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  1. Article ; Online: Exploratory investigation of the anti-inflammatory effects of RNase A-treated

    Tamaki, Ryuji / Takahashi, Mio / Tai, Shoya / Makioka-Itaya, Yuko / Ijich, Tetsuo / Inoue, Ryo

    Bioscience, biotechnology, and biochemistry

    2019  Volume 83, Issue 7, Page(s) 1343–1353

    Abstract: We previously reported that the major component ... ...

    Abstract We previously reported that the major component of
    MeSH term(s) Animals ; Anti-Inflammatory Agents/pharmacology ; Culture Media ; Dextran Sulfate/adverse effects ; Enterococcus faecalis/drug effects ; Humans ; Interleukin-10/biosynthesis ; Mice ; Ribonuclease, Pancreatic/pharmacology
    Chemical Substances Anti-Inflammatory Agents ; Culture Media ; IL10 protein, human ; Interleukin-10 (130068-27-8) ; Dextran Sulfate (9042-14-2) ; Ribonuclease, Pancreatic (EC 3.1.27.5)
    Language English
    Publishing date 2019-04-30
    Publishing country England
    Document type Journal Article
    ZDB-ID 1106450-x
    ISSN 1347-6947 ; 0916-8451
    ISSN (online) 1347-6947
    ISSN 0916-8451
    DOI 10.1080/09168451.2019.1608805
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Exploratory investigation of the anti-inflammatory effects of RNase A-treated Enterococcus faecalis strain EC-12

    Tamaki, Ryuji / Takahashi, Mio / Tai, Shoya / Makioka-Itaya, Yuko / Ijich, Tetsuo / Inoue, Ryo

    Bioscience, biotechnology, and biochemistry. 2019 July 3, v. 83, no. 7

    2019  

    Abstract: We previously reported that the major component of Enterococcus faecalis strain EC-12 (EC-12) inducing production of Interleukin (IL)-12 in mouse/human immune cells was its own RNA. This study aimed to investigate if RNase A-treated EC-12 could also ... ...

    Abstract We previously reported that the major component of Enterococcus faecalis strain EC-12 (EC-12) inducing production of Interleukin (IL)-12 in mouse/human immune cells was its own RNA. This study aimed to investigate if RNase A-treated EC-12 could also produce IL-10 and to evaluate the possible effects of IL-10 produced by RNase A-treated EC-12. Three experiments were conducted: (1) Assessment of the effect of RNase A-treated EC-12 on transcriptome profiles and biological pathways in human peripheral blood mononuclear cells; (2) Determination of cytokine concentration in its culture supernatants; and (3) Supplementation of RNase A-treated EC-12 (RN) to mice with dextran sodium sulfate-induced colitis. Treatment of EC-12 with RNase A inhibited inflammatory response including the potency to induce IL-12 production, while it did not affect IL-10 production (Experiment 1 and 2). Colitis symptoms were milder in RN than in PBS-supplemented controls (Experiment 3). RNase A-treated EC-12 likely became an anti-inflammatory agent primarily inducing IL-10 production.
    Keywords Enterococcus faecalis ; RNA ; anti-inflammatory agents ; biotechnology ; colitis ; dextran ; humans ; inflammation ; interleukin-10 ; interleukin-12 ; mice ; ribonucleases ; sodium ; transcriptome
    Language English
    Dates of publication 2019-0703
    Size p. 1343-1353.
    Publishing place Taylor & Francis
    Document type Article
    Note NAL-light
    ZDB-ID 1106450-x
    ISSN 1347-6947 ; 0916-8451
    ISSN (online) 1347-6947
    ISSN 0916-8451
    DOI 10.1080/09168451.2019.1608805
    Database NAL-Catalogue (AGRICOLA)

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  3. Article: Topoisomerase I and ATP activate cDNA synthesis of human immunodeficiency virus type 1.

    Takahashi, Hidehiro / Sawa, Hirofumi / Hasegawa, Hideki / Shoya, Yuko / Sata, Tetsutaro / Hall, William W / Nagashima, Kazuo / Kurata, Takeshi

    Biochemical and biophysical research communications

    2002  Volume 294, Issue 2, Page(s) 509–517

    Abstract: Replication of human immunodeficiency virus type 1 (HIV-1) is regulated at reverse transcription. Cellular topoisomerase I has been reported to be carried into HIV-1 virions and enhance cDNA synthesis in vitro, suggesting that topoisomerase I expressed ... ...

    Abstract Replication of human immunodeficiency virus type 1 (HIV-1) is regulated at reverse transcription. Cellular topoisomerase I has been reported to be carried into HIV-1 virions and enhance cDNA synthesis in vitro, suggesting that topoisomerase I expressed in virus producer cells regulates reverse transcription. Here, by employing both indicator cell assay and endogenous reverse transcription (ERT) assay, we show that topoisomerase I and adenosine triphosphate (ATP) enhanced cDNA synthesis of HIV-1. In addition, topoisomerase I mutants, R488A and K532A, lacking enzymatic activity, attenuated the efficiency of cDNA synthesis and resulted in inhibition of the infectivity of HIV-1, suggesting that the activity of topoisomerase I lacking in these mutants is indispensable for the cDNA synthesis in the HIV-1 replication process. Furthermore, ATP could dissociate topoisomerase I from the topoisomerase I-RNA complex and enhance cDNA synthesis in vitro. These findings suggest that cellular topoisomerase I and ATP play a pivotal role in the synthesis of cDNA of HIV-1.
    MeSH term(s) Adenosine Diphosphate/pharmacology ; Adenosine Triphosphate/analogs & derivatives ; Adenosine Triphosphate/metabolism ; Adenosine Triphosphate/pharmacology ; Amino Acid Substitution/genetics ; DNA Topoisomerases, Type I/genetics ; DNA Topoisomerases, Type I/metabolism ; DNA Topoisomerases, Type I/pharmacology ; DNA, Complementary/biosynthesis ; Genes, Reporter ; HIV Reverse Transcriptase/metabolism ; HIV-1/growth & development ; HIV-1/metabolism ; HeLa Cells ; Humans ; Macromolecular Substances ; RNA, Viral/metabolism ; Virus Replication/drug effects ; Virus Replication/physiology
    Chemical Substances DNA, Complementary ; Macromolecular Substances ; RNA, Viral ; adenosine 5'-O-(3-thiotriphosphate) (35094-46-3) ; Adenosine Diphosphate (61D2G4IYVH) ; Adenosine Triphosphate (8L70Q75FXE) ; HIV Reverse Transcriptase (EC 2.7.7.49) ; DNA Topoisomerases, Type I (EC 5.99.1.2)
    Language English
    Publishing date 2002-06-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1016/S0006-291X(02)00503-X
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Nucleolin and the packaging signal, psi, promote the budding of human immunodeficiency virus type-1 (HIV-1).

    Ueno, Tomonori / Tokunaga, Kenzo / Sawa, Hirofumi / Maeda, Masae / Chiba, Joe / Kojima, Asato / Hasegawa, Hideki / Shoya, Yuko / Sata, Tetsutaro / Kurata, Takeshi / Takahashi, Hidehiro

    Microbiology and immunology

    2004  Volume 48, Issue 2, Page(s) 111–118

    Abstract: Gag proteins of human immunodeficiency virus type 1 (HIV-1) play a pivotal role in the budding of the virion, in which the zinc finger motifs of the gag proteins recognize the packaging signal of genomic RNA. Nucleolin, an RNA-binding protein, is ... ...

    Abstract Gag proteins of human immunodeficiency virus type 1 (HIV-1) play a pivotal role in the budding of the virion, in which the zinc finger motifs of the gag proteins recognize the packaging signal of genomic RNA. Nucleolin, an RNA-binding protein, is identified as a cellular protein that binds to murine leukemia virus (MuLV) gag proteins and regulates the viral budding, suggesting that HIV-1 gag proteins, the packaging signal, psi and nucleolin affect the budding of HIV-1. Here we report that nucleolin enhances the release of HIV-1 virions which contain psi. Furthermore, nucleolin and gag proteins form a complex incorporated into virions, and nucleolin promotes the infectivity of HIV-1. Our results suggest that an empty particle which contains neither nucleolin nor the genomic RNA is eliminated during the budding process, and this mechanism is beneficial for escape from the host immune response against HIV-1.
    MeSH term(s) Gene Products, gag/physiology ; HIV-1/genetics ; HIV-1/physiology ; HIV-1/ultrastructure ; HeLa Cells ; Humans ; Phosphoproteins/physiology ; RNA, Viral/metabolism ; RNA-Binding Proteins/physiology ; Ribonucleoproteins/metabolism ; Virion/physiology ; Virion/ultrastructure ; Virus Assembly/physiology ; Nucleolin
    Chemical Substances Gene Products, gag ; Phosphoproteins ; RNA, Viral ; RNA-Binding Proteins ; Ribonucleoproteins
    Language English
    Publishing date 2004-02-20
    Publishing country Australia
    Document type Journal Article
    ZDB-ID 224792-6
    ISSN 1348-0421 ; 0385-5600
    ISSN (online) 1348-0421
    ISSN 0385-5600
    DOI 10.1111/j.1348-0421.2004.tb03496.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Human topoisomerase I promotes HIV-1 proviral DNA synthesis: implications for the species specificity and cellular tropism of HIV-1 infection.

    Shoya, Yuko / Tokunaga, Kenzo / Sawa, Hirofumi / Maeda, Masae / Ueno, Tomonori / Yoshikawa, Tomoki / Hasegawa, Hideki / Sata, Tetsutaro / Kurata, Takeshi / Hall, William W / Cullen, Bryan R / Takahashi, Hidehiro

    Proceedings of the National Academy of Sciences of the United States of America

    2003  Volume 100, Issue 14, Page(s) 8442–8447

    Abstract: Although HIV type 1 (HIV-1) cannot efficiently replicate in simian cells, the mechanism(s) involved in the restriction of virus tropism remain unclear. To investigate this, we have focused on the identification of human cellular factors that can ... ...

    Abstract Although HIV type 1 (HIV-1) cannot efficiently replicate in simian cells, the mechanism(s) involved in the restriction of virus tropism remain unclear. To investigate this, we have focused on the identification of human cellular factors that can influence the infectivity of HIV-1 derived from African green monkey producer cells. Whereas the infectivity of HIV-1 derived from such cells was only 10-15% of that of human cell-derived virus, expression of human topoisomerase I in the African green monkey cells resulted in a 5-fold increase of the infectivity of progeny HIV-1 virions. Replacement of glutamate-236 and asparagine-237 of human topoisomerase I with the corresponding residues (aspartate and serine, respectively) of the African green monkey enzyme abolished this enhancement of HIV-1 infectivity. This positive effect of human topoisomerase I expression in the African green monkey producer cells seemed to result from the promotion of HIV-1 cDNA synthesis. Thus, human topoisomerase I plays an important role in HIV-1 replication and infectivity, and differences in the species specificity of HIV-1 infection can at least in part be attributed to differences in topoisomerase I activities.
    MeSH term(s) Amino Acid Sequence ; Animals ; COS Cells/virology ; Cell Line/virology ; Cercopithecus aethiops ; Codon ; DNA Replication ; DNA Topoisomerases, Type I/chemistry ; DNA Topoisomerases, Type I/genetics ; DNA Topoisomerases, Type I/physiology ; DNA, Complementary/genetics ; DNA, Viral/biosynthesis ; DNA, Viral/genetics ; Genes, Reporter ; HIV-1/genetics ; HIV-1/physiology ; HeLa Cells/virology ; Humans ; Kidney/cytology ; Kidney/embryology ; Luciferases/analysis ; Luciferases/genetics ; Molecular Sequence Data ; Proviruses/genetics ; Recombinant Fusion Proteins/physiology ; Sequence Alignment ; Sequence Homology, Amino Acid ; Species Specificity ; Transfection ; Vero Cells/virology ; Virus Cultivation ; Virus Replication
    Chemical Substances Codon ; DNA, Complementary ; DNA, Viral ; Recombinant Fusion Proteins ; Luciferases (EC 1.13.12.-) ; DNA Topoisomerases, Type I (EC 5.99.1.2)
    Language English
    Publishing date 2003-07-08
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1430827100
    Database MEDical Literature Analysis and Retrieval System OnLINE

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