Shirozu Michio

Health Care CenterProfessor
Last Updated :2025/04/27

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Profile Information

  • Name (Japanese)

    Shirozu
  • Name (Kana)

    Michio

Degree

  • Kyoto University, 1996

Research Areas

  • Life sciences, Internal medicine - General

Research History

  • Apr. 2017 - Present, 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

Education

  • 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

Teaching Experience

  • Apr. 2018 - Present, Undergraduate special subjects, Japan
  • Oct. 2016 - Present, Undergraduate liberal arts, Japan
  • Apr. 2016 - Present, Undergraduate liberal arts, Japan

Social Activities

  • Apr. 2004 - Mar. 2016

■Ⅱ.研究活動実績

Published Papers

  • Refereed, Biomedical Research, Biomedical Research Foundation, 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., 1999, 20, 1, 43, 49, Scientific journal, 10.2220/biomedres.20.43
  • Refereed, Genomics, 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, 37, 3, 273, 80, Scientific journal, True
  • Refereed, Gene, 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, 176, 1-2, 211, 4, Scientific journal, True
  • Refereed, Genomics, 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, 28, 3, 495, 500, Scientific journal, True
  • Refereed, The Journal of biological chemistry, 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, 268, 23, 17463, 70, Scientific journal, True
  • Refereed, Science (New York, N.Y.), 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, 261, 5121, 600, 3, Scientific journal, True

MISC

  • 2020, 36, 25, 37
  • Not Refereed, Nov. 2003, 43, 11, 786, 786
  • Not Refereed, Mar. 2000, 52, 3, 157, 157
  • Not Refereed, Mar. 2000, 52, 3, 156, 157
  • Not Refereed, Jan. 2000, 40, 1, 74, 74
  • Not Refereed, Nov. 1998, 50, 6, 426, 427
  • Not Refereed, Sep. 1998, 3, 1, 30, 30
  • Not Refereed, Feb. 1998, 62, 2, 102, 104
  • Not Refereed, Oct. 1997, 12, 3, 268, 274
  • Not Refereed, Sep. 1997, 臨増, 医療改革, 129, 132
  • Not Refereed, Aug. 1997, 7, 8, 679, 682
  • Not Refereed, Jul. 1997, 7, 7, 546, 547

Books etc

Presentations

  • Poster presentation
  • Poster presentation
  • Poster presentation
  • Oral presentation, 05 Oct. 2021 - 06 Oct. 2021