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
発行日 2013-02
出版物タイトル Acta Medica Okayama
67巻
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 English
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 Sience 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
発行日 2012-08
出版物タイトル Acta Medica Okayama
66巻
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 English
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 Sience 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
発行日 2012-06
出版物タイトル Acta Medica Okayama
66巻
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 English
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 Sience KeyUT 000305669700009
関連URL http://ousar.lib.okayama-u.ac.jp/metadata/48451