支部賛助企業（裏表紙）_130613
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6 PPARα 12 40mg/kg/day 80mg/kg/day Vehicle n DMSO 50µl 16 RNA PCR 16 16
7 PGC
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9 Pru p Pru p 1Pru p 3Pru p 4Pru p 3Lipid Transfer ProteinLTPLTP 9kDaS-S ImmunoCAPLTPIgE LTPLTP Gibberellin Regulated ProteinGRPPru p 7GRP63 126S-S GRP LTPGRPmAb LTPGRP 30M:F=11:1932.2ELISA 3 Pru p 1Pru p 3Pru p 4 ImmunoCAPIgE 1416 GRPELISA724/5 0/6LTPPichia pastorisltpgrpmab IgEGRPGRP LTPGRP mabelisa LTPGRPLTPGRP LTPGRP
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11 1, 2, L. delbrueckiil. paracasei IFsIFs IFs L. paracaseil. delbrueckii L. delbrueckiiifs IFs L. paracasei MRS IFs L. delbrueckiil. paracasei2ph TLC IFs IFsL. delbrueckiil. paracasei IFs HPLC IFs L. delbrueckiiifs L. paracaseitlcl. paracaseiifs L. delbrueckiihplcl. paracasei IFsL. delbrueckii L. paracaseiifs L. delbrueckiiifs L. delbrueckiiifs
12 Thermococcus kodakarensis 3-phosphoglycerate dehydrogenase homolog 1 1, 2 1 1, JST, CREST Thermococcus kodakarensis Ser glycine/serine hydroxymethyltransferase (Tk-glyA, TK0528) (Fig. 1) Ser Gly Ser Ser pyruvate (Pyr) Pyr Ser Pyr (Fig. 1) Pyr 3-phosphoglycerate (3PGA) 3-phosphohydroxypyruvate 3-phosphoglycerate dehydrogenase (3PGDH) T. kodakarensis Sulfolobus tokodaii 3-phosphoglycerate dehydrogenase 3 TK0551 (Tk-ldhA; 28.8%)TK0683 (Tk-ldhA; 33.2%)TK1966 (Tk-serA; 41.2%) 3 3PGDH homolog Ser (Fig. 1) T. kodakarensis Ser Ser Tk-glyA Gly Ser 3 3PGDH homolog Pyr Ser Tk-glyA TK1966 Pyr Ser Tk-glyA Tk-ldhA annotate TK0551 TK0683 Tk-glyA TK1966 Pyr Ser TK0551 TK0683
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14 Mortierella alpina 1S-4 Δlig ,2 3 1,4 1, º
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16 ECOR ,2 1 2 DNA ECORE. coli Collection of Reference24 ECOR24 8kb 10kb 8kb 8.5kb BLAST 8kb transposase DNA DNA PCR 10kb 8kb
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18 New source of L-asparaginase from Arthrospira (Spirulina) platensis : localization and improvement of production of L-asparaginase Asep A. Prihanto, Midori Umekawa, and Mamoru Wakayama (Dept. Biotechnology, Graduate School of Life Sciences, Ritsumeikan University) [Introduction] L-Asparaginase (EC ; L-asparagine amidohydrolase) has been attracting intense research interest over the past year due to their potential medicinal uses and application in food. Among microbial source of L-asparaginase, only Aspergillus oryzae in food and Escherichia coli and Erwinia sp. in medicine have been intensively studied. Recent finding showed that the application of those enzymes contained several drawbacks. In this study, we explored and investigated the new source of L-asparaginase, Arthrospira (Spirulina) platensis throughout localization of L-asparaginase in A. platensis and enhanced its production. [Methods] Enzyme localization was conducted by culturing cells in SOT medium and extracting the enzymes from different parts of the cell. The Taguchi method with L9 orthogonal array was designed for improving L-asparaginase production. The factors studied in this study consist of nitrogen (N), iron (Fe), and sodium chloride (NaCl) along with temperature stress at 22 C in dark for varied duration [Result and Discussion] L-asparaginase mostly exists in the cytoplasmic region. Its production could be induced by subjecting combined stress culture conditions. The highest production of L-asparaginase was attained by NaNO 3, NaCl, and FeSO 4 7H 2 O at concentrations of, g/l, 0.25 M, and g/l, respectively with 1-h temperature shock at 22 C in the dark. In individual factor analysis, nitrogen was the most critical compound in order to produce high production of L-asparaginase in A. platensis and the least effect was shown in iron. Contrastingly, combination of sodium chloride and duration of temperature stress contributed the highest impact in producing L-asparaginase. This result gives us a new understanding that interactions of parameters could have different effects on L-asparaginase production compared with individual parameters. Our combined stress culture condition that was designed through the Taguchi method analysis successfully enhanced 2.17-fold L-asparaginase production in A. platensis. Here we revealed that combined stresses could be applied to optimize L-asparaginase production in A. platensis.
19 O O- 2 Tetranychus urticae O-DMAE Fig. 1 PBO DMAE - PBO DMAE DMAE p-qm Fig. 2
20 P6522 (/)8 C G1 G4 G5 G6 G3 G4 G4 α-1,6 G3 G3
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23 Shewanella livingstonensis Ac10
24 AD 40 β Aβ40 42 Aβ40Aβ42 Aβ42 AD 2 ~ 4 Aβ42 AD Aβ42 Aβ42 Aβ42 Aβ42 AD AD in vitro in vivo β Aβ42 Aβ42 PEG-PS HATU Fmoc Aβ42 Aβ42 β Aβ42 Glu22 Asp23 1 AD Glu22 Asp23 Aβ42 ESRAβ42
25 β Tyr10 Met35 15 A Aβ40 15~20 A Aβ42 C β Met C C Aβ42 1 PC12 Aβ42 Aβ40 Aβ42 AD Aβ42 NMR Aβ42 2 2A Aβ42
26 ハプテンには 毒性ターン構造をミミ ック 模倣 した配座固定ペプチド 図 2A を設計し 22 番目付近でタ ーン構造を取りやすい E22P-Aβ42 に 対して強く反応し ターンを取りにく い E22V-Aβ42 にはほとんど反応しな いモノクローン 11A1 と命名 の取 得に成功した 一方 22 番目付近のア ミノ酸配列をエピトープとした従来の 市販抗体 4G8 も同様に評価したと ころ 11A1 とは異なり E22P-Aβ42 にはほとんど反応せず E22V-Aβ42 に 対して顕著に結合した 次に AD 患者の剖検脳 海馬なら びに前頭葉領域 を用いて 11A1 抗 体の免疫組織染色実験を行ったところ 4G8 などの従来の市販抗体では染色さ れない細胞内 Aβ に対しても 11A1 抗 体は反応した 図 2B 矢頭 また 図 2 毒性ターン抗体 11A1 の A 作製戦略なら びに AD 患者脳を用いた B 免疫組織染色 矢頭 11A1 抗体は AD 患者脳の抽出物中の 細胞内 Aβ 矢印 細胞外 Aβ 老人班 ならびに Aβ オリゴマー 3 量体 に対して C ウェスタンブロッティング 強く反応することも明らかになった 図 2C 近年 AD 発症前に現れる Aβ オリゴマーは細胞内に多く存在する臨床デ ータが報告されていることから 11A1 抗体は AD 発症の前段階を捉えている可能性 がある ごく最近 11A1 を用いた国内外の複数の研究グループとの共同研究によっ て 既存抗体では染色が困難とされる細胞内 Aβ オリゴマーの検出や AD 病態を反映 した染色像が報告されており 関連分野の研究者の関心を集めている 以上の結果 より 11A1 抗体は有望な AD 治療薬及び診断薬になる可能性が高い ３.酸化ストレスによる Aβ42 の in vivo での神経細胞毒性発現機構と機能性食品因 子による AD 病態の予防 Aβ42 のオリゴマー化は Aβ42 自身が酸化によりラジカル化することが引き金に なることが 本講演者らの研究によって明らかになった 図 1 そこで 酸化スト レスに対する修復酵素の一つである CuZn-SOD 細胞質 SOD or SOD1 の欠損マウ スと代表的な AD モデルマウス Tg2576 系統 を交配させることで AD 病態への 酸化ストレスの影響を調べた SOD1 の欠損マウス自身は 種々の老年病様症状 加 齢黄斑変性 骨粗鬆症 皮膚萎縮 筋萎縮など を示すことが知られている その 結果 SOD1 が欠損した AD マウスでは脳内の酸化ストレス 細胞質スーパーオキシ ドラジカル量の亢進など が増大し 老人斑だけでなく Aβ オリゴマー量が顕著に
27 図 3 SOD1 が欠損した AD モデルマウスの A 老人斑染色, B ドットブロット法によるオリゴマー 形成能評価, C 空間記憶機能テスト モリス水迷路試験による遊泳の軌跡を示し 矢頭は遊泳の 出発地点を指す SOD1 が欠損した AD マウスは 他の 3 種類のマウス群とは異なり プール全 体に徘徊軌跡が広がっている 増大した 図 3A, B またオリゴマー量の増大と相関して 神経細胞毒性ならびに 空間記憶機能の異常を示す時期が著しく早くなった 図 3C 興味深いことに AD 患者の剖検脳抽出物を用いて各種 SOD アイソザイム SOD1~3 の量を調べたとこ ろ SOD1 のみ非 AD 群に比べて有意に低下していた 本結果は 細胞質における抗 酸化機能の低下が AD 発症に関与していることを in vivo で初めて実証したものであ る 近年 AD は生活習慣病の一種と考えられていること Aβ 凝集体の蓄積は 40 代頃 から始まることが指摘されていることから 食生活やサプリメントによる AD 予防 の必要性が強く望まれている 本講演者らは 代表的な抗酸化剤であるビタミン C あるいはマリアアザミに含まれるフラボノイド類であるシリマリンを 予防的に AD モデルマウスに摂餌させたところ いずれも Aβ のオリゴマー化ならびに AD 特有の 行動異常の出現を遅延させることができた これまで 機能性食品因子による Aβ42 のオリゴマー化抑制についての in vitro データは数多く報告されているが 動物レベ ルでの成功例はほとんどない お わ り に 現在 AD 治療に向けて多くの薬剤に関する臨床試験が行われているが そのほと んどが AD 患者を対象とした第 3 相試験ではあまり良好な結果は得られていない このような状況下 毒性立体構造という独自の視点から開発した抗 Aβ 毒性ター ン 抗体 11A1 抗体 は 停滞していた治療薬開発においてブレークスルーを与え る可能性がある 本抗体は 2010 年に国際特許出願され 2012 年 3 月に免疫生物研 究所から販売開始された 今後 11A1 抗体を機軸とした更なる展開が期待される
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