Updated on 2024/02/15

写真b

 
MASHIMA Keisuke
 
*Items subject to periodic update by Rikkyo University (The rest are reprinted from information registered on researchmap.)
Affiliation*
College of Science Department of Life Science
Graduate School of Science Doctoral Program in Life Science
Graduate School of Science Master's Program in Life Science
Title*
Professor
Degree
理学博士 / 理学博士 ( 大阪大学 )
Contact information
Mail Address
Research Theme*
  • 細胞内情報伝達機構の分子的側面の解析を研究テーマとする。免疫細胞を中心に細胞の分化・活性化などを誘導するリン酸化チロシンを介した情報の伝達機構を明らかにするため、チロシン残基のリン酸化に関与するタンパク質チロシンリン酸化酵素(PTK)とタンパク質チロシン脱リン酸化酵素(PTP)について研究している。

  • Research Interests
  • リン酸化・脱リン酸化

  • signal transduction

  • Protein tyrosine phosphatase

  • Campus Career*
    • 4 2010 - Present 
      College of Science   Department of Life Science   Professor
    • 4 2010 - Present 
      Graduate School of Science   Master's Program in Life Science   Professor
    • 4 2010 - Present 
      Graduate School of Science   Doctoral Program in Life Science   Professor
    • 4 2007 - 3 2010 
      College of Science   Department of Life Science   Associate Professor
    • 4 2007 - 3 2010 
      Graduate School of Science   Master's Program in Life Science   Associate Professor
    • 4 2007 - 3 2010 
      Graduate School of Science   Doctoral Program in Life Science   Associate Professor
    • 4 2002 - 3 2007 
      College of Science   Department of Life Science   Associate Professor (as old post name)
    • 4 2005 - 3 2007 
      Graduate School of Science   Master's Program in Life Science   Associate Professor (as old post name)
    • 4 2005 - 3 2007 
      Graduate School of Science   Doctoral Program in Life Science   Associate Professor (as old post name)
    • 4 2003 - 3 2004 
      Graduate School of Science   Doctoral Program in Life Science   Associate Professor (as old post name)
    • 4 1997 - 3 2002 
      College of Science   Department of Chemistry   Associate Professor (as old post name)
    • 4 1995 - 3 1997 
      College of Science   Department of Chemistry   Lecturer
    • 4 1989 - 3 1995 
      College of Science   Department of Chemistry   Full-time Research Assistant

    ▼display all

     

    Research Areas

    • Life Science / Immunology

    • Life Science / Functional biochemistry

    Research History

    • 4 2010 - Present 
      RIKKYO UNIVERSITY   Graduate School of Science Field of Study: Life Science   Professor

      More details

    • 4 2010 - Present 
      RIKKYO UNIVERSITY   Graduate School of Science Field of Study: Life Science   Professor

      More details

    • 4 2010 - Present 
      RIKKYO UNIVERSITY   College of Science Department of Life Science   Professor

      More details

    • 4 2007 - 3 2010 
      RIKKYO UNIVERSITY   College of Science Department of Life Science   Associate Professor

      More details

    • 4 2002 - 3 2007 
      RIKKYO UNIVERSITY   College of Science Department of Life Science   Associate Professor (as old post name)

      More details

    • 4 1997 - 3 2002 
      RIKKYO UNIVERSITY   College of Science Department of Chemistry   Associate Professor (as old post name)

      More details

    • 4 1995 - 3 1997 
      RIKKYO UNIVERSITY   College of Science Department of Chemistry   Lecturer

      More details

    • 4 1989 - 3 1995 
      RIKKYO UNIVERSITY   College of Science Department of Chemistry   Full-time Research Assistant

      More details

    • 6 1987 - 6 1988 
      岡崎国立共同研究機構・基礎生物学研究所   講師(PD相当)

      More details

    ▼display all

    Education

    • - 3 1987 
      Osaka University   Graduate School, Division of Natural Science

      More details

      Country: Japan

      researchmap

    • - 3 1984 
      Osaka University   Graduate School, Division of Natural Science

      More details

      Country: Japan

      researchmap

    • - 3 1981 
      University of Tsukuba   Second Cluster of College

      More details

      Country: Japan

      researchmap

    Papers

    • Muscarinic receptor stimulation induces TASK1 channel endocytosis through a PKC-Pyk2-Src pathway in PC12 cells. Peer-reviewed

      Matsuoka, H, Harada, K, Mashima, K, Inoue, M

      Cellular signaling65   109434   2020

      More details

      Language:English   Publishing type:Research paper (scientific journal)  

      researchmap

    • Mechanistic Insights into the Activation of Soluble Guanylate Cyclase by Carbon Monoxide: A Multi-Step Mechanism Proposed for the BAY 41-2272-Induced Formation of 5-Coordinate CO‒Heme. Peer-reviewed International journal

      Makino, R, Obata, Y, Tsubaki, M, Iizuka, T, Hamajima, Y, Kato-Yamada, Y, Mashima, K, Shiro, Y

      Biochemistry57 ( 10 ) 1620 - 1631   2018

      More details

      Language:English   Publishing type:Research paper (scientific journal)  

      Soluble guanylate cyclase (sGC) is a heme-containing enzyme that catalyzes cGMP production upon sensing NO. While the CO adduct, sGC-CO, is much less active, the allosteric regulator BAY 41-2272 stimulates the cGMP productivity to the same extent as that of sGC-NO. The stimulatory effect has been thought to be likely associated with Fe-His bond cleavage leading to 5-coordinate CO-heme, but the detailed mechanism remains unresolved. In this study, we examined the mechanism under the condition including BAY 41-2272, 2'-deoxy-3'-GMP and foscarnet. The addition of these effectors caused the original 6-coordinate CO-heme to convert to an end product that was an equimolar mixture of a 5- and a new 6-coordinate CO-heme, as assessed by IR spectral measurements. The two types of CO-hemes in the end product were further confirmed by CO dissociation kinetics. Stopped-flow measurements under the condition indicated that the ferrous sGC bound CO as two reversible steps, where the primary step was assigned to the full conversion of the ferrous enzyme to the 6-coordinate CO-heme, and subsequently followed by the slower second step leading a partial conversion of the 6-coordinate CO-heme to the 5-coordinate CO-heme. The observed rates for both steps linearly depended on CO concentrations. The unexpected CO dependence of the rates in the second step supports a multistep mechanism, in which the 5-coordinate CO-heme is led by CO release from a putative bis-carbonyl intermediate that is likely provided by the binding of a second CO to the 6-coordinate CO-heme. This mechanism provides a new aspect on the activation of sGC by CO.

      DOI: 10.1021/acs.biochem.7b01240

      PubMed

      researchmap

    • The Initial O2 Inserting Step of Tryptophan Dioxygenase Reaction Proposed by a Heme-Modification Study. Peer-reviewed

      Makino, R, Obayashi, E, Hori, H, Iizuka, T, Mashima, K, Shiro, Y, Ishimura, Y

      Biochemistry54   3604 - 3616   2015

      More details

      Language:English  

      researchmap

    • Protein tyrosine phosphatase-PEST (PTP-PEST) regulates mast cell-activating signals in PTP activity-dependent and -independent manners. Peer-reviewed

      Motohashi, S, Koizumi, K, Honda, R, Maruyama, A, Palmer, E.F. H, Mashima, K

      Cell Immunol.287   128 - 134   2014

      More details

      Authorship:Corresponding author   Language:English   Publishing type:Research paper (scientific journal)  

      researchmap

    • Protein Phosphatase 1alpha Associates to Protein Tyrosine Phosphatase-PEST inducing dephosphorylation of phospho-Serine 39. Peer-reviewed

      Nakamura, K, Palmer, E.E.H, Ozawa, T, Mashima, K

          2010

      More details

      Authorship:Corresponding author   Language:English   Publishing type:Research paper (scientific journal)  

      researchmap

    • PICOT, protein kinase C -theta interacting protein, is a novel regulator of FcRI-mediated mast cell activation. Peer-reviewed

      Kato, N, Motohashi, S, Okada, T, Ozawa, T, Mashima, K

      Cell Immunol.251 ( 1 ) 62 - 67   2008

      More details

      Authorship:Corresponding author   Language:English   Publishing type:Research paper (scientific journal)  

      researchmap

    • Intracellular localization and domain organization of human TRIM41 proteins. Peer-reviewed

      Tanaka, M, Fukuda, Y, Mashima, K, Hanai, R

      Mol. Biol. Rep32   87 - 93   2005

      More details

      Language:English   Publishing type:Research paper (scientific journal)  

      researchmap

    • Leupaxin binds to PEST domain tyrosine phosphatases PEP. Peer-reviewed

      Watanabe, N, Ishizuka, H, Amano, N, Mashima, K

      Mol. Cell. Biochem.269   13 - 17   2005

      More details

      Authorship:Corresponding author   Language:English   Publishing type:Research paper (scientific journal)  

      researchmap

    • Gene expression profile in the livers of rats orally administered ethinylestradiol for 28 days using a microarray technique. Peer-reviewed

      Kato, N, Shibutani, M, Takagi, H, Uneyama, C, Lee, K-Y, Takigami, S, Mashima, K, Hirose, M

      Toxicology30   179 - 192   2004

      More details

      Language:English   Publishing type:Research paper (scientific journal)  

      researchmap

    • Characterization of two isoforms of a human DnaJ homologue, HSJ2. Peer-reviewed

      Ryo Hanai, Keisuke Mashima

      Mol. Biol. Rep.30   149 - 153   2003

      More details

      Language:English   Publishing type:Research paper (scientific journal)  

      researchmap

    • Requirement of PEST domain tyrosine phosphatase PEP in B cell antigen receptor-induced growth arrest and apoptosis Peer-reviewed

      Kiminori Hasegawa, Hiroaki Yajima, Tatsuo Katagiri, Mami Ogimoto, Yutaka Arimura, Katsuyuki Mitomo, Keisuke Mashima, Kazuya Mizuno, Hidetaka Yakura

      European Journal of Immunology29 ( 3 ) 887 - 896   1999

      More details

      Language:English   Publishing type:Research paper (scientific journal)   Publisher:Wiley-VCH Verlag  

      Signaling events leading to B cell growth or apoptosis are beginning to be unravelled, but detailed information is still lacking. To identify signaling molecules involved in B cell antigen receptor (BCR)-initiated pathways, we used the immature B cell line, WEHI-231, to investigate protein tyrosine phosphatases (PTP) whose expression was modulated by BCR ligation. Among the PTP cloned by reverse transcription-PCR, mRNA expression of the proline-, glutamic acid-, serine- and threonine-rich (PEST) domain phosphatase (PEP) was selectively elevated 3.1-fold within 3 h after anti-IgM antibody stimulation. In contrast, expression of another PEST domain phosphatase, PTP-PEST, was unaffected. Western blot analysis revealed that 71% of PEP was located in the cytosolic fraction, while 29% was in the membrane fraction. To examine the direct contribution made by PEP to BCR-initiated signal transduction, we transfected an antisense PEP cDNA into WEHI-231 cells. Two stable clones were established in which PEP expression was reduced by 34% and 47%, respectively. Strikingly, BCR-mediated inhibition of DNA synthesis was significantly rescued in the clones, and G1 phase cell cycle arrest and apoptosis were almost completely ablated. Considered collectively, these results indicate that PEP is a positive, crucial regulator in determining B cell fate triggered by BCR engagement.

      DOI: 10.1002/(SICI)1521-4141(199903)29:03<887::AID-IMMU887>3.0.CO;2-9

      Scopus

      PubMed

      researchmap

    • Antigen receptor‐initiated growth inhibition is blocked in CD45‐loss variants of a mature B lymphoma, with limited effects on apoptosis Peer-reviewed

      Mami Ogimoto, Tatsuo Katagiri, Keisuke Mashima, Kiminori Hasegawa, Kazuya Mizuno, Hidetaka Yakura

      European Journal of Immunology25 ( 8 ) 2265 - 2271   1995

      More details

      Language:English   Publishing type:Research paper (scientific journal)  

      Role of CD45 in B cell antigen receptor (BcR)‐mediated signaling events in mature B cells was examined using BAL‐17 and its CD45‐negative clones. In the CD45‐negative clones, BcR stimulation induced tyrosine phosphorylation almost identical to the parental cells, with a few exceptions of reduced phosphorylation, especially of a protein of about 60 kDa. BcR‐induced calcium responses were reduced in the CD45‐negative clones, but the kinetics were similar to the parent. BcR stimulation led to growth inhibition in the parental cells, but signals for growth inhibition were completely blocked in the CD45‐negative clones. Interestingly, the same stimulation induced low, but significant levels of apoptosis both in the parent and in the CD45‐negative clones. Thus, in mature BAL‐17 cells, CD45 subtly mediates early signaling events (tyrosine phosphorylation and Ca2+ mobilization), and is absolutely required for the signaling pathway leading to growth regulation, but has limited effects on apoptosis. Copyright © 1995 WILEY‐VCH Verlag GmbH &amp
      Co. KGaA, Weinheim

      DOI: 10.1002/eji.1830250823

      Scopus

      PubMed

      researchmap

    • Adhesion-inducible DNA synthesis regulated by tyrosine phosphorylation/dephosphorylation

      Keisuke Mashima, Yuriko Furuya

      Biochemical and Biophysical Research Communications214 ( 3 ) 856 - 860   1995

      More details

      Authorship:Lead author, Corresponding author   Language:English   Publishing type:Research paper (scientific journal)  

      Non-malignant rat liver epithelial cell line BRL was reported to adhere to a substrate by fibronectin. DNA synthesis of these cells was induced by adhesion to a substrate by fibronectin, while DNA synthesis in non-adhered cells was not observed. These results indicated that DNA synthesis in BRL cells is inducible by the cell adhesion signaling. Adhesion-inducible DNA synthesis was strongly inhibited by Herbimycin A. In contrast, vanadate showed the tendency to promote adhesion-inducible DNA synthesis. These results suggest that DNA synthesis caused by the cell adhesion in these cells was regulated by both phosphorylation and dephosphorylation at tyrosine residue. © 1995 by Academic Press, Inc.

      DOI: 10.1006/bbrc.1995.2365

      Scopus

      researchmap

    • 分子細胞生物学基礎実験法

      南江堂   424-439   4 1994

      More details

      Language:Japanese   Publishing type:Research paper (other academic)  

      researchmap

    • Alteration in protein-tyrosine phosphatase of rat epithelial cells by RSV-transformation: Application of phospho-tyrosyl glutamine synthetase to the study of protein-tyrosine phosphatase

      Keisuke Mashima, Youko Okajima, Junko Usui, Takeo Shimizu, Kinuko Kimura

      Journal of Biochemistry115 ( 2 ) 333 - 337   1994

      More details

      Authorship:Lead author, Corresponding author   Language:English   Publishing type:Research paper (scientific journal)   Publisher:Oxford University Press  

      We prepared phospho-tyrosyl glutamine synthetase (P-GS) with suppressed activity from a highly adenylylated glutamine synthetase and applied it to the assay of protein-tyrosine phosphatase (PTPase) present in non-malignant rat liver cells (BRL) by RSV-transformation. The maximum PTPase activity toward P-GS was observed at neutral pH (pH 7.5-8.0) in the soluble and particulate fractions prepared from both BRL and RSV-transformed (RSV-BRL) cells. At low activity levels (&lt
      about 0.3 U), the PTPase activity in each fraction was proportional to the sample protein concentration (A280) and the specific activity of PTPase in the soluble fraction of BRL cells was about twofold higher than that in the soluble fraction of BRL cells, while those in particulate fractions of BRL and RSV-BRL cells were almost the same as each other. Soluble fractions of BRL and RSV-BRL were subjected to molecular-sieve and anion-exchange chromatographies. One major PTPase activity, with an Mr of about 40, 000 (40k), was detected in the BRL soluble fraction, and two were detected in the RSV-BRL soluble fraction with Mrs of about 40k and 60k. The 40k PTPases in BRL and RSV-BRL had the same profiles on anion-exchange chromatography, but the 60k PTPase in RSV-BRL cells showed a different profile. We suggest that the RSV-transformation of BRL cells induced the appearance of the 60k PTPase in the soluble fraction. © 1994 BY THE JOURNAL OF BIOCHEMISTRY.

      DOI: 10.1093/oxfordjournals.jbchem.a124338

      Scopus

      PubMed

      researchmap

    • Negative regulation of apoptotic death in immature B cells by CD45 Peer-reviewed

      Mami Ogimoto, Tatsuo Katagiri, Keisuke Mashima, Kiminori Hasegawa, Kazuya Mizuno, Hidetaka Yakura

      Int. Immunology6   647 - 654   1 1 1994

      More details

      Language:English   Publishing type:Research paper (scientific journal)  

      researchmap

    • 遺伝子のクローニング

      眞島 恵介

      堀尾武一 分子細胞生物学基礎実験法 南江堂   424 - 439   1 1 1994

      More details

      Language:Japanese   Publishing type:Research paper (other academic)  

      researchmap

    • Changes in cell attachment by RSV-transforma-tion in rat epithelial cells

      Keisuke Mashima, Junko Mizuguchi

      Biochem. Biophys. Res. Commun.189   350-355   4 1992

      More details

      Authorship:Lead author, Corresponding author   Language:English   Publishing type:Research paper (other academic)  

      researchmap

    • Purification and properties of growth inhibitor from normal rabbit serum Peer-reviewed

      Takashi Kimura, Kaoru Miyazaki, Keisuke Mashima, Jinpei Yamashita, Takekazu Horio, Tomisaburo Kakuno

      Journal of Biochemistry110 ( 3 ) 423 - 328   1991

      More details

      Language:English   Publishing type:Research paper (scientific journal)   Publisher:Oxford University Press  

      It was previously found that rabbit serum contains a growth-inhibitory substance for a tumorigenic rat liver cell line RSV-BRL. In the present study, the growth inhibitor was purified from normal rabbit serum to show a homogeneous protein band with a molecular weight (Mr) of 56 k on SDS-polyacrylamide gel electrophoresis under non-reducing conditions. The purified growth inhibitor, tentatively named rabbit serum-derived growth inhibitor (RSGI), potently inhibited the growth of RSV-BRL and nine kinds of other cell lines including three human tumor cell lines at a concentration of 20 ng/ml or higher. The growth-inhibitory effect of RSGI was reversible and appeared to be cytostatic rather than cytotoxic. RSGI was stable to heating at 56°C for 30 min or treatment with 0.1 M 2-mercaptoethanol, but labile to heating at 100°C for 3 min or treatment with 1 M acetic acid (pH 2.3), 6 M urea, 50% (v/v) 1-propanol, or 0.1% (w/v) trypsin. These properties of RSGI suggested that it was different from type β transforming growth factors, tumor necrosis factor-α, and other known growth-regulatory factors. © 1991 by The Journal of Biochemistry.

      DOI: 10.1093/oxfordjournals.jbchem.a123597

      Scopus

      PubMed

      researchmap

    • 増殖阻害因子の分子的多様性と生理活性 - 特に血清中の増殖阻害因子とラットの形質転換細胞RSV-BRLが分泌する増殖阻害因子について(共著)

          285-291   4 1989

      More details

      Language:Japanese   Publishing type:Research paper (other academic)  

      researchmap

    • Structure of expression of elongation factor 2 gene during development of Dictyostelium discoideum Peer-reviewed

      K. Toda, M. Tasaka, K. Mashima, K. Kohno, T. Uchida, I. Takeuchi

      Journal of Biological Chemistry264 ( 26 ) 15489 - 15493   1989

      More details

      Language:English   Publishing type:Research paper (scientific journal)  

      A cDNA library constructed from poly(A)+ RNA isolated from Dictyostelium discoideum cells at 12 h of development was screened with the hamster elongation factor 2 (EF-2) cDNA. Several different cDNA clones which hybridized were isolated after a second screening. A cDNA clone representing the 5'-end of the mRNA was obtained by primer extension. By comparing the amino acid sequence deduced from the nucleotide sequences of these clones with that of hamster EF-2, we found enough homology between them to conclude that the isolated clones were complementary to the mRNA of D. discoideum EF-2. The N terminus which is the GTP-binding domain and the C-terminal half where it interacts with a ribosome showed a high degree of homology. The amino acid sequence of the carboxyl half includes that it contain a site of ADP-ribosylation by diphtheria toxin. From the Northern blotting analysis, the size of the mRNA was estimaed to be 2.6 kilobases. The expression of the mRNA was high in vegetative cells, became maximal at the aggregation stage, and decreased thereafter through development. Upon differentiation of prespore and prestalk cells, the mRNA was highly enriched in the former over the latter. ADP-ribosylation assay of EF-2 protein by diphtheria toxin showed nearly the same developmental changes for the protein as the mRNA. However, prestalk cells were found to contain the same amount of the protein as prespore cells. The Southern blot analyses indicated that the gene encoding EF-2 is unique.

      Scopus

      PubMed

      researchmap

    • 続生化学実験講座2 タンパク質の化学(上)(共著)

      角野富三郎, 眞島恵介, 山下仁平, 堀尾武一

      東京化学同人 日本生化学会編2   209-220   4 1988

      More details

      Language:Japanese   Publishing type:Part of collection (book)  

      researchmap

    • Multiple forms of growth inhibitors secreted from cultured rat liver cells: Purification and characterization

      Keisuke Mashima, Takashi Kimura, Weida Huang, Kazuo Yano, Yoshiyuki Ashida, Yoshiki Yamagata, Kaoru Miyazaki, Jinpei Yamashita, Takekazu Horio

      Journal of Biochemistry103 ( 6 ) 1020 - 1026   1988

      More details

      Authorship:Lead author   Language:English   Publishing type:Research paper (scientific journal)   Publisher:Oxford University Press  

      It was found that a non-tumorigenic epithelial cell line from the liver of a Buffalo-strain rat (BRL) secreted into the culture medium various inhibitors of the growth of BRL and RSV-BRL (tumorigenic BRL transformed by infection of Rous sarcoma virus). The secreted inhibitors were classified into two types: one inhibited the growth of BRL to a greater extent than that of RSV-BRL (non-tumorigenic BRL growth inhibitor, NGI), and the other, vice versa (tumorigenic BRL growth inhibitor, TGI). Two NGI (NGI-I and NGI-II) and two TGI (TGI-I and TGI-II) were highly purified from the serum-free conditioned medium. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis without 2-mercaptoethanol, NGI-I and II gave protein bands with molecular weights (Mr) of 56,000 and 21,000, respectively. TGI-I and II gave a band that migrated faster than bromophenol blue marker dye, but they did not pass through an ultrafiltration membrane with an Mr cutoff of 5,000. In the presence of a reducing reagent, only NGI-II showed a decrease of Mr, from 21,000 to 11,000. NGI and TGI showed 50% growth inhibition with BRL and RSV-BRL, respectively, at 5-15 ng/ml in the medium containing 10% fetal calf serum. NGI and TGI all were stable to 1 M acetic acid (pH 2.3) and 6 M urea, but labile to 5 mM dithiothreitol or trypsin. Of the eight cell lines tested, NGI-I was most effective on BRL, NGI-II on BRL and HSC-3 (human tongue squamous carcinoma), and both TGI-I and II on RSV-BRL. © 1988 BY THE JOURNAL OF BIOCHEMISTRY.

      DOI: 10.1093/oxfordjournals.jbchem.a122373

      Scopus

      PubMed

      researchmap

    • GROWTH-INHIBITORY PROTEIN PRESENT IN RABBIT SERUM, WHICH IS MORE EFFECTIVE ON TUMORIGENIC RAT-LIVER EPITHELIAL-CELLS THAN ON NONTUMORIGENIC ONES - ITS SPECIES, AND MODE OF EXISTENCE

      K MASHIMA, T KIMURA, K MIYAZAKI, J YAMASHITA, T HORIO

      BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS148 ( 3 ) 1215 - 1222   11 1987

      More details

      Authorship:Lead author   Language:English   Publishing type:Research paper (scientific journal)   Publisher:ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS  

      researchmap

    • TRANSFORMATION OF RAT-LIVER CELL-LINE BY ROUS-SARCOMA VIRUS CAUSES LOSS OF CELL-SURFACE FIBRONECTIN, ACCOMPANIED WITH SECRETION OF METALLOPROTEINASE THAT PREFERENTIALLY DIGESTS THE FIBRONECTIN Peer-reviewed

      K MIYAZAKI, Y ASHIDA, Y KIHIRA, K MASHIMA, J YAMASHITA, T HORIO

      JOURNAL OF BIOCHEMISTRY102 ( 3 ) 569 - 582   9 1987

      More details

      Language:English   Publishing type:Research paper (scientific journal)   Publisher:JAPANESE BIOCHEMICAL SOC  

      researchmap

    • GROWTH-INHIBITORS IN SERUM, PLATELETS, AND NORMAL AND MALIGNANT-TISSUES Peer-reviewed

      K MIYAZAKI, K MASHIMA, T KIMURA, W HUANG, K YANO, Y ASHIDA, Y KIHIRA, J YAMASHITA, T HORIO

      ADVANCES IN ENZYME REGULATION26   225 - 237   1987

      More details

      Language:English   Publishing type:Research paper (scientific journal)   Publisher:PERGAMON-ELSEVIER SCIENCE LTD  

      researchmap

    • Epithelial growth inhibitors in rat serum and human platelets(共著) Peer-reviewed

      Miyazaki, K., Mashima, K., Kimura, T., Huang, W., Masaki, H., Yamashita, J., Horio, T.

      Protides of the Biological Fluids34   553-556   4 1986

      More details

      Language:English   Publishing type:Research paper (other academic)  

      researchmap

    • Purification and properties of epithelial growth inhibitor (EGI) from human platelets: Its separation from type β transforming growth factor (TGF-β) Peer-reviewed

      Weida Huang, Takashi Kimura, Keisuke Mashima, Kaoru Miyazaki, Hiroaki Masaki, Jinpei Yamashtta, Takekazu Horio

      Journal of Biochemistry100 ( 3 ) 687 - 696   1986

      More details

      Language:English   Publishing type:Research paper (scientific journal)   Publisher:Oxford University Press  

      We previously reported that sera from various kinds of animals contain a protein(s) capable of inhibiting the growth of the non-malignant epithelial cell line derived from Buffalo rat liver (BRL). In the present study, a similar epithelial cell-specific growth inhibitor (EGI) was purified to homogeneity from an acid-ethanol extract of human platelets. During purification, EGI was separated from the major component of type β transforming growth factor (TGF-β), which can stimulate the colony formation of the non-malignant fibroblastic cell line derived from rat kidney (NRK) in soft agar in the presence of epidermal growth factor (EGF). The purified EGI had an Mr of 27,000, and was composed of two subunits identical in Mr. It significantly inhibited the growth in monolayer cultures of three non-malignant epithelial cell lines, BRL, MDCK (from Madin-Darby canine kidney) and BSC-1 (from African green monkey kidney), at doses lower than 40 pg/ml in medium containing 10% fetal calf serum. Its inhibitory activity was stable against heating at 90°C for 3min, but not against treatment with 50 mM dithiothreitol. In addition, TGF-β was also partially purified from the same extract. The purified TGF-β did not show any inhibitory activity toward the growth of BRL, MDCK, BSC-1, or NRK. © 1986, by the Japanese Biochemical Society.

      DOI: 10.1093/oxfordjournals.jbchem.a121761

      Scopus

      PubMed

      researchmap

    • Growth regulation of normal and RSV-transformed liver cells of rat by growth inhibitors presented in serum(共著)

      Proceeding of the International Symposium on Growth and Differentiation of Cell in Defined Environment, Springer-Verlag, Kohdansha, Belin, Tokyo,   443-448   4 1985

      More details

      Language:English   Publishing type:Research paper (international conference proceedings)  

      researchmap

    • Characterization of a growth-inhibiting protein present in rat serum that exerts a differential effect on in vitro growth of nonmalignant rat liver cells when compared with Rous sarcoma virus-transformed rat liver cells. Peer-reviewed

      Miyazaki K, Mashima K, Yamashita N, Yamashita J, Horio T

      In vitro cellular & developmental biology : journal of the Tissue Culture Association21   62 - 66   1 1985

      More details

      Publisher:1  

      PubMed

      researchmap

    • CHARACTERIZATION OF A GROWTH-INHIBITING PROTEIN PRESENT IN RAT SERUM THAT EXERTS A DIFFERENTIAL EFFECT ON INVITRO GROWTH OF NONMALIGNANT RAT-LIVER CELLS WHEN COMPARED WITH ROUS-SARCOMA VIRUS-TRANSFORMED RAT-LIVER CELLS Peer-reviewed

      K MIYAZAKI, K MASHIMA, N YAMASHITA, J YAMASHITA, T HORIO

      IN VITRO CELLULAR & DEVELOPMENTAL BIOLOGY21 ( 1 ) 62 - 66   1985

      More details

      Language:English   Publishing type:Research paper (scientific journal)   Publisher:SOC IN VITRO BIOLOGY  

      researchmap

    • 細胞増殖におけるプロテアーゼの役割(共著)

      宮崎 香, 山下信彦, 眞島恵介, 山下仁平, 堀尾武一

      日本応用酵素協会誌19   23-35   4 1984

      More details

      Language:Japanese   Publishing type:Research paper (other academic)  

      researchmap

    • 癌細胞の増殖機構の研究(共著)

      宮崎 香, 眞島恵介, 山下信彦, 紀平安則, 山下仁平, 堀尾武一

      生物物理化学28   195-200   4 1984

      More details

      Language:Japanese   Publishing type:Research paper (other academic)  

      researchmap

    ▼display all

    Research Projects

    • ウニの初期胚発生におけるタンパク質チロシン残基のリン酸化・脱リン酸化の機能解析

      立教大学  立教大学研究奨励助成金 

      More details

      4 1999 - 3 2000

      Grant type:Competitive

      個人研究

      researchmap

    • 免疫担当細胞であるBリンパ球で発現している受容体型チロシンホスファターゼCD45と特異的に結合するリガンドの同定とその構造解析

      立教大学  立教大学研究奨励助成金 

      More details

      4 1996 - 3 1997

      Grant type:Competitive

      個人研究

      researchmap

    • 骨髄性白血病細胞のタンパク質チロシンホスファターゼ(PTP)の多様性と機能に関する研究

      金子・成田財団  受託研究(一般受託研究) 

      More details

      4 1994 - 3 1996

      Grant type:Competitive

      researchmap

    • 細胞の癌化における チロシンホスファターゼの役割に関する研究

      日本学術振興会  科学研究費助成事業 

      More details

      4 1991 - 3 1992

      Grant type:Competitive

      researchmap

    • 細胞の癌化及び分化におけるチロシン残基のリン酸化反応・脱リン酸化反応の役割に関する研究

      立教大学  立教大学研究奨励助成金 

      More details

      4 1991 - 3 1992

      Grant type:Competitive

      個人研究

      researchmap

    • A study of protein tyrosine phosphatase on signal transduction.

      More details

      Grant type:Competitive

      researchmap

    • チロシンホスファターゼによる細胞内情報伝達の制御機構

      フロンティア研究 

      More details

      Grant type:Competitive

      researchmap

    ▼display all

    Social Contribution

    • 神経科学総合研究所

      4 1997 - Present

      More details

      客員研究員

      researchmap