還元酵素(SQR)欠損マウスの開発と機能解析

    守田匡伸, 井田智章, 田中智弘, 松永哲郎, 西村明, 西田基宏, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2019

  64. 種横断的な活性パースルフィド産生経路とその生理的意義の解明

    西村明, 井田智章, 守田匡伸, 松永哲郎, 高木博史, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2019

  65. 硫化水素キノン酸化還元酵素(SQR)を介したミトコンドリアにおけるイオウ依存型エネルギー形成機構の解明

    大野木孝嘉, 松永哲郎, 守田匡伸, 西村明, 井田智章, 赤池孝章, 本橋ほづみ

    日本酸化ストレス学会学術集会プログラム・抄録集 2019

  66. Mitochondria-specific SQR deficiency in mice causes lethal impairment of sulfur respiration

    Masanobu Morita, Tomoaki Ida, Tomohiro Tanaka, Tetsuro Matsunaga, Akira Nishimura, Shigemoto Fujii, Motohiro Nishida, Hozumi Motohashi, Takaaki Akaike

    FREE RADICAL BIOLOGY AND MEDICINE 2018/11

  67. 活性イオウ分子種によるミトコンドリア膜電位形成機構の解明

    松永哲郎, 守田匡伸, 西村明, 井田智章, 藤井重元, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2018/09

  68. 活性パースルフィドによるミトコンドリア膜電位形成機構の解明

    松永哲郎, 守田匡伸, 南嶋洋司, 西村明, 井田智章, 藤井重元, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2018/04/19

  69. ニトロソグルタチオン代謝酵素アルコールデヒドロゲナーゼ5のタンパク質ポリスルフィド化による活性制御機構

    藤井重元, 笠松真吾, MORSHEDUL Alam Md, 井田智章, 守田匡伸, 居原秀, 西村明, 松永哲郎, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2018/04/19

  70. 新興感染症菌Helicobacter cinaediの骨髄内における潜伏感染と細胞内寄生性の解析

    松永 哲郎, 西村 明, 守田 匡伸, 藤井 重元, 井田 智章, 澤 智裕, 河村 好章, 赤池 孝章

    日本細菌学雑誌 2018/02

  71. 新興感染症菌Helicobacter cinaediの骨髄内における潜伏感染と細胞内寄生性の解析

    松永哲郎, 西村明, 守田匡伸, 藤井重元, 井田智章, 澤智裕, 河村好章, 赤池孝章

    日本細菌学雑誌(Web) 2018/02

  72. NRF2による生体防御とがんの悪性化

    本橋ほづみ, 井田智章, ALAM Md. Morshedul, 北村大志, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2018

  73. NRF2による代謝リプログラミングとがんの悪性化

    本橋ほづみ, 井田智章, MORSHEDUL Alam Md., 北村大志, 赤池孝章

    日本抗加齢医学会総会プログラム・抄録集 2018

  74. 病原細菌の活性パースルフィド産生によるオートファジー制御と生体防御異常

    西村明, 松永哲郎, 藤井重元, 井田智章, 小野勝彦, 津々木博康, 澤智裕, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2018

  75. 硫化水素解毒酵素sulfide-quinone oxidoreductaseの機能解析

    西村明, 守田匡伸, 南嶋洋司, 井田智章, 松永哲郎, 藤井重元, 本橋ほづみ, 赤池孝章

    Journal of Toxicological Sciences 2018

  76. 種横断的なシステインパースルフィド産生経路とその生理的意義

    西村明, 井田智章, 守田匡伸, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2018

  77. システイニルtRNA合成酵素によるパースルフィド合成制御機構の解明

    井田智章, 西村明, 守田匡伸, 松永哲郎, 澤智裕, 居原秀, 藤井重元, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2018

  78. ミトコンドリア/イオウ呼吸選択的sulfide-quinone reductase(SQR:硫化水素キノン還元酵素)欠損マウスの開発

    守田匡伸, 井田智章, 松永哲郎, 西村明, 藤井重元, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2018

  79. システイニルtRNA合成酵素のパースルフィド合成制御機構

    井田智章, 西村明, 守田匡伸, 松永哲郎, 澤智裕, 居原秀, 藤井重元, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2018

  80. ミトコンドリア/イオウ呼吸選択的硫化水素キノン還元酵素(SQR)欠損マウスの開発および機能解析

    守田匡伸, 井田智章, 田中智弘, 松永哲郎, 西村明, 藤井重元, 西田基宏, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2018

  81. 種横断的新しいシステインパースルフィド合成酵素の発見

    井田智章, 守田匡伸, 西村明, 松永哲郎, 居原秀, 澤智裕, 藤井重元, 本橋ほづみ, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2018

  82. Environmental electrophilic stress caused by impairment of endogenous persulfide detoxification

    AKAIKE Takaaki, IDA Tomoaki, IHARA Hideshi, NISHIDA Motohiro

    Annual Meeting of the Japanese Society of Toxicology 2017

    More details Close

    メチル水銀(MeHg)などの環境親電子物質による細胞毒性発現機構は、これまで、強力な親電子性によるタンパク質の不可逆的アルキル化や細胞レベルでの酸化ストレス誘導などにより説明されてきた。一方我々は、MeHgが、システインパースルフィドなどの活性イオウ分子種により代謝制御されることを明らかにした。そこで本講演では、親電子毒性を、システインパースルフィドの分解代謝によるレドックスシグナルおよびミトコンドリア機能制御異常という視点から考察する。例えば、MeHg処理による細胞内レドックスシグナルへの影響を、蛍光イメージング解析および質量分析を用いて検討すると、MeHg処理による活性イオウ分子産生の減少、内因性レドックス子シグナル分子である8-nitro-cGMP産生の増加が認められる。また、MeHg処理により、8-nitro-cGMP 依存的にH-RasとERK1/2の活性化と細胞老化が誘発される。さらに、活性イオウ分子種は、Drp1(dymanin-related protein 1)を負に制御しているが、MeHg曝露によってその制御が破綻し、Drp1の異常活性化によりミコトンドリアが断片化し、ミトコンドリア機能が低下する。よって、親電子細胞毒性の新しい発現機構として、親電子物質による活性イオウ分子の枯渇を介するレッドクスシグナルとミトコンドリア機能制御の破綻が明らかとなった。

  83. アミノアシル‐tRNA合成酵素のシステインパースルフィド産生能の検討

    薗部武, 工藤梨沙, 西村明, 井田智章, 赤司壮一郎, JUNG Minkyung, 守田匡伸, 松永哲郎, 笠松真吾, 藤井重元, 居原秀, 赤池孝章

    日本細菌学雑誌(Web) 2017

  84. タンパク質ポリサルファ化の分子メカニズムの解明

    井田 智章, 魏 研范, 笠松 真吾, 守田 匡伸, 松永 哲郎, 居原 秀, 富澤 一仁, 熊谷 嘉人, 澤 智裕, 本橋 ほづみ, 赤池 孝章

    日本生化学会大会プログラム・講演要旨集 2016/09

  85. 細菌における新規シグナル伝達物質8‐ニトロ‐cGMPの生成と制御

    松永哲郎, 井田智章, 小野勝彦, 津々木博康, 藤井重元, 澤智裕, 赤池孝章

    日本生化学会大会(Web) 2016/09

  86. 活性イオウ分子種によるミトコンドリア機能制御

    赤池孝章, 井田智章

    日本酸化ストレス学会学術集会プログラム・抄録集 2016/08/30

  87. 8‐Nitro‐cGMPは成長板軟骨で産生される骨伸長因子である

    宮本洋一, 金子児太郎, 金子児太郎, 星野真理江, 赤池孝章, 井田智章, 藤井重元, 馬場一美, 近津大地, 上條竜太郎

    日本酸化ストレス学会学術集会プログラム・抄録集 2016/08/30

  88. 8‐NO2‐cGMPは骨の伸長を促進する内因性シグナル分子である

    金子児太郎, 金子児太郎, 星野真理江, 星野真理江, 宮本洋一, 赤池孝章, 井田智章, 藤井重元, 近津大地, 馬場一美, 上條竜太郎

    日本酸化ストレス学会学術集会プログラム・抄録集 2016/08/30

  89. 細菌における新規シグナル伝達物質8‐ニトロ‐cGMPの生成とその制御機構の解明

    松永哲郎, 井田智章, 小野勝彦, 津々木博康, 藤井重元, 居原秀, 澤智裕, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2016/08/30

  90. 1‐Methyl‐4‐phenylpyridinium(MPP+)誘導性の神経毒性はNO/ROSシグナルにより制御されている

    垣花優希, 津々木博康, 吉岡寿, 桝田くみこ, 笠松真吾, 井田智章, 澤智裕, 赤池孝章, 居原秀

    日本酸化ストレス学会学術集会プログラム・抄録集 2016/08/30

  91. Ethylmalonic encephalopathy 1(ETHE1)による活性イオウ分子種の制御機構

    JUNG Minkyung, 松永哲郎, 井田智章, 笠松真吾, 北村大志, 小野勝彦, 藤井重元, 澤智裕, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2016/08/30

  92. 活性イオウ分子種の新規検出法の開発

    HAMID Hisyam Abdul, HAMID Hisyam Abdul, 井田智章, 笠松真吾, 居原秀, 土屋幸弘, 渡邊泰男, 澤智裕, 藤井重元, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2016/08/30

  93. タンパク質ポリサルファ化によるアルコールデヒドロゲナーゼ5の新規酵素活性制御機構

    笠松真吾, ALAM Md. Morshedul, 井田智章, 松永哲郎, 藤井重元, 居原秀, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2016/08/30

  94. 酵母における活性イオウ分子種:システインパースルフィドの産生とその生理的役割

    西村明, 那須野亮, 松永哲郎, 井田智章, 笠松真吾, 守田匡伸, 藤井重元, 高木博史, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2016/08/30

  95. 8‐nitro‐cGMPによるメチル水銀毒性の調節機構

    藪川啓司, 石崎健勝, 北村篤志, 笠松真吾, 津々木博康, 井田智章, 藤井重元, 澤智裕, 赤池孝章, 居原秀

    日本酸化ストレス学会学術集会プログラム・抄録集 2016/08/30

  96. ヒトCARS2 KO細胞株を用いたタンパク質ポリサルファ化およびミトコンドリア生合成におけるCARS2の機能解析

    守田匡伸, 井田智章, 松永哲郎, 笠松真吾, 藤井重元, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2016/08/30

  97. 新しいシステインパースルフィド合成酵素の発見とパースルフィドによるミトコンドリア機能制御機構の解明

    井田智章, 魏范研, 松永哲郎, 西田基宏, 澤智裕, 西村明幸, 守田匡伸, 笠松真吾, 居原秀, 藤井重元, 熊谷嘉人, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2016/08/30

  98. Nitrative signal through formation of 8-nitroguanosine during differentiation of 3T3-L1 preadipocytes

    Yuka Unno, Teruo Akuta, Tomoaki Ida, Tomohiro Sawa, Yasuo Ono, Takaaki Akaike

    The 16th Annual Scientific Meeting of the Nitric Oxide Society of Japan / The 9th Internatinal Conference on the Biology, Chemistry, and Therapeutic Applications of Nitric Oxide. 2016/05

  99. 成人喘息病態 喘息における呼気凝縮液中の活性イオウ分子種に関する検討

    小野寺 克洋, 杉浦 久敏, 沼倉 忠久, 佐藤 慶, 井田 智章, 赤池 孝章, 一ノ瀬 正和

    アレルギー 2016/05

  100. COPD患者肺における活性イオウ分子種の産生に関する検討

    沼倉 忠久, 杉浦 久敏, 井田 智章, 佐藤 慶, 田中 里江, 小野寺 克洋, 橋本 祐一郎, 宍倉 裕, 阿部 恭子, 平野 泰三, 山田 充啓, 小荒井 晃, 藤井 重元, 赤池 孝章, 一ノ瀬 正和

    日本呼吸器学会誌 2016/03

  101. 大腸菌システインtRNA合成酵素による新規システインパースルフィド生成機構の解明

    赤司 壮一郎, 井田 智章, 居原 秀, Wei Fanyan, 富澤 一仁, 笠松 真吾, 松永 哲郎, 藤井 重元, 澤 智裕, 赤池 孝章

    日本細菌学雑誌 2016/02

  102. 健常者における新興感染症菌Helicobacter cinaedi感染スクリーニングと感染疫学研究

    松永 哲郎, 藤井 重元, 井田 智章, 津々木 博康, 澤 智裕, 河村 好章, 赤池 孝章

    日本細菌学雑誌 2016/02

  103. Helicobacter cinaediの持続感染と動脈硬化促進メカニズム

    松永哲郎, 藤井重元, 井田智章, 小野勝彦, 津々木博康, 澤智裕, 河村好章, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2016

  104. 生体内ポリサルファー代謝とレドックス制御機能

    藤井重元, 澤智裕, 井田智章, 笠松真吾, 松永哲郎, 守田匡伸, 赤池孝章

    日本生化学会大会(Web) 2016

  105. アルコールデヒドロゲナーゼ5の酵素活性制御におけるタンパク質ポリサルファ化の機能

    笠松真吾, MORSHEDUL Alam Md, 井田智章, 松永哲朗, 藤井重元, 居原秀, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2016

  106. システインtRNA合成酵素によるシステインパースルフィド生成とミトコンドリア機能制御

    井田智章, 魏范研, 富澤一仁, 守田匡伸, 居原秀, 松永哲郎, 笠松真吾, 澤智裕, 藤井重元, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2016

  107. CARS2欠損細胞株の作製とポリサルファ化およびミトコンドリア生合成におけるCARS2の機能解析

    守田匡伸, 井田智章, 松永哲郎, 笠松真吾, 藤井重元, 赤池孝章

    日本生化学会大会(Web) 2016

  108. 活性イオウ分子種によるメチル水銀毒性制御機構

    北村篤志, 笠松真吾, 津々木博康, 井田智章, 藤井重元, 澤智裕, 赤池孝章, 居原秀

    日本分子生物学会年会プログラム・要旨集(Web) 2016

  109. 活性イオウ分子種の新しい解析法の構築

    HISYAM Abdul Hamid, HISYAM Abdul Hamid, 井田智章, 笠松真吾, 居原秀, 土屋幸弘, 渡邊泰男, 澤智裕, 藤井重元, 赤池孝章

    日本生化学会大会(Web) 2016

  110. 酵母をモデル生物とした活性イオウ分子種:システインパースルフィドの生理的役割の解明

    西村明, 那須野亮, 松永哲郎, 井田智章, 笠松真吾, 守田匡伸, 藤井重元, 高木博史, 赤池孝章

    日本生化学会大会(Web) 2016

  111. Ethylmalonic encephalopathy1(ETHE1)による活性イオウ分子種の制御メカニズム

    JUNG Minkyung, 松永哲郎, 笠松真吾, 北村大志, 小野勝彦, 井田智章, 澤智裕, 藤井重元, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2016

  112. 新しい活性パースルフィド産生系の発見

    JUNG Minkyung, 井田智章, 居原秀, 魏范研, 富澤一仁, 笠松真吾, 松永哲郎, 藤井重元, 澤智裕, 赤池孝章

    臨床フリーラジカル会議 2016

  113. Re-emerging reactive sulfur-containing compounds and their unique biological functions

    Tomoaki Ida, Tetsuro Matsunaga, Shigemoto Fujii, Tomohiro Sawa, Takaaki Akaike

    Folia Pharmacologica Japonica 2016

  114. Analysis Of Reactive Sulfur Species Production In Lungs Of COPD

    T. Numakura, H. Sugiura, T. Ida, K. Sato, R. Tanaka, K. Onodera, Y. Hashimoto, T. Hirano, M. Yamada, A. Koarai, S. Fujii, T. Akaike, M. Ichinose

    AMERICAN JOURNAL OF RESPIRATORY AND CRITICAL CARE MEDICINE 2016

  115. 大腸菌における蛋白質S-グアニル化標的タンパク質のプロテオーム解析

    津々木博康, 小野勝彦, 張田力, 井田智章, 居原秀, 赤池孝章, 澤智裕

    日本酸化ストレス学会学術集会プログラム・抄録集 2016

  116. 8-ニトロ-cGMPによるcGMP依存性プロテインキナーゼの活性化とエンドトキシンショック病態形成のメカニズム

    赤司壮一郎, AHMED Kahndaker Ahtesham, 澤智裕, 小野勝彦, 津々木博康, 井田智章, 藤井重元, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2016

  117. 8-ニトロ-cGMPとオートファジーによる細菌感染防御機構と硫化水素による制御

    藤井重元, 松永哲郎, 井田智章, 小野勝彦, 澤智裕, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2016

  118. ニトロ化環状ヌクレオチドによる感染防御機構と細菌由来硫化水素による制御

    藤井重元, 松永哲郎, 井田智章, 赤池孝章

    日本農芸化学会大会講演要旨集(Web) 2016

  119. ニトロ化環状ヌクレオチドによる細菌感染防御機構と硫化水素による制御

    藤井重元, 松永哲郎, 井田智章, 小野勝彦, 澤智裕, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2016

  120. 部位特異的タンパク質S-グアニル化を介したcGMP依存性プロテインキナーゼの持続的活性化

    赤司壮一郎, AHTESHAM Ahmed Khandaker, 澤智裕, 小野勝彦, 津々木博康, 井田智章, 藤井重元, 赤池孝章

    日本生化学会大会(Web) 2016

  121. Rp-8-ニトロcGMPSによるS-グアニル化を介したプロテインキナーゼG(PKG)の活性阻害

    小野勝彦, KHANDARKER Ahtesham Ahmed, 津々木博康, 張田力, 井田智章, 宮田敬士, 尾池雄一, 赤池孝章, 澤智裕

    日本酸化ストレス学会学術集会プログラム・抄録集 2016

  122. 親電子プローブを用いたMRM-MSによる生体試料中の活性イオウ分子の定量法の構築

    新開泰弘, 秋山雅博, 鵜木隆光, 井田智章, 赤池孝章, 熊谷嘉人

    衛生薬学・環境トキシコロジー講演要旨集 2016

  123. COPD患者肺におけるreactive persulfidesの産生に関する検討

    沼倉忠久, 杉浦久敏, 井田智章, 佐藤慶, 田中里江, 小野寺克洋, 平野泰三, 山田充啓, 小荒井晃, 藤井重元, 赤池孝章, 一ノ瀬正和

    日本酸化ストレス学会学術集会プログラム・抄録集 2016

  124. 喘息の気道におけるreactive persulfidesに関する検討

    小野寺克洋, 杉浦久敏, 沼倉忠久, 佐藤慶, 京極自彦, 井田智章, 赤池孝章, 一ノ瀬正和

    日本酸化ストレス学会学術集会プログラム・抄録集 2016

  125. タンパク質ポリサルファ化の分子メカニズムの解明

    井田 智章, 居原 秀, 魏 范研, 富澤 一仁, 長尾 翌手可, 鈴木 勉, 熊谷 嘉人, 澤 智裕, 笠松 真吾, 本橋 ほづみ, 赤池 孝章

    日本生化学会大会・日本分子生物学会年会合同大会講演要旨集 2015/12

  126. 新規活性イオウ分子過硫化水素(HSSH)の生体内生成の検出と生成機序の解明

    松永哲郎, 井田智章, 藤井重元, 渡邊泰男, 澤智裕, 本橋ほづみ, XIAN Ming, 赤池孝章

    日本生化学会大会(Web) 2015/12

  127. タンパク質S‐ポリチオール化を介する親電子シグナルの制御メカニズム

    赤司壮一郎, 笠松真吾, ジョン ミンギョン, 松永哲郎, 井田智章, 藤井重元, 澤智裕, 熊谷嘉人, 本橋ほづみ, 赤池孝章

    日本NO学会学術集会プログラム抄録集 2015/06/12

  128. HPLC‐蛍光検出法によるシステインパースルフィドの新しい定量システムの構築

    ジョン ミンギョン, 井田智章, 笠松真吾, 松永哲郎, 土屋幸弘, 渡邊泰男, 藤井重元, 赤池孝章

    日本NO学会学術集会プログラム抄録集 2015/06/12

  129. 加齢に伴うタンパク質中システインパーサルファイドの変動

    藪川啓司, 津々木博康, 井田智章, 笠松真吾, 赤池孝章, 居原秀

    日本NO学会学術集会プログラム抄録集 2015/06/12

  130. 活性イオウ分子のNO・活性酸素シグナル制御異常に起因する有機水銀の新規毒性発現機構の解析

    笠松真吾, 笠松真吾, 居原秀, 津々木博康, 津々木博康, 石崎健勝, 井田智章, 藤井重元, 澤智裕, 熊谷嘉人, 赤池孝章

    日本NO学会学術集会プログラム抄録集 2015/06/12

  131. タンパク質S‐ポリチオール化によるアルコールデヒドロゲナーゼ5の活性制御機構

    藤井重元, MORSHEDUL Alam Md, 井田智章, 松永哲郎, 笠松真吾, 居原秀, 赤池孝章, 本橋ほづみ

    日本NO学会学術集会プログラム抄録集 2015/06/12

  132. 活性イオウ分子種によるカルモデュリンキナーゼIV活性の阻害

    高田剛, 土屋幸弘, 井田智章, 澤智裕, 赤池孝章, 渡邊泰男

    日本NO学会学術集会プログラム抄録集 2015/06/12

  133. 活性イオウ分子産生酵素のNO応答性

    中村麻里江, 松本卓巳, 高田剛, 土屋幸弘, 井田智章, 澤智裕, 赤池孝章, 渡邊泰男

    日本NO学会学術集会プログラム抄録集 2015/06/12

  134. タンパク質S‐ポリチオール化による親電子シグナル制御

    赤司壮一郎, 笠松真吾, JUNG Minkyung, 松永哲郎, 井田智章, 藤井重元, 本橋ほづみ, 澤智裕, 熊谷嘉人, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2015/05/29

  135. アルコールデヒドロゲナーゼ5の活性発現におけるタンパク質S‐ポリチオール化の役割

    藤井重元, MD.MORSHEDUL Alam, 井田智章, 松永哲郎, 笠松真吾, 居原秀, 赤池孝章, 本橋ほづみ

    日本酸化ストレス学会学術集会プログラム・抄録集 2015/05/29

  136. 活性イオウ分子の親電子シグナル制御異常に起因する有機水銀の新規毒性発現機構の解明

    笠松真吾, 津々木博康, 居原秀, 井田智章, 藤井重元, 澤智裕, 赤池孝章

    日本衛生学雑誌 2015/03

  137. Helicobacter cinaedi感染による動脈硬化促進作用と感染疫学解析

    松永哲郎, 藤井重元, 井田智章, 河村好章, 赤池孝章

    日本細菌学雑誌 2015/02/25

  138. タンパク質ポリサルファ化を介したアルコールデヒドロゲナーゼ5の酵素活性制御機構

    笠松真吾, ALAM Md. Morshedul, 井田智章, 松永哲郎, 藤井重元, 居原秀, 赤池孝章, 本橋ほづみ

    日本生化学会大会(Web) 2015

  139. 有機水銀の神経毒性発現における8‐ニトロ‐cGMPの役割と活性イオウ分子による制御

    藤井重元, 笠松真吾, 居原秀, 津々木博康, 石崎健勝, 井田智章, 澤智裕, 熊谷嘉人, 赤池孝章

    日本生化学会大会(Web) 2015

  140. 活性イオウ分子種のメタボローム解析法の新たな展開

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    日本生化学会大会(Web) 2015

  141. タンパク質poly‐S‐グアニル化を介した親電子シグナルの可逆的制御

    赤司壮一郎, 笠松真吾, ジョン ミンギョン, 松永哲郎, 井田智章, 藤井重元, 澤智裕, 熊谷嘉人, 本橋ほづみ, 赤池孝章

    日本生化学会大会(Web) 2015

  142. 活性システインパースルフィドによる8‐ニトロ‐cGMP制御機構

    井田智章, 居原秀, 澤智裕, 津々木博康, 笠松真吾, 松永哲郎, 赤司壮一郎, 有本博一, 藤井重元, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2015

  143. シアノバクテリアSynechocystis sp.PCC6803の塩ストレス誘導性バイオフィルム形成に必要なヒスチジンキナーゼの同定とシグナル伝達機構

    永山達也, 久米井智裕, 牧野恒平, 井田智章, 赤池孝章, 鈴木石根, 七谷圭, 魚住信之

    日本農芸化学会大会講演要旨集(Web) 2015

  144. タンパク質S-グアニル化を介したオートファジー誘導と細菌感染防御における役割

    藤井重元, 松永哲郎, 井田智章, 澤智裕, 赤池孝章

    日本細菌学雑誌 2015

  145. 活性システインパースルフィドのメタボロミクスとプロテオミクス

    井田智章, 居原秀, 澤智裕, 土屋幸弘, 渡邊泰男, 藤井重元, 熊谷嘉人, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2015

  146. 心虚血再灌流障害におけるホモシステインの新規作用機序

    石井功, 中埜信太郎, 新村健, 玉城香代子, 菱木貴子, 赤星軌征, 井田智章, 中西豪, 鎌田祥太郎, 熊谷嘉人, 赤池孝章, 福田恵一, 佐野元昭, 末松誠

    日本生化学会大会(Web) 2015

  147. 活性システインパースルフィドのメタボロームおよびプロテオーム解析

    井田智章, 居原秀, 澤智裕, 土屋幸弘, 渡邊泰男, 藤井重元, 熊谷嘉人, 本橋ほづみ, 赤池孝章

    日本NO学会学術集会プログラム抄録集 2015

  148. 8-ニトロ-cGMPと活性システインパースルフィドを介した酸化ストレス制御機構とその生理機能の解明

    井田智章

    日本生体防御学会学術総会講演抄録集 2015

  149. 生体防御における転写因子Nrf2とグルタチオン依存性ホルムアルデヒド脱水素酵素Adh3による協調作用

    後藤 まき, 北村 大志, 井田 智章, 澤 智裕, 赤池 孝章, 長谷場 健, 秋元 敏雄, 山本 照子, 野, 山本 雅之, 本橋 ほづみ

    日本生化学会大会プログラム・講演要旨集 2014/10

  150. 細菌における新規シグナル伝達物質8‐ニトロ‐cGMPの生成とその機能

    松永哲郎, 藤井重元, 井田智章, ジョン ミンキョン, 赤司壮一郎, 津々木博康, 居原秀, 澤智裕, 赤池孝章

    日本生化学会大会(Web) 2014/10

  151. 8‐ニトロ‐cGMPを介した感染防御機構と細菌が産生する硫化水素による抑制

    松永哲郎, 赤司壮一郎, ジョン ミンキョン, 伊藤千秋, 井田智章, 藤井重元, 澤智裕, 有本博一, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2014/08/29

  152. 新興感染症菌Helicobacter cinaedi感染による動脈硬化促進作用についての検討

    松永哲郎, 藤井重元, 岡本竜哉, 井田智章, 澤智裕, 河村好章, 赤池孝章

    東北公衆衛生学会講演集 2014/07

  153. 8‐ニトロ‐cGMPによる感染防御機構と細菌由来硫化水素による抑制

    松永哲郎, 赤司壮一郎, JUNG Minkyung, 伊藤千秋, 井田智章, 藤井重元, 澤智裕, 有本博一, 赤池孝章

    日本NO学会学術集会プログラム抄録集 2014/05/16

  154. カルモデュリンキナーゼIVのシステイン過硫化修飾による活性制御

    高田剛, 土屋幸弘, 井田智章, 澤智裕, 赤池孝章, 渡邊泰男

    日本NO学会学術集会プログラム抄録集 2014/05/16

  155. 新興感染症菌Helicobacter cinaedi感染による動脈硬化の促進作用

    松永哲郎, 岡本竜哉, 藤井重元, 井田智章, 澤智裕, 河村好章, 赤池孝章

    日本細菌学雑誌 2014/02/25

  156. H-RasのS-グアニル化を介したオートファジーのレドックス制御

    井上博文, 藤井重元, 西田基宏, 井田智章, 澤智裕, 赤池孝章

    日本NO学会学術集会プログラム抄録集 2014

  157. 細菌の新しいシグナル伝達物質8-nitro-cGMPの同定と機能解析

    藤井重元, 松永哲郎, 井田智章, JUNG Minkyung, 赤司壮一郎, 津々木博康, 居原秀, 澤智裕, 澤智裕, 赤池孝章

    日本NO学会学術集会プログラム抄録集 2014

  158. 8-ニトロ-cGMPによる細菌感染防御機構と硫化水素による制御

    JUNG Minkyung, 藤井重元, 松永哲郎, 井田智章, 澤智裕, 赤池孝章

    日本細菌学雑誌 2014

  159. 8-ニトロ-cGMPによる新規タンパク質翻訳後修飾poly-S-グアニル化の特異的検出

    赤司壮一郎, MINKYUNG Jung, 松永哲郎, 井田智章, 藤井重元, 澤智裕, 熊谷嘉人, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2014

  160. プロテインキナーゼGの活性化ドメインへのS-グアニル化とその敗血症における遷延性血圧低下への関与

    澤智裕, AHTESHAM Ahmed, 藤井重元, 井田智章, 赤池孝章

    日本細菌学雑誌 2014

  161. 新規レドックス調節因子の制御機構:ethylmalonic encephalopathy1による活性イオウ分子種の制御

    JUNG Minkyung, 松永哲郎, 北村大志, 井田智章, 藤井重元, 澤智裕, 本橋ほづみ, 赤池孝章

    日本NO学会学術集会プログラム抄録集 2014

  162. ラン藻の塩誘導性バイオフィルム形成に関与する二成分系c-di-GMP合成酵素の同定

    牧野恒平, 七谷圭, 井田智章, 澤智裕, 澤智裕, 佐伯千香, 鈴木石根, 兵藤守, 早川芳弘, 赤池孝章, 魚住信之

    日本分子生物学会年会プログラム・要旨集(Web) 2014

  163. 8-ニトロ-cGMPによる細菌感染防御機構と硫化水素による制御

    JUNG Minkyung, 松永哲郎, 藤井重元, 井田智章, 澤智裕, 赤池孝章

    日本生体防御学会学術総会講演抄録集 2014

  164. 活性システインパーサルファイドによる酸化ストレス制御

    井田智章, 澤智裕, 居原秀, 土屋幸弘, 渡邊泰男, 熊谷嘉人, 藤井重元, 松永哲郎, FUKUTO Jon, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2014

  165. 新規レドックス調節因子の制御機構:Ethylmalonic encephalopathy1(ETHE1)による活性イオウ分子種の制御機構

    JUNG Minkyung, 松永哲郎, 北村大志, 井田智章, 藤井重元, 澤智裕, 本橋ほづみ, 赤池孝章

    日本酸化ストレス学会学術集会プログラム・抄録集 2014

  166. 活性システインパーサルファイドとS-ポリチオレイションが酸化ストレスとレドックスシグナルを制御する

    井田智章, 澤智裕, 居原秀, 土屋幸弘, 松永哲郎, 藤井重元, 熊谷嘉人, 渡邊泰男, FUKUTO M Jon, 赤池孝章

    日本NO学会学術集会プログラム抄録集 2014

  167. 8-ニトロ-cGMPによる宿主と細菌のGAPDH制御を介する解糖系リプログラミング

    赤司壮一郎, JUNG Minkyung, 松永哲郎, 井田智章, 藤井重元, 澤智裕, 居原秀, 川端重忠, 熊谷嘉人, 赤池孝章

    日本細菌学雑誌 2014

  168. Synaptosomal-associated protein25(SNAP25)のS-グアニル化

    國枝恒兵, 井田智章, 澤智裕, 赤池孝章, 板倉誠, 高橋正身, 居原秀

    生化学 2009

  169. アストロサイトにおける未熟温州みかんによる誘導型一酸化窒素合成酵素発現抑制効果

    居原秀, 井田智章, 山本英之, 森下将次, 小崎俊司

    日本農芸化学会大会講演要旨集 2009

  170. N-ethylmaleimide-sensitive factor(NSF)のS-グアニル化

    深瀬真由子, 井田智章, 國枝恒兵, 板倉誠, 高橋正身, 澤智裕, 赤池孝章, 居原秀

    生化学 2009

  171. 未熟温州みかんによる転写因子NF-κBシグナル伝達経路に対する影響

    居原秀, 井田智章, 山本英之, 山本英之, 友松秀寧, 森下将次, 森下正春, 小崎俊司

    日本農芸化学会関西支部講演会講演要旨集 2008

  172. 新規ニトロ化セカンドメッセンジャー,8-ニトログアノシン3’,5’-環状1リン酸による開口放出の調節

    居原秀, 津々木博康, 井田智章, 國枝恒兵, 笹川展幸, 板倉誠, 澤智裕, 赤池孝章

    生化学 2008

  173. アストロサイトにおける新規ニトロ化セカンドメッセンジャー8-nitroguanosine3’,5’-cyclic monophosphate(8-nitro cGMP)の産生

    井田智章, 澤智裕, 赤池孝章, 居原秀

    生化学 2008

  174. Nitric oxide mediates cytokine-induced enhancement of Ca2+-dependent Glu release from astrocytes

    Tomoaki Ida, Ybichi Nakamura, Shunji Kozaki, Hideshi Ihara

    NEUROSCIENCE RESEARCH 2007

  175. 未熟温州みかんの神経保護作用

    山本英之, 居原秀, 井田智章, 岡田利也, 小崎俊司

    日本農芸化学会大会講演要旨集 2007

  176. Nitric oxide mediates cytokine-induced enhancement of calcium-dependent glutamate release from astroeytes

    Tomoaki Ida, Shigeru Tsunoda, Masayuki Hara, Shunji Kozaki, Hideshi Ihara

    NITRIC OXIDE-BIOLOGY AND CHEMISTRY 2006/06

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Research Projects 13

  1. Discovery of a novel persulfide synthase and analysis of its physiological function.

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research

    Category: Grant-in-Aid for Scientific Research (C)

    Institution: Osaka Metropolitan University

    2023/04/01 - 2026/03/31

  2. 超硫黄分子の代謝制御メカニズムの解明

    守田 匡伸, 松永 哲郎, 井田 智章

    Offer Organization: 日本学術振興会

    System: 科学研究費助成事業

    Category: 基盤研究(C)

    Institution: 東北大学

    2023/04/01 - 2026/03/31

  3. Reaction mechanism of a novel cysteine persulfide synthase and its function

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)

    Category: Grant-in-Aid for Scientific Research (C)

    Institution: Tohoku University

    2020/04/01 - 2023/03/31

  4. Novel reactive persulfide-producing system in bacteria and its involvement in bacterial pathogenicity Competitive

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)

    Category: Grant-in-Aid for Scientific Research (C)

    Institution: Tohoku University

    2018/04 - 2020/03

  5. Production of polysulfidated protein and regulation mechanism of its structure/functions Competitive

    Ida Tomoaki

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)

    Category: Grant-in-Aid for Scientific Research (C)

    Institution: Tohoku University

    2017/04 - 2019/03

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    A specific and highly sensitive polysulfide protein analysis system, which is essential for elucidating the protein polysulfide level, biosynthesis, structure, and regulation mechanism, has not been established. In this research project, we showed the unique chemical reactivity of reactive sulfur species. Furthermore, an analysis system using a mass spectrometer was developed to detect polysulfided proteins with high specificity. Using this analysis system, the dynamics, structure and function of polysulfated proteins were clarified.

  6. Polysulfur metabolome and regulation of anti-oxidative stress responses Competitive

    Akaike Takaaki

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)

    Category: Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)

    Institution: Tohoku University

    2014 - 2018

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    Polysulfides is reactive persulfide species which have extra sulfur atoms in cysteine thiol and cellular proteins contain polysulfides abundantly (protein polysulfuration). In this study, we investigated the translation-coupled mechanism of protein polysulfidation mediated by cysteinyl-tRNA synthetase (CARS) and its biological functions. CARSs from various biological species including bacteria and mammals are found to have cysteine persulfide-producing activity and to be critically involved in protein polysulfuration. Protein polysulfuration is suggested to play important roles in the regulation of cellular function such as mitochondrial morphogenesis.

  7. Study of the mechanism of biosynthesis of polysulfurated proteins coupled with translation Competitive

    AKAIKE Takaaki

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research Grant-in-Aid for Challenging Exploratory Research

    Category: Grant-in-Aid for Challenging Exploratory Research

    Institution: Tohoku University

    2016/04 - 2017/03

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    Polysulfur is reactive persulfide species which have extra sulfur atoms in cysteine thiol and cellular proteins contain polysulfur abundantly (protein polysulfuration). In this study, we investigated the translation-coupled mechanism of protein polysulfuration mediated by cysteinyl-tRNA synthetase (CARS) and its biological functions. CARSs from various biological species including bacteria and mammals are found to have cysteine persulfide-producing activity and to be critically involved in protein polysulfuration. Protein polysulfuration is suggested to play important roles in the regulation of cellular function such as mitochondrial morphogenesis.

  8. Novel oxidative stress response mechanism by reactive sulfur species and 8-nitro-cGMP Competitive

    Tomoaki Ida

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research Grant-in-Aid for Young Scientists (B)

    Category: Grant-in-Aid for Young Scientists (B)

    Institution: Tohoku University

    2015/04 - 2017/03

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    We investigated novel oxidative stress response mechanism by 8-nitro-cGMP and reactive sulfur species such as cysteine persulfide. We developed a quantitative method, i.e, sulfur omics analysis, for determination of the level of cysteine persulfides/polysulfides and protein polysulfidation using liquid chromatography-tandem mass spectrometry (LC-MS/MS) and iodoacetamide-based derivative. Using this technique, it was found that reactive sulfur species play an important role in oxidative stress response, via crosstalk with 8-nitro-cGMP. We also found a new cysteine persulfide producing system in cells, which is originally known as a master enzyme for protein translation, and elucidated its pivotal roles in protein polysulfidation and protein function.

  9. Novel signaling pathway of bacterial stress responses and host defense via autophagy Competitive

    AKAIKE Takaaki, MATSUNAGA Tetsuro, IDA Tomoaki

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research Grant-in-Aid for Challenging Exploratory Research

    Category: Grant-in-Aid for Challenging Exploratory Research

    Institution: Tohoku University

    2014/04 - 2016/03

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    To clarify the molecular mechanism of pathogenesis of bacterial infection, we investigated the functions of 8-nitro-cGMP which is a signaling molecule both in bacteria and host cells. Protein S-guanylation induced by 8-nitro-cGMP was involved in stress responses in bacteria, and also play an important role in antibacterial host defense via autophagy. Hydrogen sulfide and reactive sulfur species produced by bacteria were suggested to regulate signaling function of 8-nitro-cGMP and to be involved in bacterial growth in infected cells.

  10. Mechanism of intracellular formation of cysteine polysulfide and reactive oxygen species signaling Competitive

    AKAIKE Takaaki

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (A)

    Category: Grant-in-Aid for Scientific Research (A)

    Institution: Tohoku University

    2013/04 - 2015/05

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    We investigated physiological roles of reactive sulfur species having extra sulfur atoms in cysteine thiol moiety, such as cysteine polysulfides. Quantitation of these species indicated that high levels of glutathione persulfide (over 100 microM) and other cysteine persulfides were produced in cells and its roles in regulation of reactive oxygen species signaling and protein functions were revealed. We also found a new cysteine persulfide-producing system in cells, which is originally known as a master enzyme for protein translation, and elucidated its pivotal roles in protein polysulfidation and regulation of mitochondrial function.

  11. Regulatory mechanisms of protein S-polythiolation Competitive

    Sawa Tomohiro, IDA Tomoaki

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research Grant-in-Aid for Challenging Exploratory Research

    Category: Grant-in-Aid for Challenging Exploratory Research

    Institution: Kumamoto University

    2014/04 - 2015/03

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    Protein S-polythiolation is a post-translational modification that introduce additional sulfur atoms on cysteine residues in proteins. We developed specific method that enables biotin-labeling on S-polythiolated cysteines by using methylsulfonyl benzothiazole and cyanide biotin. We successfully identified endogenous S-polythiolated proteins including cytoskeleton proteins. The method we developed may help further understanding of signal transduction mediated via protein S-polythiolation.

  12. Analysis of intarocular antioxidant and development of intraocular irrigating solution Competitive

    Nakazawa Toru, Kunikata HIROSHI, Ida TOMOAKI, Akaike TAKAAKI

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research Grant-in-Aid for Challenging Exploratory Research

    Category: Grant-in-Aid for Challenging Exploratory Research

    Institution: Tohoku University

    2014/04 - 2015/03

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    We found that there were reactive persulfides and polysulfides in blood, aqueous humor and vitreous in diabetic eyes as well as controls. Furthermore, the concentration of some persulfides was different between diabetic eyes and controls, and there were some correlations between the persulfides in aqueous humor and vitreous.

  13. Clarification of the endogenous formation of the novel cyclic nucleotide 8-SH-cGMP and its signaling function Competitive

    IDA Tomoaki

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research Grant-in-Aid for Young Scientists (B)

    Category: Grant-in-Aid for Young Scientists (B)

    Institution: Tohoku University

    2013/04 - 2014/03

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    The cyclic nucleotide 8-SH-cGMP is produced by the metabolism of 8-nitro-cGMP, which serves as a secondary messenger for NO and reactive oxygen species signaling. However, the mechanisms controlling the formation and levels of intracellular 8-SH-cGMP have not yet been identified. In this study, the principal investigator precisely quantified the formation of 8-SH-GMP via a mass spectrometry-based metabolomic method. The results revealed that 8-SH-cGMP is produced from 8-nitro-cGMP via sulfhydration by reactive sulfur species generated from the cystathione beta-synthase and cystathionine gamma-lyase systems. Moreover, the formation of S-S-guanylation (cGMP adduction to the thiol group of the protein via disulfide linkage) was specifically identified using proteome analysis of S-polythiolation.

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