ISHINO Masaho

写真a

Affiliation

School of Medicine, Department of Innovative Medical IP Management

Job title

Professor

Education 【 display / non-display

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    1988

    Sapporo Medical University  

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    1988

    Sapporo Medical University  

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    1984

    Hokkaido University  

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    1984

    Hokkaido University  

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    1982

    Hokkaido University  

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Degree 【 display / non-display

  • Ph.D.

Professional Memberships 【 display / non-display

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    Japanese Biochemical Society

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    Molecular Biology Society of Japan

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    JAPAN SOCIETY FOR INTELLECTUAL PRODUCTION

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    Intellectual Property Association of Japan

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    THE JAPANESE SOCIETY FOR REGENERATIVE MEDICINE

Affiliation 【 display / non-display

  • Sapporo Medical University   School of Medicine, Dept.of Hygiene   Associate Professor  

 

Misc 【 display / non-display

  • Adenovirus E4orf6 targets pp32/LANP to control the fate of ARE-containing mRNAs by perturbing the CRM1-dependent mechanism

    F Higashino, M Aoyagi, A Takahashi, M Ishino, M Taoka, T Isobe, M Kobayashi, Y Totsuka, T Kohgo, M Shindoh

    JOURNAL OF CELL BIOLOGY ( ROCKEFELLER UNIV PRESS )  170 ( 1 ) 15 - 20  2005.07

     View Summary

    E4orf6 plays an important role in the transportation of cellular and viral mRNAs and is known as an oncogene product of adenovirus. Here, we show that E4orf6 interacts with pp32/leucine-rich acidic nuclear protein ( LANP). E4orf6 exports pp32/LANP from the nucleus to the cytoplasm with its binding partner, HuR, which binds to an AU-rich element ( ARE) present within many protooncogene and cytokine mRNAs. We found that ARE-mRNAs, such as c-fos, c-myc, and cyclooxygenase-2, were also exported to and stabilized in the cytoplasm of E4orf6-expressing cells. The oncodomain of E4orf6 was necessary for both binding to pp32/LANP and effect for ARE-mRNA. C-fos mRNA was exported together with E4orf6, E1B-55kD, pp32/LANP, and HuR proteins. Moreover, inhibition of the CRM1-dependent export pathway failed to block the export of ARE-mRNAs mediated by E4orf6. Thus, E4orf6 interacts with pp32/LANP to modulate the fate of ARE-mRNAs by altering the CRM1-dependent export pathway.

    DOI PubMed CiNii

  • Analysis of the prevalence of tetracycline resistance genes in clinical isolates of Enterococcus faecalis and Enterococcus faecium in a Japanese hospital

    Yutaka Nishimoto, Nobumichi Kobayashi, Mohammed Mahbub Alam, Masaho Ishino, Nobuyuki Uehara, Naoki Watanabe

    Microbial Drug Resistance   11 ( 2 ) 146 - 153  2005.06

     View Summary

    Prevalence of seven tetracycline resistance (TCR) genes-tet(L), tet(M), tet(K), tet(O), tet(S), tef(T), and tet(U)-which are known to be distributed to gram-positive cocci was analyzed for 224 Enterococcus faecalis and 46 Enterococcus faecium clinical isolates obtained in a Japanese hospital. Any of the TCR genes was detected in 75.9% of all the enterococcal strains. The tet(M) was detected at highest rates in both E. faecalis (75.0%) and E. faecium (69.6%), followed by tet(L), which was harbored in 6.7% of E. faecalis isolates and 30.4% of E. faecium isolates. The tet(O), tet(S), and tet(T) were detected in E. faecalis at low frequencies mostly associated with tet(M), while tet(K) and tet(U) were not detected. Nucleotide sequences of tet(S) from E. faecalis strains were identical to that reported in Listeria monocytogenes. Sequences of tet(O) from two E. faecalis strains were almost identical to each other and also to those from Streptococcus pneumoniae, Streptococcus pyogenes, Streptococcus mutans, Campylobacter jejuni, and Campylobacter coli, although minor sequence divergence was observed. The tet(T), which had been reported only in Streptococcus pyogenes, was found in five E. faecalis strains. Sequence of the enterococcal tet(T) differed from that of S. pyogenes by only four nucleotides (four amino acids) and showed high sequence identity (99.8%, amino acid level). Enterococcal strains with any one TC R gene or those with two TCR genes showed generally similar MICs of tetracyclines, and no evident difference in resistance level was observed.

    DOI PubMed

  • Comparison of NSP4 protein between group A and B human rotaviruses: detection of novel diarrhea-causing sequences in group B NSP4.

    Arch Virol    2005

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    Patent   58   44 - 49  2005

  • Genetic analysis of group B human rotaviruses detected in Bangladesh in 2000 and 2001

    MU Ahmed, N Kobayashi, M Wakuda, T Sanekata, K Taniguchi, A Kader, TN Naik, M Ishino, MM Alam, K Kojima, K Mise, A Sumi

    JOURNAL OF MEDICAL VIROLOGY ( WILEY-BLACKWELL )  72 ( 1 ) 149 - 155  2004.01

     View Summary

    Group B rotaviruses detected in Bangladesh in 2000 and 2001 were analyzed genetically to clarify relatedness to human group B rotaviruses reported previously in China and India, and to animal group B rotaviruses. VP7 gene sequences of the Bangladeshi group B rotaviruses (Bang373, Bang544, Bang334, and Bang402) were almost identical to each other and also showed high sequence identity to the Indian strain CAL-1 (98%) and Chinese strain adult diarrhea rotavirus (ADRV) (92%), while identities to bovine and murine viruses were considerably low (60-63%). Other genes of Bang373 and Bang544 encoding VP2, VP4, VP6, and NSP1 similar to NSP5 also showed much higher sequence identities to those of CAL-1 (97.7-99.4%) than to those of ADRV (89.9-93.9%). Characterization of nucleotide substitutions among Bang373, CAL-1, and ADRV suggested that all the gene segments might have evolved neutrally at similar mutation rates, while some of the gene segments (e.g., VP2 gene) were suggested to be more conserved than others. In conclusion, group B rotaviruses detected in Bangladesh represented by Bang373 and the Indian virus CAL-1 were considered as virtually identical viruses which are distinct genetically from ADRV, and it was suggested that Bang373 (CAL-1)-like group B rotavirus (Bengali strains) might be distributed primarily in an area around the Bay of Bengal.

    DOI

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Awards 【 display / non-display

  • Kurozumi Medical Foundation

    1997  

  • The Akiyama Foundation

    1996