KINDAI UNIVERSITY


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TAGUCHI Yoshitomo

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FacultyDepartment of Genetic Engineering / Graduate School of Biology-Oriented Science and Technology
PositionAssociate Professor
Degree
Commentator Guidehttps://www.kindai.ac.jp/meikan/779-taguchi-yoshitomo.html
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Last Updated :2020/09/02

Education and Career

Education

  •  - 1997 , Kyoto University, Graduate School, Division of Agriculture
  •  - 1992 , Kyoto University, Faculty of Agriculture
  •  - 1992 , Kyoto University, Faculty of Agriculture

Academic & Professional Experience

  •   2019 ,  - 現在, Associate Professor, Dept. Genetic Engineering, Kindai Univ.
  •   2003 ,  - 2019 , Lecturer, Dept. Genetic Engineering, Kindai Univ.
  •   1998 ,  - 2003 , Assistant Professor, Dept. Genetic Engineering, Kindai Univ.
  •   1997 ,  - 1998 , Reseach Associate, Japan Society for the Promotion of Science

Research Activities

Research Areas

  • Life sciences, Applied biochemistry
  • Life sciences, Molecular biology

Research Interests

  • Molecular Biology, Applied Microbiochemistry and Applied Biochemistry

Published Papers

  • In Vitro Culture of Single Bovine Embryos with Microwell Plates Made of Poly(dimethylsiloxane) Cured under Low Pressure, IWAMOTO Daisaku, KATO Nobuhiro, TANIGUCHI Shunji, TAGUCHI Yoshitomo, KISHI Masao, SAEKI Kazuhiro, International Journal of Biomaterials, International Journal of Biomaterials, 2018(7546986), 1 - 7, Jun. 2018 , Refereed
  • Molecular cloning and expression analysis of Bovine alpha-tocopherol transfer protein (a-TTP), TAGUCHI Yoshitomo, KOMATSU-TANAKA Mari, HIROSE Norie, KAJI Yurie, SAEKI Kazuhiro, Annual Research & Review in Biology, Annual Research & Review in Biology, 12(5), 1 - 7, May 2017 , Refereed
  • Functional expression of a Delta 12 fatty acid desaturase gene from spinach in transgenic pigs, K Saeki, K Matsumoto, M Kinoshita, Suzuki, I, Y Tasaka, K Kano, Y Taguchi, K Mikami, M Hirabayashi, N Kashiwazaki, Y Hosoi, N Murata, A Iritani, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 101(17), 6361 - 6366, Apr. 2004
    Summary:Linoleic acid (18:2n-6) and a-linolenic acid (18:3n-3) are polyunsaturated fatty acids that are essential for mammalian nutrition, because mammals lack the desaturases required for synthesis of Delta12 (n-6) and n-3 fatty acids. Many plants can synthesize these fatty acids and, therefore, to examine the effects of a plant desaturase in mammals, we generated transgenic pigs that carried the fatty acid desaturation 2 gene for a Delta12 fatty acid desaturase from spinach. Levels of linoleic acid (18:2n-6) in adipocytes that had differentiated in vitro from cells derived from the transgenic pigs were approximate to10 times higher than those from wild-type pigs. In addition, the white adipose tissue of transgenic pigs contained approximate to20% more linoleic acid (18:2n-6) than that of wild-type pigs. These results demonstrate the functional expression of a plant gene for a fatty acid desaturase in mammals, opening up the possibility of modifying the fatty acid composition of products from domestic animals by transgenic technology, using plant genes for fatty acid desaturases.
  • Functional analysis of MRP1 cloned from bovine 「共著」, TAGUCHI Yoshitomo, SAEKI Kazuhiro, KOMANO Tohru, FEBS Letters, FEBS Letters, 521, 211-213, 2002
  • Non-equivalent cooperation between the two nucleotide-binding folds of P-glycoprotein, Y Takeda, K Yamada, Y Taguchi, K Kino, M Matsuo, SJ Tucker, T Komano, T Amachi, K Ueda, BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 1373(1), 131 - 136, Aug. 1998
    Summary:To identify the roles of the two nucleotide-binding folds (NBFs) in the function of human P-glycoprotein, a multidrug transporter, we mutated the key lysine residues to methionines and the cysteine residues to alanines in the Walker A (W-A) motifs (the core consensus sequence) in the NBFs. We examined the effects of these mutations on N-ethylmaleimide (NEM) and ATP binding, as well as on the vanadate-induced nucleotide trapping with 8-azido-[alpha-P-32]ATP, Mutation of the W-A lysine or NEM binding cysteine in either of the NBFs blocked vanadate-induced nucleotide trapping of P-glycoprotein. These results suggest that if one NBF is non-functional, there is no ATP hydrolysis even if the other functional NBF contains a bound nucleotide, further indicating the strong cooperation between the two NBFs of P-glycoprotein. However, we found that the effect of NEM modification at one NBF on ATP binding ar the other NBF was not equivalent, suggesting a non-equivalency of the role of the two NBFs in P-glycoprotein function. (C) 1998 Elsevier Science B.V. All rights reserved.
  • Alteration of substrate specificity by mutations at the His(61) position in predicted transmembrane domain 1 of human MDR1/P-glycoprotein, Y Taguchi, K Kino, M Morishima, T Komano, SE Kane, K Ueda, BIOCHEMISTRY, BIOCHEMISTRY, 36(29), 8883 - 8889, Jul. 1997
    Summary:In CFTR, a member of the ABC superfamily and a chloride channel, amino acid substitutions in its transmembrane domains 1 and 6 (TM1, TM6) have been reported to modulate the anion selectivity or ion conductance of the ion channel. In P-glycoprotein, no amino acid substitution in TM1, but some in TM6, have been reported to modify the substrate specificity of this protein. In this work, we demonstrated the involvement of His(61), which is in the middle of the predicted TM1, in the function of P-glycoprotein. His(61) was replaced by all other amino acid residues, and each of the mutant cDNAs was introduced into drug-sensitive human carcinoma cells, KB3-1. The drug-resistance profile of cells stably expressing each mutated P-glycoprotein was investigated by comparing their relative resistance to vinblastine, colchicine, VP16, and adriamycin. The resistance to vinblastine was increased by replacing His(61) by amino acids with smaller side chains, while it was lowered by replacing by amino acids with bulkier side chains. The reverse effect was observed for resistance to colchicine and VP16. The resistance to adriamycin was increased by replacing by amino acids with bulkier side chains except Lys or Arg, which have a basic side chain. We also showed that the replacement of His(61) by Phe and Lys greatly impaired the efflux of calcein AM, while the replacement had no effect on the efflux of rhodamine 123. These results suggest that an amino acid residue at position 61 in TM1 is important in deciding the substrate specificity of P-glycoprotein.
  • How does P-glycoprotein recognize its substrates?, K Ueda, Y Taguchi, M Morishima, SEMINARS IN CANCER BIOLOGY, SEMINARS IN CANCER BIOLOGY, 8(3), 151 - 159, Jun. 1997
    Summary:We review how P-glycoprotein recognizes a wide variety of compounds and how it carries its substrates across membranes. Amino acid substitutions that affect the substrate specificity of P-glycoprotein have been found scattered throughout the molecule. In particular, some amino acid residues in the putative transmembrane domain (TM)1 together with TM5-6 and TM11-12 may help to govern substrate specificity. The features that substrates for P-glycoprotein share are also discussed. The amphipathy of a substrate may decide whether the substrate can be intercalated into the lipid bilayer of the membrane. In addition, only certain molecular volumes and tertiary structures may mab it possible for the substrate to fit into the substrate-binding site(s) of P-glycoprotein.
  • Anti-cancer drugs and glutathione stimulate vanadate-induced trapping of nudeotide in multidrug resistance-associated protein(MRP)「共著」, TAGUCHI Y, YOSHIDA A, TAKADA Y, KOMANO T, UEDA K, FEBS Letters, FEBS Letters, 401(1), 11 - 14, 1997
  • Amio acid substitution in the first transmembrane domain(TM1)of P-glycoprotein that alter substrate specificity「共著」, TAGUCHI Y, MORISHIMA M, KOMANO T, UEDA K, FEBS Letters, FEBS Letters, 413(1), 142 - 146, 1997
  • Aureobasidin A, an antifungal cyclic depsipeptide antibiotic, is a substrate for both human MDR1 and MDR2/P-glycoproteins, K Kino, Y Taguchi, K Yamada, T Komano, K Ueda, FEBS LETTERS, FEBS LETTERS, 399(1-2), 29 - 32, Dec. 1996
    Summary:The human MDR1 gene encodes the multidrug transporter P-glycoprotein (Pgp). Although the MDR2/Pgp shares about 80% identity at the amino acid level with the MDR1/Pgp, the MDR2/Pgp cannot act as a multidrug transporter. We examined the drug sensitivity of Saccharomyces cerevisiae expressing either the human MDR1/Pgp or MDR2/Pgp. The human MDR1/Pgp conferred about 4-fold resistance to aureobasidin A, a cyclic depsipeptide antifungal antibiotic, on the drug-sensitive yeast strains. Interestingly the human MDR2/Pgp also conferred about 2.5-fold resistance to aureobasidin A. The resistance to aureobasidin A conferred by the MDR2/Pgp as well as by the MDR1/Pgp was overcome by vinblastine, verapamil, and cyclosporin A, depending on their concentrations, but not by colchicine. Aureobasidin A probably interacts directly with Pgps, because it overcame multidrug resistance of human cells and inhibited azidopine photoaffinity labeling of MDR1/Pgp in human cell membranes. These results suggest the possibility that the human MDR1 and MDR2/Pgps have conserved domain(s) for drug recognition.
  • Aureobasidin A, an antifungal cyclic depsipeptide antibiotic, is a substrate for both human MDR1 and MDR2/P-glycoproteins, Ueda, K, Taguchi, Y, Yamada, K, Kino, K, Komano, T, Proceedings of the American Association for Cancer Research Annual Meeting (Washington D.C., USA), Proceedings of the American Association for Cancer Research Annual Meeting (Washington D.C., USA), 37, 327, Apr. 1996 , Refereed
  • A dnaA box functionally substitute for the priming signals in the ┣DBoriV(/)-┫DB of the broad host-range plasmid RSF1010「共著」, TAGUCHI Y, TANAKA K, HONDA Y, MIAO D‐M, SAKAI H, KOMANO T, BAGDASARIAN M, FEBS Letters, FEBS Letters, 388(2/3), 169 - 172, 1996
  • Functional features of ┣DBorivV(/)-┫DB of the broad host range plasmid RSF1010 in ┣DBPseudomonas(/)-┫DB ┣DBaeruginosa(/)-┫DB「共著」, HIGASHI A, SAKAI H, HONDA Y, TANAKA K, MIAO D‐M, NAKAMURA T, TAGUCHI Y, KOMANO T, BAGDASARIAN M, PLASMID, PLASMID, 31(2), 196 - 200, 1994
  • Functional difference between the two oppositely oriented priming signals essential for the initiation of the broad host-range plasmid RSF1010 DNA replication「共著」, TANAKA K, KINO K, TAGUCHI Y, MIAO D‐M, HONDA Y, SAKAI H, KOMANO T, BAGDASARIAN M, Nucleic Acids Reseach, Nucleic Acids Reseach, 22(5), 767 - 772, 1994
  • Mutational analysis of specific priming signal essential for DNA replication of the broad host-range plasmid RSF1010「共著」, HONDA Y, AKIOKA T, TAKEBE S, TANAKA K, MIAO D, HIGASHI A, NAKAMURA T, TAGUCHI Y, BAGDASARIAN M, FEBS Letters, FEBS Letters, 324(1), 67 - 70, 1993
  • A base-paired hairpin structure essential for the functional priming signal for DNA replication of the broad host range plasmid RSF1010「共著」, MIAO D‐M, HONDA Y, TANAKA K, HIGASHI A, NAKAMURA T, TAGUCHI Y, SAKAI H, KOMANO T, BAGDASARIAN M, Nucleic Acids Reseach, Nucleic Acids Reseach, 21(21), 4900 - 4903, 1993
  • Peroxiredoxin as a functional endogenous antioxidant enzyme in pronuclei of mouse zygotes, Kohtaro Morita, Mikiko Tokoro, Yuki Hatanaka, Chika Higuchi, Haruka Ikegami, Kouhei Nagai, Masayuki Anzai, Hiromi Kato, Tasuku Mitani, Yoshitomo Taguchi, Kazuo Yamagata, Yoshihiko Hosoi, Kei Miyamoto, Kazuya Matsumoto, Journal of Reproduction and Development, Journal of Reproduction and Development, 64(2), 161 - 171, 2018 , Refereed
    Summary:Antioxidant mechanisms to adequately moderate levels of endogenous reactive oxygen species (ROS) are important for oocytes and embryos to obtain and maintain developmental competence, respectively. Immediately after fertilization, ROS levels in zygotes are elevated but the antioxidant mechanisms during the maternal-to-zygotic transition (MZT) are not well understood. First, we identified peroxiredoxin 1 (PRDX1) and PRDX2 by proteomics analysis as two of the most abundant endogenous antioxidant enzymes eliminating hydrogen peroxide (H2O2). We here report the cellular localization of hyperoxidized PRDX and its involvement in the antioxidant mechanisms of freshly fertilized oocytes. Treatment of zygotes at the pronuclear stage with H2O2 enhanced pronuclear localization of hyperoxidized PRDX in zygotes and concurrently impaired the generation of 5-hydroxymethylcytosine (5hmC) on the male genome, which is an epigenetic reprogramming event that occurs at the pronuclear stage. Thus, our results suggest that endogenous PRDX is involved in antioxidant mechanisms and epigenetic reprogramming during MZT.
  • Application of laser-assisted zona drilling to in vitro fertilization of cryopreserved mouse oocytes with spermatozoa from a subfertile transgenic mouse, Masayuki Anzai, Megumi Nishiwak, Miho Yanagi, Tatsuyuki Nakashima, Takehito Kaneko, Yoshitomo Taguchi, Mikiko Tokoro, Seung-Wook Shin, Tasuku Mitani, Hiromi Kato, Kazuya Matsumoto, Naomi Nakagata, Akira Iritani, JOURNAL OF REPRODUCTION AND DEVELOPMENT, JOURNAL OF REPRODUCTION AND DEVELOPMENT, 52(5), 601 - 606, Oct. 2006
    Summary:Development of assisted reproductive technologies is necessary to obtain fertilized oocytes in a subfertile transgenic mouse strain. Here, we showed the application of laser-assisted drilling of the zona pellucida to in vitro fertilization of cryopreserved mouse oocytes with sperm from subfertile transgenic mice (C57BL/6N-Tg(UCP/FAD2)U8 strain). After cryopreservation by vitrification, the recovery and survival rates of the zona-drilled mouse oocytes were 97% (97/100) and 94% (91/97), respectively. In vitro fertilization of the cryopreserved zona-drilled mouse oocytes with sperm from the subfertile transgenic mice was greatly facilitated (60%, 55/91) compared to that of the cryopreserved zona-intact mouse oocytes (11%, 81/768). In vitro fertilized embryos that developed to the 2-cell stage were again cryopreserved by vitrification, and after warming they were transferred into recipient females. Subsequently, six viable offspring were delivered, and all were confirmed to be transgenic mice. These results indicate that laser-assisted zona drilling of oocytes combined with cryopreservation by vitrification may be a useful approach for large-scale production of in vitro fertilized embryos for managing transgenic mouse strains with reproductive disabilities such as subfertile sperm.

Books etc

  • How do P-glycoprotein and other ABC proteins recognize their substrates? (共著), 「Control and diseases of sodium dependent transport Proteins and ion channels」Elsevier Science B.V.,   2000
  • Multidurg resistance in cancer cells. (分担題名 : Role of P-glycoprotein in the transport of hormones and peptides. )「共著」, John Wiley & Sons Ltd.,   1996

Conference Activities & Talks

  • Interactions of mechanisms between lipid transporter ABCA1 and α1-syntrophin or α-TTP, Yurie Kaji, Shiho Taniguchi, Kana Fujibayasi, Naoki Sugimoto, Kazuhiro Saeki, Yoshitomo Taguchi, The 2018 Annual Meeting of JSBBA,   2018 03
  • Mechanisms for interactions between cholesterol efflux protein ABCA1 and cytoplasmic proteins modulating its stability (α1-syntrophin) and transport activity (α-TTP)., Yurie Kaji, Kana Fujibayasi, Shiho Taniguchi, Naoki Sugimoto, Kazuhiro Saeki, Yoshitomo Taguchi, 7th FEBS Special Meeting on ABC proteins "From Multidrug Resistance to Genetic Diseases",   2018 03
  • Expressional induction of Bcrp1 in mouse embryonic stem cells by oxidative stress, ConBio2017,   2017 12
  • Mechanisms for interactions between cholesterol efflux protein ABCA1 and cytoplasmic proteins modulating its transport activity(α-TTP) and stability(α1-syntrophin), Yurie Kaji, Kana Fujibayasi, Shiho Taniguchi, Naoki Sugimoto, Kazuhiro Saeki, Yoshitomo Taguchi, ConBio2017,   2017 12
  • Analysis for mechanisms of interactions between lipid transporter ABCA1 and its functional modulator proteins, Yurie KAJI, Kana FUJIBAYASHI, Kazuhiro SAEKI, Yoshitomo TAGUCHI,   2017 03
  • Screening for proteins which interact with anti-cancer drug transporter BCRP1 (ABCG2) in mouse embryonic stem cells, Tomohiro OKASAKO, Ryunosuke AOKI, Yurie KAJI, Yuka NISHIGAITO, Moe KUWAYAMA, Yuuki SAKATE, Miki KOUDA, Nao ARITA, Motoki YOSHIDA, Takeshi MATSUI, Munehiro OKUDA, Kazuhiro SAEKI, Tasuku MITANI, Yoshitomo TAGUCHI,   2017 03
  • Functional interactions between vitamin E binding protein α-TTP and ABC proteins involved in lipid transport., Yoshitomo Taguchi, Michihiro Nagoshi, Mari Tanaka, Norie Hirose, Keisuke Komatsu, Yuuta Nagano, Ryuhei Ogawa, Kanako Kishi, Tatsuro Shirata, Kazuhiro Saeki, 5th FEBS Special Meeting on ABC proteins "From Multidrug Resistance to Genetic Disease",   2014 03
  • Transcriptional regulation of Bcrp1 mRNA splice-variants in mouse embryonic stem cells,   2012 12
  • Analysis for the differences between the two isoforms of Ca2+-dependent phoshatidylserine-binding protein annexinA5.,   2012 12
  • Mutations of the amino acid residues which are different between two isoforms of bovine Annexin A5,   2011 12
  • Transcriptional regulation of Bcrp1 mRNA splice-variants in mouse embryonic stem cells,   2011 12
  • Expressional and functional analysis of bovine α-tocopherol transfer protein (α-TTP),   2011 12
  • Analysis for expression and functions of Vitamin E binding protein α-TTP (α-tocopherol transfer protein),   2011 03
  • Mechansims for substrate recognition and transport of anti-cancer drug transporter MRP1 (ABCC1),   2011
  • Amino acids in MSD0 and L0 domain determine the substrate specificity of MRP1 (ABCC1),   2011
  • Molecular clonig and functional analysis of bvine α-tocopherol transfer protein(α-TTP),   2010 12
  • Mutational analysis of Met98 and Arg309 of xenobiotics transporter ABCC1(MRP1) cloned from bovine,   2010 03
  • Alterations of Substrate Specificity by Mutations at the Met98 in TMD0 and at Arg309 in L0 of Bovine MRP1 (ABCC1), 3rd FEBS Special Meeting “ATP-Binding Cassette Proteins" (ABC2010),   2010 03 , 3rd FEBS Special Meeting “ATP-Binding Cassette Proteins" (ABC2010)
  • Mutational analysis of Met98 and Arg309 of xenobiotics transporter ABCC1(MRP1) cloned from bovine,   2009 12
  • Molecular cloning of cDNA for α-tocopherol transfer protein (α-TTP) from bovine,   2009 03
  • Functional analysis of MSD0 of anti-cancer drug transporter ABCC1 (MRP1),   2009 03
  • Mutational analysis for MSD0 and L0 domain of anti-cancer drug resistance protein ABCC1 (MRP1),   2008 12
  • Functional analysis of N-end domain of xenobiotics transporter MRP1 (ABCC1),   2008 03
  • Funcitonal analysis of xenobiotics transporter MRP1 (ABCC1) cloned from bovine,   2007 12
  • Identification of functional domain of xenobiotics transporter MRP1 by site-directed mutagenesis,   2006 12
  • Molecular cloning and expression analysis of new genes encoding ABC transporters from streptomyces producing actionmycin D,   2006 03
  • Functional analysis of anti-cancer drug transporter MRP1 by comparison between bovine and human MRP1 orthologs,   2006 03
  • Functional analysis of xenobiotics transporter MRP1 by site-directed mutagenesis,   2005 12
  • Molecular cloning of new genes encoding ABC transporters from streptomyces producing an anti-cancer drug,   2005 12
  • Molecular cloning and functional analysis of genes encoding proteins interacted with vitamin E,   2005 08
  • Mutational analysis for functional domains of anti-cancer drug transprter MRP1,   2005 08
  • Identification of putative transporter genes from anti-cancer drug producing microorganism,   2005 08
  • Identification of new genes encoding ABC proteins from Stereptomyces producing actinomycinD,   2005 06
  • Functional analysis of xenobiotics transporter MRP1,   2004 09
    Summary:Multidrug resistance protein 1 (MRP1), a member of the ATP-binding cassette (ABC) family of membrane transport proteins, functions as an energy-dependent efflux pump that extrudes many kinds of xenobiotics out of cells. In order to identify the domains involving recognition and transport of substrates of MRP1, we replace several non-conserved amino acids in bovine MRP1 by corresponding ones of the human ortholog by site-directed mutagenesis, and examine whether the amino acid substitutions alter the substrate specificity of bovine MRP1.
  • Cloning and characterization of the ostrich growth hormone?encoding gene,   2002 10
  • Molecular cloning and functional analysis of bovine MRP1,   2002 06
  • Functional characterization of bovine MRP1,   2002 03
  • Molecular cloning and functional analysis of bovine MRP1,   2001 12
  • Functional analysis of anti cancer drug transporter MRP1 in mammary gland,   2001 05
  • Molecular cloning of bovine MRP1 cDNA,   2001 03

Misc

  • Cloning of novel ABC transporter genes from Streptomyces producing anti-cancer drug, actinomycin D, Memoirs of Faculty of Biology Oriented Science and Technology, Kinki University, 24, 19, 25,   2009 09
  • Alteration of Substrate Specificity by Mutation at the Gln1088 Position of Bovine MRP1 (ABCC1), Memoirs of Biology-Oriented Science and Technology, Kinki University, 20, 13, 20,   2007 09
  • Xenobiotics transporter MRP1 (Multidrug Resistance Protein 1) cloned from bovine - Comparison of its expression, structure and functions with human and mouse MRP1, Memoirs of The School of B.O.S.T. of Kinki University, 15, 21, 26,   2005 03

Research Grants & Projects

  • Analysis of molecular mechanisms for drug resistance of cancer cells
  • Analysis of molecular mechanisms for lactational transfer of xenobiotics
  • Analysis of mechanisms for substrate recognition and transport of anti-cancer drug transporters, P-glycoprotein and MRP.
  • Analysis of molecular mechanisms for lactational transfer of xenobiotics.