| JaLCDOI | 10.18926/AMO/49252 |
|---|---|
| フルテキストURL | 67_1_9.pdf |
| 著者 | Fatmawati, Ni Nengah Dwi| Sakaguchi, Yoshihiko| Suzuki, Tomonori| Oda, Masataka| Shimizu, Kenta| Yamamoto, Yumiko| Sakurai, Jun| Matsushita, Osamu| Oguma, Keiji| |
| 抄録 | Clostridium botulinum type C and D strains recently have been found to produce PLC on egg yolk agar plates. To characterize the gene, enzymatic and biological activities of C. botulinum PLCs (Cb-PLCs), the cb-plc genes from 8 strains were sequenced, and 1 representative gene was cloned and expressed as a recombinant protein. The enzymatic and hemolytic activities of the recombinant Cb-PLC were measured and compared with those of the Clostridium perfringens alpha-toxin. Each of the eight cb-plc genes encoded a 399 amino acid residue protein preceded by a 27 residue signal peptide. The protein consists of 2 domains, the N- and C-domains, and the overall amino acid sequence identity between Cb-PLC and alpha-toxin was greater than 50%, suggesting that Cb-PLC is homologous to the alpha-toxin. The key residues in the N-domain were conserved, whereas those in the C-domain which are important in membrane interaction were different than in the alpha-toxin. As expected, Cb-PLC could hydrolyze egg yolk phospholipid, p-nitrophenylphosphorylcholine, and sphingomyelin, and also exhibited hemolytic activity;however, its activities were about 4- to over 200-fold lower than those of alpha-toxin. Although Cb-PLC showed weak enzymatic and biological activities, it is speculated that Cb-PLC might play a role in the pathogenicity of botulism or for bacterial survival. |
| キーワード | botulinum phospholipase C botulinum toxin phospholipase C activity sphingomyelinase activity hemolytic activity |
| Amo Type | Original Article |
| 出版物タイトル | Acta Medica Okayama |
| 発行日 | 2013-02 |
| 巻 | 67巻 |
| 号 | 1号 |
| 出版者 | Okayama University Medical School |
| 開始ページ | 9 |
| 終了ページ | 18 |
| ISSN | 0386-300X |
| NCID | AA00508441 |
| 資料タイプ | 学術雑誌論文 |
| 言語 | 英語 |
| 著作権者 | CopyrightⒸ 2013 by Okayama University Medical School |
| 論文のバージョン | publisher |
| 査読 | 有り |
| PubMed ID | 23439504 |
| Web of Science KeyUT | 000316829900002 |
| 関連URL | http://ousar.lib.okayama-u.ac.jp/metadata/49731 |
| JaLCDOI | 10.18926/AMO/48668 |
|---|---|
| フルテキストURL | 66_4_291.pdf |
| 著者 | Yokoyama, Teruhiko| Yamamoto, Yumiko| Suzuki, Tomonori| Oguma, Keiji| Nagai, Atsushi| |
| 抄録 | Several studies have demonstrated the efficacy of intraprostatic injection of botulinum neurotoxin type A (BoNT/A) against symptomatic benign prostatic hyperplasia (BPH). The most commonly used BoNT/A product, Botox®, forms large complexes and composed of neurotoxin (NTX) as well as non-toxic components. We purified NTX lacking non-toxic components. We investigated the efficacy of this newly purified NTX for men with BPH. Ten male patients (mean age, 70.0 years) with BPH received 100 units (prostate volume [PV] ＜30ml) or 200 units (PV ｧ30ml) of NTX injected into the prostate via a minimally invasive outpatient technique. Evaluation included uroflowmetry, postvoid residual urine volume (PVR), PV, and International Prostate Symptom Score (IPSS) measured at baseline and 1, 3, 6, and 12 months post-treatment. The status of 7 of the 10 patients examined was found to have improved within 1 month of treatment. The mean IPSS decreased from 23.8±7.0 to 16.3±10.3 (p＝0.0093) at 1 month, to 14.9±8.2 (p＝0.0074) at 3 months, and to 16.9±7.3 (p＝0.018) at 12 months. The mean PV decreased from 47.8±21.2 to 39.2±19.5ml (p＝0.0076) at 3 months. The PVR improved at 3 and 6 months post-treatment. Intraprostatic NTX injection induces prostate shrinkage and is effective in men with BPH. |
| キーワード | botulinum neurotoxin type A benign prostatic hyperplasia therapy |
| Amo Type | Original Article |
| 出版物タイトル | Acta Medica Okayama |
| 発行日 | 2012-08 |
| 巻 | 66巻 |
| 号 | 4号 |
| 出版者 | Okayama University Medical School |
| 開始ページ | 291 |
| 終了ページ | 297 |
| ISSN | 0386-300X |
| NCID | AA00508441 |
| 資料タイプ | 学術雑誌論文 |
| 言語 | 英語 |
| 著作権者 | CopyrightⒸ 2012 by Okayama University Medical School |
| 論文のバージョン | publisher |
| 査読 | 有り |
| PubMed ID | 22918201 |
| Web of Science KeyUT | 000307918900001 |
| JaLCDOI | 10.18926/AMO/48565 |
|---|---|
| フルテキストURL | 66_3_253.pdf |
| 著者 | Zhang, Kai| Yamamoto, Yumiko| Suzuki, Tomonori| Yokota, Kenji| Ma, Shaobo| Nengah Dwi Fatmawati, Ni| Oguma, Keiji| |
| 抄録 | Cultured Clostridium botulinum strains produce progenitor toxins designated as 12S, 16S, and 19S toxins. The 12S toxin consists of a neurotoxin (NTX, 7S) and a non-toxic non-hemagglutinin (NTNH). The 16S and 19S toxins are formed by conjugation of the 12S toxin with hemagglutinin (HA), and the 19S toxin is a dimer of the 16S toxin. Type A cultures produce all 3 of these progenitor toxins, while type E produces only the 12S toxin. The 7S toxin is cleaved into heavy (H) and light (L) chains by a protease(s) in some strains, and the H chain has 2 domains, the N-terminus (Hn) and C-terminus (Hc). It has been reported that type A toxins bind to the intestinal cells or cultured cells via either HA or Hc. In this study, we investigated the binding of type A and E toxins to Caco-2 cells using Western blot analysis. Both the type E 7S and 12S toxins bound to the cells, with the 7S toxin binding more strongly, whereas, in the type A strain, only the 16S/19S toxins showed obvious binding. Pre-incubation of the type E 7S toxin with IgG against recombinant type E Hc significantly inhibited the 7S toxin binding, indicating that Hc might be a main binding domain of the type E toxin. |
| キーワード | Clostridum botulinum neurotoxins Caco-2 binding Hc |
| Amo Type | Original Article |
| 出版物タイトル | Acta Medica Okayama |
| 発行日 | 2012-06 |
| 巻 | 66巻 |
| 号 | 3号 |
| 出版者 | Okayama University Medical School |
| 開始ページ | 253 |
| 終了ページ | 261 |
| ISSN | 0386-300X |
| NCID | AA00508441 |
| 資料タイプ | 学術雑誌論文 |
| 言語 | 英語 |
| 著作権者 | CopyrightⒸ 2012 by Okayama University Medical School |
| 論文のバージョン | publisher |
| 査読 | 有り |
| PubMed ID | 22729106 |
| Web of Science KeyUT | 000305669700009 |
| 関連URL | http://ousar.lib.okayama-u.ac.jp/metadata/48451 |