start-ver=1.4
cd-journal=joma
no-vol=36
cd-vols=
no-issue=2
article-no=
start-page=61
end-page=66
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2002
dt-pub=200203
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=Cytotoxicity of the Bacillus thuringiensis Crystal Protein against Mammalian Cells
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=The crystal proteins produced by Bacillus thuringiensis subsp, israelensis (Bti) and subsp. coreanensis A1519 strain were examined for the cytotoxicity against MOLT-4 and HeLa cells by MTT assay and LDH assay, The A1519 crystal proteins processed by proteinase K exhibited the specific cell-killing activity toward MOLT-4 with little damage to the cell membrane, On the other hand, the Bti crystal proteins processed by proteinase K caused the substantial damage to the cell membrane of both MOLT-4 and HeLa, leading to the cell lysis. The non-digested crystal proteins of both strains exhibited no cytotoxicity, These data suggested that while the Bti crystal proteins caused the colloid-osmotic swelling and cell lysis of MOLT-4 and HeLa, the proteinase K-digested A1519 crystal proteins induced the specific cell death of MOLT-4 through a mechanism other than that of Bti.
en-copyright=
kn-copyright=

en-aut-name=YamagiwaMasashi
en-aut-sei=Yamagiwa
en-aut-mei=Masashi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=NambaAkitoshi
en-aut-sei=Namba
en-aut-mei=Akitoshi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=2
ORCID=

en-aut-name=AkaoTetsuyuki
en-aut-sei=Akao
en-aut-mei=Tetsuyuki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=3
ORCID=

en-aut-name=MizukiEiichi
en-aut-sei=Mizuki
en-aut-mei=Eiichi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=4
ORCID=

en-aut-name=OhbaMichio
en-aut-sei=Ohba
en-aut-mei=Michio
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=5
ORCID=

en-aut-name=SakaiHiroshi
en-aut-sei=Sakai
en-aut-mei=Hiroshi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=6
ORCID=

affil-num=1
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Okayama University

affil-num=2
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Okayama University

affil-num=3
en-affil=
kn-affil=Biotechnology and Food Research Institute, Fukuoka Industrial Technology Center

affil-num=4
en-affil=
kn-affil=Biotechnology and Food Research Institute, Fukuoka Industrial Technology Center

affil-num=5
en-affil=
kn-affil=Graduate School of Agriculture, Kyusyu University

affil-num=6
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Okayama University
END

start-ver=1.4
cd-journal=joma
no-vol=37
cd-vols=
no-issue=2
article-no=
start-page=67
end-page=72
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2003
dt-pub=200303
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=The role of helices of domain I for the insecticidal activity of Bacillus thuringiensis Cry4A toxin
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=An active form of Cry4A is a heterodimer of the 20- and 45-kDa fragments that are derived from the 130-kDa Cry4A protoxin. To investigate the function of these two fragments, several deletion mutants were constructed and expressed in E.coli as the GST (glutathione-S-transferase) fusion proteins. The results of the bioassay against Culex pipiens larvae showed that the interaction of two fragments of Cry4A was necessary for the toxicity, and that the C-terminal 67 amino acids of the 20-kDa fragment corresponding to the helices α4 and α5 were involved in determining the insecticidal activity. Surprisingly the lack of helix α5 did not affect the toxicity to C. pipiens, suggesting that the role of helix α5 of Cry4A was different from that postulated in the case of Cry4A toxins.
en-copyright=
kn-copyright=

en-aut-name=YamagiwaMasashi
en-aut-sei=Yamagiwa
en-aut-mei=Masashi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=SakaiHiroshi
en-aut-sei=Sakai
en-aut-mei=Hiroshi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=2
ORCID=

affil-num=1
en-affil=
kn-affil=Department of Bioscience and Biotechnology Okayama University

affil-num=2
en-affil=
kn-affil=Department of Bioscience and Biotechnology Okayama University
END

start-ver=1.4
cd-journal=joma
no-vol=38
cd-vols=
no-issue=1-2
article-no=
start-page=97
end-page=100
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2004
dt-pub=200403
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=The cytotoxicity of Bacillus thuringiensis subsp. coreanensis A2316 strain against the human leukemic T cell
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=Bacillus thuringiensis subsp. coreanensis A2316 is a newly isolated strain from Yonakunijima Island in Japan. It produces the proteinaceous inclusion body (crystal) which has no insecticidal and hemolytic activities. When the crystal proteins were digested by proteinase K, they exhibited the strong cytotoxicity against human leukemic T cell, MOLT-4. The proteinase K-digested A2316 crystal proteins have little damage upon the cell membrane of MOLT-4, suggesting that the cell death of MOLT-4 was induced through a mechanism other than the colloid-osmotic swelling and cell lysis as caused by hitherto known B. thuringiensis crystal proteins. The 29-kDa polypeptide proved to be an active component of the proteinase K-digested A2316 crystal proteins. EC(50) of the purified 29-kDa polypeptide was 0.0579 μg/ml. The N-terminal amino acid sequence of the 29-kDa polypeptide was identical with that of p29 produced by B. thuringiensis A1519 strain and shared no significant homology with all the known proteins, suggesting that this polypeptide belong to a new family of B. thuringiensis crystal proteins.
en-copyright=
kn-copyright=

en-aut-name=YamagiwaMasashi
en-aut-sei=Yamagiwa
en-aut-mei=Masashi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=HiraoTaichi
en-aut-sei=Hirao
en-aut-mei=Taichi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=2
ORCID=

en-aut-name=KiyomiMasaaki
en-aut-sei=Kiyomi
en-aut-mei=Masaaki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=3
ORCID=

en-aut-name=AkaoTetsuyuki
en-aut-sei=Akao
en-aut-mei=Tetsuyuki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=4
ORCID=

en-aut-name=MizukiEiichi
en-aut-sei=Mizuki
en-aut-mei=Eiichi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=5
ORCID=

en-aut-name=OhbaMichio
en-aut-sei=Ohba
en-aut-mei=Michio
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=6
ORCID=

en-aut-name=SakaiHiroshi
en-aut-sei=Sakai
en-aut-mei=Hiroshi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=7
ORCID=

affil-num=1
en-affil=
kn-affil=Department of Bioscience and Biotechnology Okayama University

affil-num=2
en-affil=
kn-affil=Department of Bioscience and Biotechnology Okayama University

affil-num=3
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University

affil-num=4
en-affil=
kn-affil=Biotechnology and Food Research Institute Fukuoka Industrial Technology Center

affil-num=5
en-affil=
kn-affil=Biotechnology and Food Research Institute Fukuoka Industrial Technology Center

affil-num=6
en-affil=
kn-affil=Graduate School of Agriculture Kyushu University

affil-num=7
en-affil=
kn-affil=Department of Bioscience and Biotechnology Okayama University
END

start-ver=1.4
cd-journal=joma
no-vol=25
cd-vols=
no-issue=
article-no=
start-page=2
end-page=6
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2003
dt-pub=200308
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=微生物農薬による害虫の防除と環境保全
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=
en-copyright=
kn-copyright=

en-aut-name=SakaiHiroshi
en-aut-sei=Sakai
en-aut-mei=Hiroshi
kn-aut-name=酒井裕
kn-aut-sei=酒井
kn-aut-mei=裕
aut-affil-num=1
ORCID=

en-aut-name=YamagiwaMasashi
en-aut-sei=Yamagiwa
en-aut-mei=Masashi
kn-aut-name=山際雅詩
kn-aut-sei=山際
kn-aut-mei=雅詩
aut-affil-num=2
ORCID=

affil-num=1
en-affil=
kn-affil=岡山大学工学部生物機能工学科

affil-num=2
en-affil=
kn-affil=岡山大学工学部生物機能工学科
END

start-ver=1.4
cd-journal=joma
no-vol=93
cd-vols=
no-issue=5-6
article-no=
start-page=579
end-page=592
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=1981
dt-pub=19810630
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=Body surface isopotential maps in the case of R.B.B.B. special reference to Atrial Septal Defect. (Comparative study of the data from cardiac catetherization and two dimensional echocardiograms.)
kn-title=右脚ブロックの体表面心臓電位図（特に心房中隔欠損症を中心として）―超音波検査,右心カテーテル検査との対比―
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=A body surface isopotential map was recorded in 30 cases of ASD and 3 cases of ECD with right bundle branch block in ECG, then analyzed in comparison with results obtained by cardiac catetherization and two dimensional echocardiograms. 1) In all cases of right bundle branch block, breakthrough minimum appeared later and shifted to the left compared with the normal. 2) Breakthrough minimum of ASD and ECD appeared progressively later associated with Qp/Qs ratio and left to right intracardiac shunt ratio obtained with cardiac catetherization and RVDd with echocardiogram. Breakthrough minimum of ASD and ECD moved to the left accompanied by increases in mean RV pressure, mean PA pressure and RVDd. 3) R'max voltage, the maximum positive potential in the late stage of ventricular depolarization on the right precordial area, increased and correlated well with the mean RV pressure and left to right shunt ratio increment. 4) In the case of ASD, breakthrough minimum appeared later and shifted to the left along with age.
en-copyright=
kn-copyright=

en-aut-name=YoshidaHidenori
en-aut-sei=Yoshida
en-aut-mei=Hidenori
kn-aut-name=吉田英紀
kn-aut-sei=吉田
kn-aut-mei=英紀
aut-affil-num=1
ORCID=

en-aut-name=IhoriyaKazuo
en-aut-sei=Ihoriya
en-aut-mei=Kazuo
kn-aut-name=庵谷和夫
kn-aut-sei=庵谷
kn-aut-mei=和夫
aut-affil-num=2
ORCID=

en-aut-name=NagahanaHaruki
en-aut-sei=Nagahana
en-aut-mei=Haruki
kn-aut-name=長花晴樹
kn-aut-sei=長花
kn-aut-mei=晴樹
aut-affil-num=3
ORCID=

en-aut-name=NishiharaMasanobu
en-aut-sei=Nishihara
en-aut-mei=Masanobu
kn-aut-name=西原正信
kn-aut-sei=西原
kn-aut-mei=正信
aut-affil-num=4
ORCID=

en-aut-name=HyodoTatsuo
en-aut-sei=Hyodo
en-aut-mei=Tatsuo
kn-aut-name=兵頭多津男
kn-aut-sei=兵頭
kn-aut-mei=多津男
aut-affil-num=5
ORCID=

en-aut-name=UchidaToshiaki
en-aut-sei=Uchida
en-aut-mei=Toshiaki
kn-aut-name=内田俊明
kn-aut-sei=内田
kn-aut-mei=俊明
aut-affil-num=6
ORCID=

en-aut-name=KimuraMasashi
en-aut-sei=Kimura
en-aut-mei=Masashi
kn-aut-name=木村正司
kn-aut-sei=木村
kn-aut-mei=正司
aut-affil-num=7
ORCID=

en-aut-name=TakedaKou
en-aut-sei=Takeda
en-aut-mei=Kou
kn-aut-name=武田光
kn-aut-sei=武田
kn-aut-mei=光
aut-affil-num=8
ORCID=

en-aut-name=FujiiAkinobu
en-aut-sei=Fujii
en-aut-mei=Akinobu
kn-aut-name=藤井章伸
kn-aut-sei=藤井
kn-aut-mei=章伸
aut-affil-num=9
ORCID=

en-aut-name=SaitoDaiji
en-aut-sei=Saito
en-aut-mei=Daiji
kn-aut-name=斉藤大治
kn-aut-sei=斉藤
kn-aut-mei=大治
aut-affil-num=10
ORCID=

en-aut-name=TanataniSetsuro
en-aut-sei=Tanatani
en-aut-mei=Setsuro
kn-aut-name=種谷節郎
kn-aut-sei=種谷
kn-aut-mei=節郎
aut-affil-num=11
ORCID=

en-aut-name=KitaToshimasa
en-aut-sei=Kita
en-aut-mei=Toshimasa
kn-aut-name=喜多利正
kn-aut-sei=喜多
kn-aut-mei=利正
aut-affil-num=12
ORCID=

en-aut-name=SakaiHiroshi
en-aut-sei=Sakai
en-aut-mei=Hiroshi
kn-aut-name=堺裕
kn-aut-sei=堺
kn-aut-mei=裕
aut-affil-num=13
ORCID=

en-aut-name=HaraokaShoichi
en-aut-sei=Haraoka
en-aut-mei=Shoichi
kn-aut-name=原岡昭一
kn-aut-sei=原岡
kn-aut-mei=昭一
aut-affil-num=14
ORCID=

affil-num=1
en-affil=
kn-affil=岡山大学医学部第一内科教室

affil-num=2
en-affil=
kn-affil=岡山大学医学部第一内科教室

affil-num=3
en-affil=
kn-affil=岡山大学医学部第一内科教室

affil-num=4
en-affil=
kn-affil=岡山大学医学部第一内科教室

affil-num=5
en-affil=
kn-affil=岡山大学医学部第一内科教室

affil-num=6
en-affil=
kn-affil=岡山大学医学部第一内科教室

affil-num=7
en-affil=
kn-affil=岡山大学医学部第一内科教室

affil-num=8
en-affil=
kn-affil=岡山大学医学部第一内科教室

affil-num=9
en-affil=
kn-affil=岡山大学医学部第一内科教室

affil-num=10
en-affil=
kn-affil=岡山大学医学部第一内科教室

affil-num=11
en-affil=
kn-affil=榊原十全病院

affil-num=12
en-affil=
kn-affil=榊原十全病院

affil-num=13
en-affil=
kn-affil=榊原十全病院

affil-num=14
en-affil=
kn-affil=岡山大学医学部附属病院中央検査部
en-keyword=体表面心臓電位図
kn-keyword=体表面心臓電位図
en-keyword=右脚ブロック
kn-keyword=右脚ブロック
en-keyword=心房中隔欠損
kn-keyword=心房中隔欠損
en-keyword=Breakthrough
kn-keyword=Breakthrough
END

start-ver=1.4
cd-journal=joma
no-vol=35
cd-vols=
no-issue=1-2
article-no=
start-page=147
end-page=154
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2001
dt-pub=20010327
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=The role of interhelical cleavage for insecticidal activityof Bacillus thuringiensis Cry4A toxin
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=The Cry4A toxin is a dipteran-specific insecticidal protein produced by Bacillus thuringiensis subsp. israelensis as a protoxin of 130 kDa. Its active form is a heterodimer of 20- and 45-kDa fragments which is generated by an interhelical cleavage of a 60-kDa intermediate at the position of Gln236 between α5 and α6 helices in domain I. On the other hand, Cry1Aa, which is also produced as a 130-kDa protoxin but toxic to lepidopteran larvae, was processed into the active 60-kDa fragment with no additional cleavage. To investigate the role of the intramolecular cleavage of Cry4A for its insecticidal activity, the loop between α5 and α6 of Cry4A which includes the cleavage site was substituted for the corresponding region of Cry1Aa. The resulting mutant designated GST-60Loop was expressed as a GST-fusion protein. A difference of the processing profile was observed between GST-60 and GST-60Loop in the in vitro digestion assay by trypsin, and the insecticidal activity of GST-60Loop was two-fold lower than that of GST-60. These results suggested that the interhelical cleavage of Cry4A promoted the toxicity against C. pipiens larvae.
en-copyright=
kn-copyright=

en-aut-name=YamagiwaMasashi
en-aut-sei=Yamagiwa
en-aut-mei=Masashi
kn-aut-name=山際雅詩
kn-aut-sei=山際
kn-aut-mei=雅詩
aut-affil-num=1
ORCID=

en-aut-name=SakaiHiroshi
en-aut-sei=Sakai
en-aut-mei=Hiroshi
kn-aut-name=酒井裕
kn-aut-sei=酒井
kn-aut-mei=裕
aut-affil-num=2
ORCID=

affil-num=1
en-affil=
kn-affil=Department of Bioscience and Biotechnology

affil-num=2
en-affil=
kn-affil=Department of Bioscience and Biotechnology
END