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Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis.

Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis. Research Abstract Details 

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  • Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis. Abstract Text:

    hideki katayamaHideki Katayama,haruo yokotaHaruo Yokota,tetsuyuki akaoTetsuyuki Akao,osamu nakamuraOsamu Nakamura,michio ohbaMichio Ohba,eisuke mekadaEisuke Mekada,eiichi mizukiEiichi Mizuki,

    Pro-parasporin-1 is a parasporal inclusion protein of the non-insecticidal Bacillus thuringiensis strain A1190. Cytotoxic fragments, named parasporin-1, were generated from pro-parasporin-1 by trypsin digestion. Parasporin-1 was purified by a combination of chromatography procedures based on the cytotoxic activity to HeLa cells. Two different fragments of 15-kDa and 56-kDa were detected in the purified parasporin-1 fraction. These fragments were tightly associated with each other and could not be separated by chromatography under conditions that preserve cytotoxic activity, indicating that the active form of parasporin-1 is a heterodimer of the 15- and 56-kDa fragments. Amino acid sequencing and MALDI-TOF mass spectrometric analysis revealed that parasporin-1 is generated from pro-parasporin-1 by trypsin digestion at Arg 93 and Arg 231. Of 12 human cell lines tested, parasporin-1 showed strong cytotoxicity to four cell lines derived from cancer tissues, but low to no cytotoxicity to the other cell lines. The time-courses of cytotoxicity indicated that the mode of action of parasporin-1 to sensitive cells differs from that shown for previously isolated cytotoxic proteins from Bacillus thuringiensis, Cyt proteins, and other bacterial pore-forming toxins. Thus, parasporin-1 is a novel cytotoxic protein to human cancer cells produced by B. thuringiensis, and may be useful as a tool to recognize and destroy specific cancer cells.

    Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis. Publishing Authors By Initials

    h katayamaH Katayama,h yokotaH Yokota,t akaoT Akao,o nakamuraO Nakamura,m ohbaM Ohba,e mekadaE Mekada,e mizukiE Mizuki,

    For similar animals: chordata: vertebrates: mammals: rodentia: muridae: murinae: mice research abstracts see: animals: chordata: vertebrates: mammals: rodentia: muridae: murinae: mice research

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    Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 137

    Page Numbers: 17-25

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Jan

    YEAR: 2005

    Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis. Keywords Mesh Terms:

    KEYWORDS: Mice

    MESH TERMS: toxicity

    Chemical & Substance for Abstract: Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis. Information

    Substance Name: parasporin

    Registry Number: 0

    Grant and Affiliation Information for Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis.

    AFFILIATION: Biotechnology and Food Research Institute, Fukuoka Industrial Technology Center, Kurume, Fukuoka 839-0861, Japan.

    Country: Japan

    Japan Research PublicationJapan Research Publication

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    MEDLINETA: J Biochem

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    Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis Related Publications

     

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