Updated on 2025/03/01

写真a

 
TSUMURA-SHISHIDO Naomi
 
Organization
School of Medicine General Education Life Science
External link

Research Interests

  • Reactive Oxygen Species

  • 活性酸素種

  • 錯体

  • Chelates

  • Alzheimer's Disease

  • redox

Research Areas

  • Life Science / Medical biochemistry

Education

  • Hokkaido University   Faculty of Pharmaceutical Science

    - 1992.3

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    Country: Japan

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  • Hokkaido University   Faculty of Pharmaceutical Science   Department of Physical Chemistry

    - 1992

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Professional Memberships

Papers

  • Specific reaction of Met 35 in amyloid beta peptide with hypochlorous acid Reviewed

    Masao Nakamura, Naomi Shishido, Akihiko Nunomura, Mark A. Smith, George Perry, Hiroaki Akutsu, Takaaki Hayashi

    FREE RADICAL RESEARCH   44 ( 7 )   734 - 741   2010.7

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:INFORMA HEALTHCARE  

    The reaction of the amyloid beta peptide (A beta) with hypochlorous acid and hydroxyl radicals was analysed by spectrophotometry and mass spectrometry. N-acetylmethionine, A beta 25-35 and A beta 1-42 reacted rapidly with hypochlorous acid. The relative reaction rates of N-acetylmethionine and A beta with hypochlorous acid was in the order N-acetylmethionine > A beta 25-35 > A beta 1-42. While the reaction of A beta 25-35 in the presence of a slight excess of hypochlorous acid resulted in complete conversion of Met35 to Met35 sulphoxide, A beta 1-42 required more than a 4-fold excess of hypochlorous acid for complete conversion of Met35. Identical products were obtained when A beta 25-35 and A beta 1-42 were treated with a hypochlorous acid generating system. Conversion of Met35 to Met35 sulphoxide in A beta abolished the aggregation of A beta 25-35. Reaction of A beta with hydroxyl radicals resulted in limited conversion of Met35 to Met35 sulphoxide. The specific reaction of Met35 in A beta with hypochlorous acid to form Met35 sulphoxide has been analysed.

    DOI: 10.3109/10715761003745954

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  • Specific reaction of Met 35 in amyloid beta peptide with hypochlorous acid. Reviewed

    Nakamura M., Shishido N., Nunomura A., Smith MA, Perry G., Akutsu H., Hayashi T.

    Free Radic. Res.   44 ( (7) )   734 - 741   2010.7

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  • Three histidine residues of amyloid beta peptide control the redox activity of transition metals.

    Nakamura M., Shishido N., Nunomura A., Smith MA, Perry G., Hayashi T.

    “Metal Metabolism: Transport, Development and Neurodegeneration (2008-London)”   12 - 12   2008.4

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  • Lipid peroxidation and 4-hydroxy-2-nonenal formation by copper ion bound to amyloid-beta peptide Reviewed

    Takaaki Hayashi, Naomi Shishido, Kenji Nakayama, Akihiko Nunomura, Mark A. Smith, George Perry, Masao Nakamura

    FREE RADICAL BIOLOGY AND MEDICINE   43 ( 11 )   1552 - 1559   2007.12

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:ELSEVIER SCIENCE INC  

    The lipid peroxidation product 4-hydroxy-2-nonenal (HNE) is proposed to be a toxic factor in the pathogenesis of Alzheimer disease. The primary products of lipid peroxidation are phospholipid hydroperoxides, and degraded reactive aldehydes, such as HNE, are considered secondary peroxidation products. In this study, we investigated the role of amyloid-beta peptide (A beta) in the formation of phospholipid hydroperoxides and HNE by copper ion bound to A beta. The A beta(1-42)-CU2+ (1:1 molar ratio) complex showed an activity to form phospholipid hydroperoxides from a phospholipid, 1-palmitoyl-2-linoleoyl phosphatidylcholine, through Cu2+ reduction in the presence of ascorbic acid. The phospholipid hydroperoxides were considered to be a racemic mixture of 9-hydroperoxide and 13-hydroperoxide of the linoleoyl residue. When Cu2+ was bound to 2 molar equivalents of A beta(1-42) (2 A beta(1-42)-Cu2+), lipid peroxidation was inhibited. HNE was generated from one of the phospholipid hydroperoxides, 1-palmitoyl-2-(13-hydroperoxy-cis-9, trans-11-octadecadienoyl) phosphatidylcholine (PLPC-OOH), by free Cu2+ in the presence of ascorbic acid through Cu2+ reduction and degradation of PLPC-OOH. HNE generation was markedly inhibited by equimolar concentrations of A beta(1-40) (92%) and A beta(1-42) (92%). However, A beta(1-42) binding 2 or 3 molar equivalents of Cu2+ (A beta(1-42)-2 Cu2+, A beta(1-42)-3Cu(2+)) acted as a pro-oxidant to form HNE from PLPC-OOH. These findings suggest that, at moderate concentrations of copper, A beta acts primarily as an antioxidant to prevent Cu2+-catalyzed oxidation of biomolecules, but that, in the presence of excess copper, pro-oxidant complexes of A beta with Cu2+ are formed. (C) 2007 Elsevier Inc. All rights reserved.

    DOI: 10.1016/j.freeradbiomed.2007.08.013

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  • Three histidine residues of amyloid-beta peptide control the redox activity of copper and iron

    M. Nakamura, N. Shishido, Akihiko Nunomura, Mark A. Smith, George Perry, Y. Hayashi, K. Nakayama, T. Hayashi

    BIOCHEMISTRY   46 ( 44 )   12737 - 12743   2007.11

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER CHEMICAL SOC  

    Zinc, iron and copper are concentrated in senile plaques of Alzheimer disease. Copper and iron catalyze the Fenton-Haber-Weiss reaction, which likely contributes to oxidative stress in neuronal cells. In this study, we found that ascorbate oxidase activity and the intensity of ascorbate radicals measured using ESR spectroscopy, generated by free Cu(II), was decreased in the presence of amyloid-beta (A beta), the major component of senile plaques. Specifically, the ascorbate oxidase activity was strongly inhibited (85% decrease) in the presence of A beta 1-16 or A beta 1-42, whereas it was only slightly inhibited in the presence of A beta 1-12 or A beta 25-35 (< 20% inhibition). Ascorbate-dependent hydroxyl radical generation by free Cu(II) decreased in the presence of A beta in the identical order of A beta 1 -42, A beta 1-16 > A beta 1 - 12 and was abolished in the presence of 2-fold molar excess glycylhystidyllysine (GHK). Ascorbate oxidase activity and ascorbate-dependent hydroxyl radical generation by free Fe(III) were inhibited by A beta 1-42, A beta 1 - 16, and A beta 1 -12. Although Cu(II)-A beta shows a significant SOD-like activity, the rate constant for the reaction of superoxide with Cu(II)-A beta was much slower than that with SOD. Overall, our results suggest that His6, His13, and His14 residues of A beta 1-42 control the redox activity of transition metals present in senile plaques.

    DOI: 10.1021/bi701079z

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  • Valence isomerization of hinokitiol under UV-irradiation.

    Seki K., Maekawa M., Kasahara S., Nakamura S., Okabe T., Yamamoto T., Inamori Y., Shishido N., Nakamura M.

    ESP 2007 (12th Congress of the European Society for Photobiology)   139 - 139   2007.4

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  • Effects of MCI-186 upon neutrophil-derived active oxygens.

    Sumitomo K., Shishido N., Aizawa H., Hasebe N., Kikuchi K., Nakamura M.

    Redox Report   12 ( (4) )   189 - 194   2007.4

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  • Effects of amyloid beta peptides upon the redox activity of copper.

    Shishido N., Hayashi Y., Hayashi T., Nakayama K., Nakamura M.

    (20th IUBMB International Congress of Biochemistry)   2006.4

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  • Reactions of 1-methyl-2-mercaptoimidazole with hypochlorous acid and superoxide Reviewed

    M Nakamura, N Shishido, H Akutsu

    JAPANESE JOURNAL OF INFECTIOUS DISEASES   57 ( 5 )   S34 - S35   2004.10

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:NATL INST INFECTIOUS DISEASES  

    Reactions of thioureylene antithyroid drugs (1-methyl-2-mercaptoimidazole and carbimazole) with hypochlorous acid (HOCl) and superoxide were followed optically and products were analyzed by,mass spectrometry. 1-Methyl-2-mercaptoimidazole (MMI) and carbimazole reacted rapidly with HOCl with a rate constant of 1 X 10(7) and 7 X 10(6) M(-1)s(-1), respectively. The characteristic spectrum assigned to MMI disulfide appeared immediately after addition of HOCl, followed by a slow conversion to a final spectrum. The conversion was dependent upon the ratio of HOCl to MMI and both antithyroid drugs uptake 3 moles HOCl for complete conversion. A similar sequence of spectral changes was also observed when the HOCl was replaced by myeloperoxidase (MPO)/H2O2/Cl- system. The final oxidation product of MMI and carbimazole with HOCl and superoxide was 1-methylimidazole.

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  • Porphyrin-induced photooxidation of conjugated bilirubin

    N Shishido, K Nakayama, M Nakamura

    FREE RADICAL RESEARCH   37 ( 10 )   1061 - 1067   2003.9

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:TAYLOR & FRANCIS LTD  

    Visible light irradiation of 18 muM bilirubin ditaurate (BR-DT) at pH 7.0 for 30 min showed a 10% decrease in absorbance at 445 nm. When the reaction was carried out in the presence of a trace amount of uroporphyrin (UP), the spectrum of BR-DT disappeared without a concomitant formation of biliverdin. Photooxidation products were confirmed to be dipyrrole-containing compounds. Photobleaching of BR-DT was accelerated by the increasing concentration of UP and was inhibited, when UP was replaced by Cu2+ UP. Formation of 2,2,6,6-tetramethylpiperidine N-oxyl through the irradiation of UP was diminished by sodium azide, a potent scavenger of singlet oxygen. The efficiency of singlet oxygen formation through visible light irradiation was in the order UP, coproporphyrin > Cu2+ UP. Both bilirubin and BR-DT bound to human serum albumin (HSA) were photooxidized effectively in the presence of UP. The results indicate that irradiation of UP produces singlet oxygen with high efficiency which then rapidly oxidizes free and conjugated bilirubin.

    DOI: 10.1080/10715760310001600381

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  • LECラット尿中銅の状態 Reviewed

    宍戸直美, 中山憲司, 中村正雄

    生化学   74 ( 8 )   829   2002.8

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  • Inhibitory effects of bucillamine on increased blood-retinal barrier permeability in streptozotocin-induced diabetic rats Reviewed

    T Hikichi, F Mori, M Nakamura, N Shishido, M Sasaki, Y Horikawa, A Yoshida

    CURRENT EYE RESEARCH   25 ( 1 )   1 - 7   2002.7

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:SWETS ZEITLINGER PUBLISHERS  

    Purpose. To investigate the effect of bucillamine for prevention of increasing blood-retinal barrier (BRB) permeability in streptozotocin (STZ)-induced diabetic rats.
    Methods. The groups included control and STZ-induced diabetic rats treated with or without bucillamine. Six months after intervention, the concentrations of reduced and oxidative glutathione (GSH and GSSG) in the retina were measured biochemically. In addition, vitreous fluorescein, which leaks from the vessels after intravenous injection of fluorescein sodium, was measured to evaluate BRB permeability. To evaluate the scavenging ability against the reactive oxygen species (ROS) in vitro, the second-order rate constant for the reaction of bucillamine with ROS was estimated from the kinetics based on the rate constant for the reaction of ROS.
    Results. The BRB permeability was significantly higher (p = 0.01) in diabetic rats not treated with bucillamine, and bucillamine inhibited the BRB permeability. The GSH concentration and the GSH/GSSG ratio in the retinas decreased in diabetic rats not treated with bucillamine; bucillamine inhibited the decrease of the GSH concentrations. The ROS scavenging activity of bucillamine was similar with that of GSH.
    Conclusions. In diabetic retinas, oxidative stress might increase, which may be one of the causes of BRB breakdown. The antioxidant effects of bucillamine might take part in inhibition of increased permeability of the BRB in diabetes.

    DOI: 10.1076/ceyr.25.1.1.9962

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  • Inhibitory effect of bucillamine on laser-induced choroidal neovascularization in rats Reviewed

    T Hikichi, F Mori, M Sasaki, A Takamiya, M Nakamura, N Shishido, M Takeda, Y Horikawa, H Matsuoka, A Yoshida

    CURRENT EYE RESEARCH   24 ( 1 )   1 - 5   2002

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:SWETS ZEITLINGER PUBLISHERS  

    Purpose. We investigated the inhibitory effects of bucillamine on formation of laser-induced choroidal neovascularization (CNV) in a rat model.
    Methods. Bucillamine administration (approximately 150 mg/kg/day) was started 1 week before photocoagulation and continued to the end of the study. Control groups received drinking water. Two weeks after photocoagulation, choroidal neovascularization development was evaluated using simultaneous fluorescein and indocyanine green angiography, and the maximal thickness of the lesions was measured histologically.
    Results. The incidence of CNV formation was 99.5 +/- 0.2% [mean +/- standard deviation (SD)] in control rats and 64.3 +/- 15.1% with bucillamine (P < 0.01). Histological study showed that the thickness of the CNV lesions was 23.4 ± 6.5 μm (mean ± SD) in the bucillamine-treated rats, which was significantly decreased compared to that in controls (60.8 ± 9.2 μm) (P < 0.01).
    Conclusions. Our results suggest that bucillamine may inhibit the development of laser-induced CNV in rats.

    DOI: 10.1076/ceyr.24.1.1.5434

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  • Cu-metallothioneins (Cu(I)(8)-MTs) in LEC rat livers 13 weeks after birth still act as antioxidants

    N Shishido, K Nakayama, A Takazawa, T Ohyama, M Nakamura

    ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS   387 ( 2 )   216 - 222   2001.3

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:ACADEMIC PRESS INC  

    Redox properties of metallothioneins (MTs) and Cu in the cytosol from Long-Evans Cinnamon (LEC) rat livers 13 weeks after birth were investigated. MTs from LEC rat livers contain 8 g atoms of Cu and 1 g atom of Zn per mole of protein (Cu(I)(8)-MTs). Titration of Cu(I)(8)-MTs with CuCl2 indicates that Cu(I)(8)-MTs were able to reduce further 2-g atoms of cupric ions per mole MTs as bound form. Hg2+-induced hydroxyl radical generation from Cu(I)(8)-MTs was demonstrated by ESR using the spin trap, 5,5-dimethyl-1-pyrroline N-oxide (DMPO). The intensity of DMPO-OH signal from Cu-loaded MTs was increased with the increasing number of Cu in MTs. The used cytosol fraction contained 1.37 mM total Cu and 5 mM DTNB titrable-SH groups has a potential to reduce 2 mM CuCl2. No ESR signal due to Cu2+ was also detected with LEC rat liver cytosol, whereas strong Cu2+ signal appeared by the addition of HgCl2. The rate constants for the reaction of Cu(I)(8)-MTs with superoxide and hydroxyl radicals were estimated to be 2 x 10(6) and greater than or equal to 10(12) M(-1)s(-1), respectively, from competition kinetics. Cu2+-catalyzed oxidation of DNA was strongly inhibited both in the presence of Cu-unsaturated MTs and GSH. The results suggest that Cu(I)(8)-MTs from LEC rat livers just before hepatitis still act as antioxidants. (C) 2001 Academic Press.

    DOI: 10.1006/abbi.2000.2233

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  • Dissociation of DNA double strand by hypohalous acids

    N Shishido, S Nakamura, M Nakamura

    REDOX REPORT   5 ( 4 )   243 - 247   2000

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:W S MANEY & SONS LTD  

    Calf thymus DNA was treated with authentic HOCl, and hypohalous acid-generating systems. This caused a decrease in fluorescence of ethidium-DNA complexes when ethidium bromide was subsequently added to the DNA. The fluorescence continued to decrease up to 30 min after adding HOCl. Loss in fluorescence was proportional to the concentration of HOCl and was complete when a 3-fold excess of HOCl was added to the DNA. No significant decrease in the fluorescence was observed when the chlorination was carried out in the presence of a concentration of monochlorodimedone (MCD) equivalent to that of HOCl. MCD is known to react stoichiometrically with HOCl. The decrease in fluorescence was completely inhibited by H2O2, ascorbate and glutathione (GSH). We have estimated the rate constant for the reaction of HOCl with H2O2 to be 1-2 x 10(5) M(-1)s(-1). When compared with authentic HOCl, HOCl-generating systems (Cl- + H2O2 + MPO or chloroperoxidase) were found to be inefficient in damaging DNA. This result most likely arises because the rate constant for reaction of HOCl with H2O2 is about 1000-fold faster than that for the reaction with DNA. HOBr and HOI generating systems also had a limited ability to damage DNA. We conclude that good chlorine accepters and antioxidants protect DNA from hypohalous acid-induced oxidative damage.

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  • Metal-induced hydroxyl radical generation by Cu+-metallothioneins from LEC rat liver Reviewed

    M Nakamura, K Nakayama, N Shishido, K Yumino, T Ohyama

    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS   231 ( 3 )   549 - 552   1997.2

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS  

    Reactions of LEC (Long-Evans rats with a cinnamon-like coat color) rat liver Cu(I)-metallothioneins (MTs) with HgCl2 or K3Fe(CN)(6) were investigated by ESR spectroscopy and generation of hydroxyl radicals was demonstrated using the ESR spin trap, 5,5-dimethyl-1-pyrroline N-oxide (DMPO), When Cu(I)-MTs were incubated with more than one equivalent mole HgCl2 or K3Fe(CN)(6) to Cu+ bound to MTs, strong signals due to Cu2+ appeared, ESR spectra, which were a combination of the DMPO-OH adduct signal and a six-line signal, were observed in the reaction of Cu(I)-MTs with HgCl2, whereas no oxygen radical signal was seen with K3Fe(CN)(6). The DMPO-OH signal intensity was greater in the presence of SOD while the signal disappeared in the presence of catalase, The results suggest that addition of HgCl2 causes the liberation of cuprous ions from MTs followed by a reaction with oxygen, leading to hydroxyl radical formation through a Fenton-type Haber-Weiss reaction. (C) 1997 Academic Press.

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Books

  • 生命と環境

    林 要喜知, 細谷 夏実, 矢澤 洋一( Role: Joint author水質汚濁)

    三共出版  2011.5 

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MISC

  • 細胞接着分子BT‐IgSFはHSP90bを介して細胞移動を促進する。

    武藤理, 宍戸直美, 上田翼, 阿久津弘明, 林要喜知

    日本生化学会大会(Web)   89th   ROMBUNNO.1P‐391 (WEB ONLY)   2016

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  • アミロイドベータペプチド(Aβ)は活性酸素(ROS)生成による酸化ストレスを抑制し化学修飾される

    中村正雄, 宍戸直美, 布村明彦, SMITH MA, PERRY G, 林要喜知, 林隆章

    日本動物学会大会予稿集   82nd   60   2011.8

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  • アミロイドベータペプチド(Aβ)は遷移金属による酸化ストレスを抑制する

    中村正雄, 宍戸直美, 布村明彦, SMITH Mark A, PERRY George, 中山憲司, 林隆章

    Biomed Res Trace Elem   22 ( 2 )   82 - 82   2011.6

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  • アミロイドベータペプチドと次亜塩素酸およびタウリンクロラミンとの反応

    宍戸 直美, 阿久津 弘明, 林 要喜知, 林 隆章, 布村 明彦, スミス・マーク A., ペリー・ジョージ, 中村 正雄

    日本生化学会大会プログラム・講演要旨集   82回   4P - 551   2009.9

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  • Determining the status of copper in the urine of Long-Evans Cinnamon rats and patients with Wilson's disease

    9 ( 1 )   11 - 23   2008

  • Amyloid peptides including His13 and His 14 inhibit redox activities of copper

    Yokichi Hayashi, Naomi Shishido, Takaaki Hayashi, Kenji Nakayama, Masao Nakamura

    ZOOLOGICAL SCIENCE   23 ( 12 )   1167 - 1167   2006.12

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    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:ZOOLOGICAL SOC JAPAN  

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  • One- and two-electron oxidations of antioxidants by peroxidase systems.

    M. Nakamura, N. Shishido

    Current Topics in Biochemistry   19 - 30   2006.4

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  • One- and two-electron oxidations of antioxidants by peroxidase systems.

    M. Nakamura, N. Shishido

    Current Topics in Biochemistry   19 - 30   2006

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  • Nitric oxide mediates glucose-induced apoptosis in long-term cultured retinal pericytes

    T Hikichi, M Sasaki, A Yoshida, N Shishido, M Nakamura, K Ishikawa, J Iwamoto, Y Hayashi

    INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE   44   U339 - U339   2003.5

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    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:ASSOC RESEARCH VISION OPHTHALMOLOGY INC  

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  • LECラット尿中での銅とポルフィリンの関係

    中山 憲司, 高澤 啓, 宍戸 直美, 奥井 登代, 市原 侃, 中村 正雄, 田村 守, 田村 正秀

    生化学   74 ( 8 )   821 - 821   2002.8

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  • Uroporphyrin-induced photooxidation of conjugated bilirubin

    N Shishido, K Nakayama, S Nakamura, M Nakamura

    FREE RADICAL BIOLOGY AND MEDICINE   33   S179 - S179   2002

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    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:PERGAMON-ELSEVIER SCIENCE LTD  

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  • 肝炎発症前のLECラット肝でも、銅メタロチオネイン(Cu(I)s-MTs)は、抗酸化的に働く

    宍戸直美, 中山憲司, 高澤啓, 大山徹, 中村正雄

    磁気共鳴と医学   11   131 - 134   2000

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    Language:Japanese  

    雑誌掲載版

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    Other Link: http://search.jamas.or.jp/link/ui/2001217161

  • Effects of CP-060S, a novel Ca2+ channel blocker, on oxidative stress in cultured cardiac myocytes

    A Hara, T Suzuki, H Hashizume, N Shishido, M Nakamura, F Ushikubi, Y Abiko

    EUROPEAN JOURNAL OF PHARMACOLOGY   385 ( 1 )   81 - 88   1999.11

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    Language:English   Publisher:ELSEVIER SCIENCE BV  

    The effect of (-)-(S)-2-[3,5-bis(1,1-dimethylethyl)-4-hyroxyphenyl]-3-[3-[N-methyl-N-[2-(3,4-methylenedioxyphenoxy)-ethyl]amino]propyl]-1,3-thiazolidin-4-one hydrogen fumarate (CP-060S), a novel Ca2+ channel blocker, on hydrogen peroxide (H2O2)- induced cytotoxicity was studied in cultured rat cardiac myocytes. The CP-060S effect was compared with that of CP-060R, an optical isomer of CP-060S with a less potent Ca2+ channel blocking action than CP-060S. H2O2 increased the release of lactate dehydrogenase from cardiac myocytes and decreased the formation of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide) (MTT) formazan in cardiac myocytes (i.e., cytotoxic action). Both CP-060S (1 mu M) and CP-060R (1 mu M) attenuated to a similar extent the foregoing alterations induced by H2O2. On the otherhand, 1,3-dimethyl-2-thiourea (10 mM), a scavenger of both H2O2 and hydroxyl radical, also attenuated the H2O2-induced cytotoxicity whereas diltiazem(10 mu M) did not. In an experiment using electron spin resonance (ESR) with 5,5-dimethyl-1-pyrroline N-oxide (DMPO), a spin-trapping agent, both CP-060S and CP-060R decreased the intensity of DMPO-hydroxyl radical signal concentration dependently. These results suggest that CP-060S protects cardiac myocytes from oxidative stress through its radical scavenging action. (C) 1999 Elsevier Science B.V. All rights reserved.

    DOI: 10.1016/S0014-2999(99)00708-6

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  • LECラット肝サイトゾルにおける銅の反応性

    宍戸 直美, 中山 憲司, 高澤 啓, 大山 徹, 中村 正雄

    生化学   71 ( 8 )   1022 - 1022   1999.8

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  • 銅によるDNA切断はGSH又はMTsの存在で抑制される

    宍戸 直美, 中山 憲司, 高沢 啓, 大山 徹, 中村 正雄

    生化学   70 ( 8 )   861 - 861   1998.8

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  • Evaluation of Cu(I)-metallothioneins from LEC rat liver as antioxidants

    NAKAMURA Masao, NAKAYAMA Kenji, SHISHIDO Naomi, YUMINO Kunio, OHYAMA Tohru

    6 ( 1 )   1 - 6   1997.6

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  • メタロチオネインに結合する銅により活性酸素種が生成する

    宍戸 直美, 中山 憲司, 大山 徹, 林 隆章, 弓野 邦夫, 中村 正雄

    日本分子生物学会年会プログラム・講演要旨集   19   490 - 490   1996.8

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Presentations

  • アミロイド前駆体タ ンパク質はNF-κBを介してIL-8/IL-8R系を調節する。

    宍戸直美, 春見達郎, 林要喜知, 村山次哉

    第91回日本生化学会大会 

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    Event date: 2018.9

    Language:Japanese   Presentation type:Poster presentation  

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  • Immunoglobulin superfamily member BT-IgSF (IgSF11) mediates neuronal network formation via regulating cell adhesion.

    Naomi Shishido, Osamu Mutoh, Tsubasa Ueda, Yoshiki Hira, Tatsuo Harumi, Yokichi Hayashi

    ConBio2017 

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    Event date: 2017.12

    Language:Japanese   Presentation type:Poster presentation  

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  • Reactions of amyloid beta peptides with HOCl and taurine-chloramine.

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    Event date: 2009.10

    Language:English   Presentation type:Poster presentation  

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  • Cross-link formation of amyloid beta peptides with ferrylMb.

    Shishido N., Akutsu H., Hayashi T., Nakamura M.

    BMB2008 

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    Event date: 2008.12

    Language:English   Presentation type:Poster presentation  

    Venue:神戸  

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  • Antioxidant activity of amyloid beta peptide.

    Shishido N., Akutsu H., Hayashi T., Nakayama K., Nakamura M.

    BMB2007 

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    Event date: 2007.12

    Language:English   Presentation type:Poster presentation  

    Venue:横浜  

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  • Effects of amyloid beta peptides upon the redox activity of copper. International conference

    Shishido N., Hayashi Y., Hayashi T., Nakayama K., Nakamura M.

    20th IUBMB 

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    Event date: 2006.6

    Language:English   Presentation type:Poster presentation  

    Venue:Kyoto, Japan  

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  • Reactions of thioureylene antithyroid drugs with hypochlorous acid. International conference

    Nakamura M., Nakamura S., Shishido N.

    The 4th International Peroxidase Meeting 

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    Event date: 2004.4

    Language:English   Presentation type:Oral presentation (general)  

    Venue:Kyoto, Japan  

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Research Projects

  • アミロイドベータペプチドの抗酸化性検討

    2004

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    Grant type:Competitive

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  • antioxidative characteristics of amyloid beta peptide

    2004

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    Grant type:Competitive

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  • 酸化還元状態

    1995

    その他の研究制度 

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    Grant type:Competitive

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  • redox state

    1995

    The Other Research Programs 

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    Grant type:Competitive

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  • 細胞接着分子IgSF11の作用機序解析と制がんへの応用

    ライフサイエンス基礎科学研究 

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Teaching Experience

  • Food and Health

    2022.10 Institution:Asahikawa Medical College

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  • 科学論文の読み方書き方

    2017.10 Institution:旭川医科大学

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  • Basic Biology Experiments

    2017.4 Institution:Asahikawa Medical College

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  • Life Science

    2017.4 Institution:Asahikawa Medical College

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  • 基礎化学、基礎生化学

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  • 薬理学

    Institution:旭川大学

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  • 基礎生化学実験

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Social Activities

  • 派遣講座 中学生の生命科学実験~ヒトの体のしくみを知ろう(ゆっくらす)

    2020.2 - 2025.2

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    令和2年2月21日
    不登校児(中学生)対象の出張実験

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  • 派遣講座 中学生の生命科学実験~ヒトの体のしくみを知ろう(旭川市立緑が丘中学校)

    2019.8

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    令和元年8月1日(木)~8月2日(金)

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  • 放送大学 北海道学習センター(旭川) 非常勤講師

    2019.5

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    面接授業(認知症予防のための遺伝医学入門)

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  • 派遣講座 中学生の生命科学実験~ヒトの体のしくみを知ろう(東川町)

    2018.7

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    平成30年7月26日(木) 東川町立東川中学校

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  • 派遣講座 中学生の生命科学実験~ヒトの体のしくみを知ろう(旭川市立緑が丘中学校)

    2017.8

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    平成29年8月1日(火)~平成29年8月2日(水)

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  • 上川教育研究会

    2017.8

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    平成29年8月23日(水)
    本学内実験実習機器センター見学

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  • 派遣講座 中学生の生命科学実験~ヒトの体のしくみを知ろう(旭川市立春光台中学校)

    2016.12

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  • 旭川大学短期大学部 非常勤講師

    2016.10 - 2017.3

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    生化学実習

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  • 派遣講座 中学生の生命科学実験~ヒトの体のしくみを知ろう(旭川市立緑が丘中学校)

    2016.8

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  • 北都保健福祉専門学校看護学科非常勤講師

    2011.4 - 2012.5

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  • 二輪草キッズサマースクール「色のしくみをりかいしよう」講師

    2010.7

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  • 旭川市総合計画推進委員会委員

    2010.5 - 2011.3

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  • サイエンス・キャンプ「ニューロンの神経突起を観察してみよう」指導員

    2010.3

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    生命科学教室への協力

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  • サイエンス・パートナーシップ・プロジョクト指導員

    2009.7 - 2021.3

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    生命科学教室への協力

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  • 旭川大学保健福祉学部保健看護学科非常勤講師

    2009.4 - 2014.9

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    薬理学、生化学

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  • 派遣講座「食べ物の化学」

    2003.5 - 2009.7

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    2003年1回、2008年2回、2009年1回実施

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