Updated on 2021/07/06

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 Field of Study: Life Science
Graduate School of Science Field of Study: Life Science
Title*
Professor
Degree
理学博士 ( 大阪大学 ) / 理学博士
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
  • signal transduction

  • Protein tyrosine phosphatase

  • リン酸化・脱リン酸化

  • Campus Career*
    • 4 2010 - Present 
      College of Science   Department of Life Science   Professor
    • 4 2010 - Present 
      Graduate School of Science   Field of Study: Life Science   Professor
    • 4 2010 - Present 
      Graduate School of Science   Field of Study: Life Science   Professor
    • 4 2007 - 3 2010 
      College of Science   Department of Life Science   Associate Professor
    • 4 2002 - 3 2007 
      College of Science   Department of 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
     

    Research Areas

    • Life Science / Functional biochemistry

    • Life Science / Immunology

    Research History

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

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

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

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

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

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

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

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

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    • 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)

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    Education

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

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      Country: Japan

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

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      Country: Japan

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

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      Country: Japan

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

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      Country: Japan

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    • - 3 1981 
      University of Tsukuba   Second Cluster of College

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      Country: Japan

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    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

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    • 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

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

      Biochemistry57   1620 - 1631   2018

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    • 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

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    • 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

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    • 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

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    • 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

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    • 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

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    • 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

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    • 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

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

      Ryo Hanai, Keisuke Mashima

      Mol. Biol. Rep.30   149 - 153   2003

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    • 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

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      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

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

      Keisuke Mashima, Yuriko Furuya

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

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      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

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    • 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

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      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

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    • 分子細胞生物学基礎実験法

      南江堂   424-439   4 1994

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    • 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

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    • 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

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    • 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

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      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

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    • 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

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    • 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

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      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

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    • 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

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    • 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

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      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.

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    • 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

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    • 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

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      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

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    • 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

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

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    • 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

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

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    • 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

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    • 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

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    • 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

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      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

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    • 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

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    • 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

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

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    • 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

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    • 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

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    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 

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      4 1999 - 3 2000

      Grant type:Competitive

      個人研究

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    • 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 

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      4 1996 - 3 1997

      Grant type:Competitive

      個人研究

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    • 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) 

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      4 1994 - 3 1996

      Grant type:Competitive

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    • 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 

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      4 1991 - 3 1992

      Grant type:Competitive

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    • 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 

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      4 1991 - 3 1992

      Grant type:Competitive

      個人研究

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    • 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 

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      Grant type:Competitive

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    • A study of protein tyrosine phosphatase on signal transduction.

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      Grant type:Competitive

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    Social Contribution

    • 神経科学総合研究所

      4 1997 - Present

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      客員研究員

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