Researchers Database

Shirozu Michio

    Health Care Center Professor
    Health Care Center Director, Health Care Center
Last Updated :2021/10/20



  • Kyoto University, 1996

Research Areas

  • Life sciences, Internal medicine - General

Research Experience

  • Apr. 2017, Nara Women's University, Health Care Center, director, Japan
  • Apr. 2016 Mar. - 2017, Nara Women's University, Health Care Center, Full-time Teacher, Japan
  • Apr. 2002 Mar. - 2016, Okatani Hospital, internal and psychosomatic medicine, 医師, Japan
  • Oct. 1999 Mar. - 2008, Kyoto University Hospital, Department of General Medicine, physician, 非常勤, Japan
  • Apr. 2000 Mar. - 2002, Yasunaka clinic, internal and psychosomatic medicine, physician, Japan
  • May 1997 Sep. - 1999, Japanpost Kyoto-Teishin Hospital, Health Care Center, industrial physician, Japan
  • Apr. 1995 Apr. - 1997, Kyoto University Hospital, Department of General Medicine, physician, Japan
  • Jun. 1989 Mar. - 1991, Kobe City central municipal hospital, internal medicine, resident, Japan


  • Apr. 1991, Mar. - 1995, Kyoto University Graduate School, medicine graduate course, medical chemistry, Japan
  • Apr. 1983, Mar. - 1989, Kyoto University, Faculty of Medicine, Department of Medical Science, Japan

Published Papers

  • Isoform specific expression of the SDR-1 protein, α and β in subregions of adult rodent brain

    Nelson D. Lopez; Ayae Kinoshita; Masafumi Taniwaki; Hideaki Tada; Michio Shirozu; Toru Nakano; Kei Tashiro; Tasuku Honjo

    Stromal cell-derived receptor-1 (SDR-1) α and β, also called gp55 and gp65, belong to the immunoglobulin (Ig) superfamily. Rabbit antisera specific to SDR-1 β and those recognizing both α and β forms of SDR-1 were raised to study regional distributions of SDR-1 α and β in the adult rodent brain. Immunohistochemical studies of adult rat brains with either antibodies revealed a granular pattern of staining distributed within neuropils. SDR-1 β form like immunoreactivity (β-LI) was detected in limited regions, namely the glomerulus of the olfactory bulb and the superficial layers (layers II, III) of the cerebral cortex, whereas αβ-LI was found in the olfactory tubercle, cerebral center, hippocampus, thalamus, midbrain, and molecular layer in the cerebellum, suggesting wider distribution of SDR-1α. The SDR1 gene is highly conserved from Xenopus to human. The human SDR-1 cDNA was isolated and the human SDR1 gene was mapped to chromosome 15q22 by fluorescence in situ hybridization., Biomedical Research Foundation, 1999, Biomedical Research, 20 (1), 43 - 49, doi

    Scientific journal

  • Characterization of novel secreted and membrane proteins isolated by the signal sequence trap method.

    M Shirozu; H Tada; K Tashiro; T Nakamura; N D Lopez; M Nazarea; T Hamada; T Sato; T Nakano; T Honjo

    We recently described a method, called the signal sequence trap (SST) method, to clone cDNAs of secreted proteins and/or type I transmembrane proteins containing N-terminal signal sequences by using an epitope-tagging expression plasmid vector. In this paper we describe the summary of a large-scale screening of approximately 5900 clones of an SST cDNA library constructed from mouse bone marrow stromal cell line ST-2 cells. Of 26 positive clones obtained and sequenced, 11 clones appeared to contain authentic signal sequences. Five of the clones corresponded to the 5' ends of the cDNA of known genes containing N-terminal signal sequences. The full-length cDNA clones of the 6 other unknown clones were isolated and sequenced. One clone, termed SDF3, encoded a mouse counterpart of human pigment epithelium-derived factor. Another clone, termed SDR1, had considerable homology with basigin, a member of the immunoglobulin superfamily. A third clone, termed SDF5, had partial homology with a Drosophila tissue polarity gene frizzled (fz) and its rat homologues, fz-1 and fz-2. The other three clones had no significant homology with sequences in the databases. These results indicate that the SST method is effective and useful for the isolation of secreted and membrane proteins without knowledge of their functions., 01 Nov. 1996, Genomics, 37 (3), 273 - 80, True, pubmed

    Scientific journal

  • Isolation and characterization of a novel secretory protein, stromal cell-derived factor-2 (SDF-2) using the signal sequence trap method.

    T Hamada; K Tashiro; H Tada; J Inazawa; M Shirozu; K Shibahara; T Nakamura; N Martina; T Nakano; T Honjo

    With use of the signal sequence trap method, we isolated a cDNA encoding a novel secretory protein, SDF-2, from the mouse stromal cell line, ST2. The human homologue of SDF-2 was also isolated. The amino acid (aa) sequences deduced from both the clones were conserved more than 92%. The chromosomal localization of the human SDF-2 gene was mapped to 17q11.2. The aa sequence of SDF-2 shows similarity to those of yeast dolichyl phosphate-D-mannose:protein mannosyltransferases, Pmt1p [Strahl-Bolsinger et al. (1993) Proc. Natl. Acad. Sci. USA 90, 8164-8168] and Pmt2p [Lussier et al. (1995) J. Biol. Chem. 270, 2770-2775], whose activities have not been detected in higher eukaryotes., 17 Oct. 1996, Gene, 176 (1-2), 211 - 4, True, pubmed

    Scientific journal

  • Structure and chromosomal localization of the human stromal cell-derived factor 1 (SDF1) gene.

    M Shirozu; T Nakano; J Inazawa; K Tashiro; H Tada; T Shinohara; T Honjo

    Stromal cell-derived factors 1 alpha and 1 beta are small cytokines belonging to the intercrine CXC subfamily and originally isolated from a murine bone-marrow stroma cell line by the signal sequence trap method. cDNA and genomic clones of human SDF1 alpha and SDF1 beta (SDF1A and SDF1B) were isolated and characterized. cDNAs of SDF1 alpha and SDF1 beta encode proteins of 89 and 93 amino acids, respectively. SDF1 alpha and SDF1 beta sequences are more than 92% identical to those of the human counterparts. The genomic structure of the SDF1 gene revealed that human SDF1 alpha and SDF1 beta are encoded by a single gene and arise by alternative splicing. SDF1 alpha and SDF1 beta are encoded by 3 and 4 exons, respectively. Ubiquitous expression of the SDF1 gene, except in blood cells, was consistent with the presence of the GC-rich sequence in the 5'-flanking region of the SDF1 gene, as is often the case in the "housekeeping" genes. Although genes encoding other members of the intercrine family are localized on chromosome 4q or 17q, the human SDF1 gene was mapped to chromosome 10q by fluorescence in situ hybridization. Strong evolutionary conservation and unique chromosomal localization of the SDF1 gene suggest that SDF1 alpha and SDF1 beta may have important functions distinct from those of other members of the intercrine family., 10 Aug. 1995, Genomics, 28 (3), 495 - 500, True, pubmed

    Scientific journal

  • The human S mu bp-2, a DNA-binding protein specific to the single-stranded guanine-rich sequence related to the immunoglobulin mu chain switch region.

    Y Fukita; T R Mizuta; M Shirozu; K Ozawa; A Shimizu; T Honjo

    We have cloned the cDNA encoding the human homologue of S mu bp-2, which binds to single-stranded DNA with 5'-phosphorylated guanine-rich sequences related to the immunoglobulin mu chain switch (S mu) region. The deduced amino acid sequences of the mouse and human S mu bp-2 are 76.5% homologous and contain motifs conserved among helicases. We have identified a domain essential for DNA binding at residues 638-786. The binding domain is less conserved (63% homologous) than the putative catalytic domain of N-terminal half containing most of the helicase motifs (85% homologous). The human and mouse S mu bp-2 have similar, although slightly different, binding specificities. Although the mouse S mu bp-2 preferentially binds to the mouse S mu motif (GGGGT), the human S mu bp-2 binds equally well to the human (GGGCT) and mouse S mu motifs. The human S mu bp-2 gene was mapped to chromosome 11 q13.2-q13.4 by in situ hybridization., 15 Aug. 1993, The Journal of biological chemistry, 268 (23), 17463 - 70, True, pubmed

    Scientific journal

  • Signal sequence trap: a cloning strategy for secreted proteins and type I membrane proteins.

    K Tashiro; H Tada; R Heilker; M Shirozu; T Nakano; T Honjo

    A method was developed to clone, without the use of specific functional assays, complementary DNAs (cDNAs) that carry specific amino-terminal signal sequences, such as those encoding intercellular signal-transducing molecules and receptors. The vector used in this system directed the cell surface expression of interleukin-2 receptor fusion proteins when inserts with signal sequences were cloned in-frame with the correct orientation. An expression cDNA library was constructed from a bone marrow stromal cell line, which contained 5' portion-enriched cDNAs (the average size was 400 base pairs). Two cDNAs that encoded putative cytokine molecules, stromal cell-derived factor-1 alpha (SDF-1 alpha) and SDF-1 beta, which belong to the intercrine-macrophage inflammatory protein superfamily, were cloned., 30 Jul. 1993, Science (New York, N.Y.), 261 (5121), 600 - 3, True, pubmed

    Scientific journal


  • 患者の真実を受け容れる 非精神病の幻覚患者の1例

    白水 倫生

    (一社)日本心身医学会, Nov. 2003, 心身医学, 43 (11), 786 - 786, jamas_url

  • 定期健康診断における尿潜血検査の意義

    金子 至寿佳; 宮田 學; 白水 倫生; 久萬田 俊明

    (株)郵研社, Mar. 2000, 逓信医学, 52 (3), 157 - 157

  • 成人病検診及び健康診断における血清鉄測定の有用性について

    宮田 學; 金子 至寿佳; 白水 倫生; 久萬田 俊明

    (株)郵研社, Mar. 2000, 逓信医学, 52 (3), 156 - 157

  • 間主観的観点に基づいたヒステリー様の難治性てんかん患者に対する治療の1例

    白水 倫生; 福井 次矢

    (一社)日本心身医学会, Jan. 2000, 心身医学, 40 (1), 74 - 74, jamas_url;jamas_url;jamas_url

  • 定期健康診断有所見者のフォローアップ

    白水 倫生; 宮田 學

    (株)郵研社, Nov. 1998, 逓信医学, 50 (6), 426 - 427

  • 入院患者でのAdverse Eventsの発生頻度

    白水 倫生; 山本 和利; 前川 宗隆; 福井 次矢

    日本総合診療医学会, Sep. 1998, 総合診療研究会会誌, 3 (1), 30 - 30

  • 【成人病から生活習慣病へ】「生活習慣病」でよいのか 臨床医の立場から

    白水 倫生; 福井 次矢

    (株)医学書院, Feb. 1998, 公衆衛生, 62 (2), 102 - 104, jamas_url;jamas_url;jamas_url

  • 人間ドックにおける糖負荷試験及び一回採血法による耐糖能障害の評価 糖負荷試験は必要か

    宮田 學; 白水 倫生; 作本 静枝

    糖負荷試験と一回採血法を対比して検討したところ,HbAlc8.0%以上或いはフルクトサミン300μmole/l以上は要治療群,HbAlc6.0%未満は要観察群とし,これ以外の群については,できれば後日糖負荷試験を施行して糖代謝異常の程度に応じて治療方針を決定するというのが実際的と考えられた, (公社)日本人間ドック学会, Oct. 1997, 健康医学, 12 (3), 268 - 274, jamas_url;jamas_url

  • 予防医学はどうして重要か

    白水 倫生; 福井 次矢

    (株)日本評論社, Sep. 1997, からだの科学 増刊, 臨増 (医療改革), 129 - 132

  • 転移性骨腫瘍が疑われた患者の鑑別診断

    白水 倫生; 山本 和利; 福井 次矢

    (株)医学書院, Aug. 1997, JIM: Journal of Integrated Medicine, 7 (8), 679 - 682, jamas_url

  • 倦怠感(だるさ)の病態

    白水 倫生

    (株)医学書院, Jul. 1997, JIM: Journal of Integrated Medicine, 7 (7), 546 - 547, jamas_url

  • シグナルシークエンストラップ法(SST)を用いた分泌蛋白およびI型膜蛋白のクローニング

    白水 倫生

    (公社)日本生化学会, Jul. 1995, 生化学, 67 (7), 746 - 746

Books etc

  • 内科学

    白水倫生; 福井次矢 (, Range: 医原性疾患)

    朝倉書店, Oct. 1999, xxxix, 2110p, cinii_books (ISBN: 4254321864)

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