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MIYAMOTO Hiroshi

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FacultyDepartment of Genetic Engineering / Graduate School of Biology-Oriented Science and Technology
PositionProfessor
Degree
Commentator Guidehttps://www.kindai.ac.jp/meikan/491-miyamoto-hiroshi.html
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Last Updated :2020/09/09

Education and Career

Education

  •  - 1992 , Osaka University
  •  - 1992 , Osaka University, Graduate School of Science

Research Activities

Research Areas

  • Life sciences, Molecular biology

Research Interests

  • Molecular Biology

Published Papers

  • Signs of biological activities of 28,000-year-old mammoth nuclei in mouse oocytes visualized by live-cell imaging, 9, 4050, 2019 , Refereed
  • Searches and characterization of shell matrix proteins common in molluscs., MIYAMOTO Hiroshi, Venus, Venus, 74, A-18, 2016
  • Bivalve-specific gene expansion in the pearl oyster genome: implications of adaptation to a sessile lifestyle., Takeuchim, T, Koyanagi, R, Gyoja, F, Kanda, M, Hisata, K, Fujie, M, Goto, H, Yamasaki, S, Nagai, K, Morino, Y, Miyamoto, H, Endo, K, Endo, H, Nagasawa, H, Kinoshita, S, Asakawa, S, Watabe, S, Satoh, N, Kawashima, T, Zoological Lett., Zoological Lett., 2, 3, 2016 , Refereed
  • Molecular characterization of glycine-rich shell matrix proteins in Pinctada fucata and Haliotis discus discus., MIYAMOTO, H, Venus : journal of the Malacological Society of Japan, Venus : journal of the Malacological Society of Japan, 72, 160, Mar. 2014
  • I-1. Shell matrix protein research starting from the pearl, Hiroshi Miyamoto, Nippon Suisan Gakkaishi (Japanese Edition), Nippon Suisan Gakkaishi (Japanese Edition), 80(1), 102 - 102, 2014
  • A new oyster carbonic anhydrase in Crassostrea gigas, Okumura, N, Miyamoto, H, Mem.Inst. Advanced Tech. Kinki Univ., Mem.Inst. Advanced Tech. Kinki Univ., 18(18), 12 - 20, Mar. 2013 , Refereed
    Summary:[Abstract] In metazoans, carbonic anhydrase(CA)is a common enzyme that catalyzes the reversible hydration of carbon dioxide. CA plays important roles in many biological processes, and in molluscs several CA-like proteins are thought to be responsible for calcification in shell formation. As part of our investigation of the process of shell formation, we searched for a CA gene in the oyster Crassostrea gigas, with resultant identification of a single cDNA that encodes two CA domains. This atypical CA is similar to an α-CA and is mainly expressed in the egg. This suggests that the newly identified CA is responsible for production of bicarbonate in the early development phase prior to metamorphosis. [要旨] 炭酸脱水酵素は後生動物に広く存在しており、二酸化炭素の水和を可逆的に触媒する。機能的には様々な生命過程で重要な役割を担っており、軟体動物では炭酸脱水酵素や類似タンパク質が貝殻形成における石灰化に関与していることが示唆されている。本論文では、貝殻形成の過程を調べる研究の中で同定したマガキの新規炭酸脱水酵素について報告する。単離したcDNA は、二つのCA ドメインを有しており、典型的な炭酸脱水酵素とは構造が異なっていたが、それぞれのCA ドメインはα タイプの炭酸脱水酵素との類似性を示した。また、今回同定した新規炭酸脱水酵素は卵での発現が著しく高く、変態前の重炭酸イオンの生成を担っていると推察される。
  • Two novel glycine-rich proteins expressed in the mantle of the pearl oyster. Recent advances in pearl research., Okumura, N, Miyamoto, H, Recent advances in pearl research., Recent advances in pearl research., 239 - 244, 2013 , Refereed
  • Highly rearranged mitochondrial genome of the bivalve pearl oyster Pinctada fucata., Okumura, N, Oishi, M, Okayama, K, Miyamoto, H, Mem. Faculty. B.O.S.T. Kinki Univ, Mem. Faculty. B.O.S.T. Kinki Univ, 29, 1 - 6, 2012 , Refereed
  • SPARC is a common calcification-related molecule expressed in the mantle of Pinctada fucata and Haliotis discus discus., Miyamoto, H, Venus, Venus, 70, 90, 2012
  • SPARC is a common mineralization-related molecule in bivalves and gastropods., Miyamoto, H, Asada, F, Mem. Faculty. B.O.S.T. Kinki Univ, Mem. Faculty. B.O.S.T. Kinki Univ, 27, 1 - 6, 2011 , Refereed
  • Comparison of shell proteins between Pinctada fucata and Haliotis discus discus., Miyamoto, H, Venus, Venus, 69, 108, 2010 , Refereed
  • 日本産と中国産アコヤガイにおけるshematrin遺伝子の比較, 矢野昌人, 宮本裕史, Mem. School B.O.S.T. Kinki Univ, Mem. School B.O.S.T. Kinki Univ, 23(23), 47 - 53, Mar. 2009 , Refereed
    Summary:Departmental Bulletin Paper
  • Molecular characterization of genes expressed in the mantle of the pearl oyster., Miyamoto, H, Yano, M, Proceedings of the WFC2008, Proceedings of the WFC2008, 1 - 2, 2008 , Refereed
  • Conserved Ribosomal Protein Sequences S5, S18, S27, S30 in the Pacific Oyster Crassostrea gigas and Crassostrea virginica., Miyamoto, H, Kajihara, K, Mem. School B.O.S.T. Kinki Univ., Mem. School B.O.S.T. Kinki Univ., 16, 1 - 5, Sep. 30 2005 , Refereed
    Summary:cDNA fragments encoding ribosomal proteins were isolated from the mantle of pacific oyster Crassostrea gigas by the subtractive hybridization method. The sequence information was used to isolate entire cDNAs, and the predicted amino acid sequences were shown to be very similar to the 40S ribosomal protein genes (S5, S18, S27, and S30) of Crassostrea virginica. Northern blot hybridization revealed that S5, S18, and S30 were predominantly expressed in the digestive gland, the gill, and the mantle. On the other hand, S27 was highly expressed in the adductor muscle.
  • Functional analysis of the nacrein gene in Pinctada fucata(Abstracts of Papers Presented at the 2005 Annual Meeting of the Malacological Society of Japan (Nishinomiya)), Miyamoto H, Venus : journal of the Malacological Society of Japan, Venus : journal of the Malacological Society of Japan, 64(1), Jun. 2005
  • The ribosomal protein S2 from the pacific oyster Crassostrea gigas., Miyamoto, H, Kajihara, K, Mem.Inst. Advanced Tech. Kinki Univ., Mem.Inst. Advanced Tech. Kinki Univ., 15, 15 - 20, Mar. 2005
  • Molecular characterization of tubulin genes of the pacific oyster Crassostrea gigas., Mem. School B.O.S.T. Kinki Univ., Mem. School B.O.S.T. Kinki Univ., 10, 37 - 41, Mar. 2005
  • Functional analysis of the nacrein gene in Pinctada fucata., Miyamoto, H, Venus, Venus, 64, 82, 2005 , Refereed
  • Molecular characterization of tubulin genes of the pacific oyster Crassostrea gigas., Miyamoto, H, Kohno, J, Kajihara, K, Mem. School B.O.S.T. Kinki Univ., Mem. School B.O.S.T. Kinki Univ., 10, 37 - 41, 2005 , Refereed
  • Identical carbonic anhydrase contributes to nacreous or prismatic layer formation in Pinctada fucata (Mollusca : Bivalvia), T Miyashita, R Takagi, H Miyamoto, A Matsushiro, VELIGER, VELIGER, 45(3), 250 - 255, Jul. 2002 , Refereed
    Summary:We have found a carbonic anhydrase (CA) in the prismatic layer of Pinctada fucata. This CA has the same kinetic properties as Nacrein, which is a CA existing in the nacreous layer of Pinctada fucata. We have examined the effects of inhibitors on the enzyme activity. Sodium sulfide and sulfanilamide are typical inhibitors of various types of CA; however. a CA in the prismatic layer and Nacrein were found to be resistant to sodium Sulfide and to show a weak resistance to sulfanilamide. This is the first report of a carbonic anhydrase with resistance to sodium sulfide, The molecular mass of the prismatic layer CA was estimated by SDS-PAGE to be approximately 60 kDa. Moreover, we have determined the N-terminal amino acid sequence of a CA in the prismatic layer. The sequence of the first 11 amino acids was in agreement with that of Nacrein, as deduced from the cDNA sequence. From these results, we have concluded that the carbonic anhydrase of the prismatic layer is Nacrein. Nacrein contributes to the formation of a prismatic layer as well as a nacreous layer of mollusk shells as a carbonic anhydrase and is a matrix component.
  • アコヤガイ感染症原因の分子生物学的手法による解析, 宮本裕史, 農林水産技術会議「魚介類の新興及び再興感染症の病害防除技術の開発, 農林水産技術会議「魚介類の新興及び再興感染症の病害防除技術の開発, 399, 67 - 76, 2002
  • A novel isoform of actin in the pacific oyster., Miyamoto, H, Mem. School B.O.S.T. Kinki Univ., Mem. School B.O.S.T. Kinki Univ., 9, 1 - 4, 2002 , Refereed
  • Miyashita, T., Takagi, Y., Miyamoto, H., and Matsushiro, A., Miyashita, T, Takagi, Y, Miyamoto, H, Matsushiro, A, The Veliger., The Veliger., 45, 250 - 255, 2002 , Refereed
  • 真珠層形成の分子機構, 宮下知幸, 宮本裕史, 松代愛三, Mem. School B.O.S.T. Kinki Univ., Mem. School B.O.S.T. Kinki Univ., 5(5), 1 - 8, Nov. 2000 , Refereed
  • Sequence of a cDNA encoding a novel basic protein expressed in rabbit placenta., Miyamoto, H, Matsumoto, K, Hosoi, Y, Saeki, K, Matsushiro, A, Iritani, A, Jpn. J. Fertil. Steril., Jpn. J. Fertil. Steril., 45(4), 37 - 39, Oct. 01 2000 , Refereed
  • Characteristics of stx-converting phages of EHEC O157., Matsushiro, A, Sato, K, Miyamoto, H, Yamamura, T, Honda, T, Mem. Research Inst. B.O.S.T. Kinki Univ., Mem. Research Inst. B.O.S.T. Kinki Univ., 2, 6 - 10, 1999 , Refereed
  • Carbonic anhydrase activity in the soluble matrix proteins from the prismatic layer in Pinctada fucata, 宮下 知幸, 高木 良介, 宮本 裕史, 松代 愛三, Memoirs of the Research Institute of Biology-Oriented Science and Technology, Kinki University, Memoirs of the Research Institute of Biology-Oriented Science and Technology, Kinki University, (1), 36 - 40, Nov. 1998
    Summary:継続後誌:近畿大学先端技術総合研究所紀要 = Memoirs of Institute of Advanced Technology, Kinki University貝殻は無脊椎動物における典型的な硬組織であり、方解石あるいはアラレ石構造の炭酸カルシウムの結晶からなる。アコヤ貝の硬組織についてみると、外側は稜中層と呼ばれ、方解石構造の炭酸カルシム結晶であり、また、真珠層と呼ばれる内側は同様に炭酸カルシムの結晶であるが、アラレ石構造である。これらの硬組織形成には以前から炭酸脱水酵素が関与することが指摘されてきたが、アコヤ貝稜中層よりEDTAで抽出した可溶性マトリックスタンパク質中にも真珠層と同様に炭酸脱水酵素の存在が確認された。この酵素は稜中層における方解石構造形成過程で働くものと思われ、真珠層のナクレインに対応するものと考えられる。また、一般的に、炭酸脱水酵素は硫化ナトリウムやスルファニルアミドで活性が阻害されるが、可溶性マトリックス中の酵素は硫化ナトリウムに抵抗性であることが解かった。 (英文) Mollusk shells are typical hard tissue in invertebrate, and composed of either calcite or aragonite, differ with polymorphs of CaCO_3. Shell of pearl oysters (Pinctada fucata) consists of both layers, one is outer prismatic layer which is bearing calcite, another is inner nacreous layer which is bearing aragonite. It is already suggested that carbonic anhydrases that catalyze the interconversion of CO_2 and H_2O (CO_ 2 + H_2O ⇔ HCO_3^- + H^+) are participate in the process of calcification. We have detected a carbonic anhydrase activity in the soluble matrix proteins from the prismatic layer in Pinctada fucata. A putative molecular weight is about 60KDa. It is assumed that this enzyme is responsible for the formation of prismatic layer and corresponds to nacrein in the nacreous layer. Sulfanilamide and sodium sulfate are generally inhibitors of carbonic anhydrases. However, these enzymes in the soluble matrix proteins are resistance to sodium sulfate.
  • Analysis of transgenic mice produced by testis-mediated gene transfer, 松本 和也, 細井 美彦, 豊川 弘治, 中上 佳世子, 宮本 裕史, 佐伯 和弘, 入谷 明, Memoirs of the Research Institute of Biology-Oriented Science and Technology, Kinki University, Memoirs of the Research Institute of Biology-Oriented Science and Technology, Kinki University, (1), 31 - 35, Nov. 1998
    Summary:継続後誌:近畿大学先端技術総合研究所紀要 = Memoirs of Institute of Advanced Technology, Kinki University微小ガラス針を使って受精卵前核に遺伝子溶液を注入する顕微注入法に代わる簡便なトランスジェニックマウスの作製方法を検討するために、外来遺伝子を雄マウスの精巣に直接注入して雌マウスと交配させることによって、トランスジェニックマウスを作製することを検討した。DNA/リポソーム複合体を4匹の雄マウスの精巣に直接注入したのち静置させ、1週間後に雌マウスと交配させたところ、計38匹の産子を獲得した。離乳後各マウスの尾部組織より抽出したゲノムDNAを使ったサザンプロット解析の結果、5匹のマウスに導入遺伝子の組込みが認められた。そのうち、次世代へ導入遺伝子の伝達が認められたトランスジェニックマウスは、2匹であった。また、トランスジェニックマウスのゲノムDNAから導入遺伝子と考えられる遺伝子断片の一部を増幅し、ダイレクトシークエンスでその塩基配列を決定したところ、導入遺伝子がマウス染色体へ組込まれていることが確認された。以上の結果より、経精巣遺伝子導入法によるトランスジェニックマウスの作製の可能性が示唆された。しかし、精巣に導入されたDNAと精子の結合様式、また卵子と受精後の染色体への組込み機序については未だ不明な点が多く、今後さらに検討が必要と考えられた。 (英文) DNA transfer mediated by sperm has the potential to simplify the production of transgenic animals, but the possibility in mice has been controversial. On the other hand, the ability of animal spermatozoa to capture foreign DNA has been suggested. In this study, we investigated the feasibility to produce transgenic mice by direct injection of foreign DNA in mouse testis. DNA/liposome complex was injected through a needle into testes bilateral testis of four mature mice. After all males were mated with female mice, 38 pups were delivered. In Southern blot analysis and direct sequencing, the foreign DNA was shown to be integrated in host genome of five mice (13%). However, only two trangenic mice exhibited the transmission of transgene to next generation. Thus, direct introduction of exogenous DNA/liposome complex into the testis will provide a simple methodin generation of transgenic mice, and further investigations are also necessary to determine molecular mechanisms based on the uptake of foreign DNA by sperm.
  • Molecular Analyses of Nacrein, a Common Carbonic Anhydrase involved in Mollusk Shell formation., Miyamoto, H, Miyashita, T, Matsushiro, A, Symposium on Molecular Bioengineering of Food Animals., Symposium on Molecular Bioengineering of Food Animals., 31 - 38, 1998 , Refereed
  • 有機マトリックスタンパク質nacreinの構造と真珠層形成における機能., Matsushiro, A, Miyashita, T, Miyamoto, H, Hontsu, S, Mem. School B.O.S.T. Kinki Univ, Mem. School B.O.S.T. Kinki Univ, 1(1), 24 - 30, Feb. 1997 , Refereed
  • Genetic and molecular analysis of a canoe, a pattern formation locus of Drosophila melanogaster., Yamamoto, D, Miyamoto, H, Basic Neuroscience in Invertebrates, Basic Neuroscience in Invertebrates, 111 - 121, 1996 , Refereed
  • Molecular cloning and expression of misty gene required for development of drosophila photoreceptor cells., Miyamoto, H, Ikegami, Y, Hirata, K, Nihinmatsu, I, Yamamoto,D, Neurosci. Res., Neurosci. Res., 18, 80, 1993 , Refereed
  • Characterization of the cDNA clone (MO25) screened by differential hybridization of a mouse 8-cell morula cDNA library. Cell Differ. and Develop., Nozaki, M, Miyamoto, H, Morita, T, Matsushiro, A, Cell Differ. and Develop., Cell Differ. and Develop., 27, 146, 1989 , Refereed
  • Analyses of mouse 8-cell cDNA clones., Nozaki, M, Miyamoto, H, Morita, T, Matsushiro, A, Develop. Growth & Differ., Develop. Growth & Differ., 30, 447 - 447, Oct. 1988 , Refereed
  • Structure of the organic matrix protein nacrein, and its function on the macreous layer formation, A.Matsushiro, T.Miyashita, H.Miyamoto, S.Hontsu, Mem. School. B.O.S.T. Kinki Univ., Mem. School. B.O.S.T. Kinki Univ., 1, 24 - 29, Refereed
  • The Diversity of Shell Matrix Proteins: Genome-wide Investigation of the Pearl Oyster, Pinctada fucata, Hiroshi Miyamoto, Hirotoshi Endo, Naoki Hashimoto, Kurin Iimura, Yukinobu Isowa, Shigeharu Kinoshita, Tomohiro Kotaki, Tetsuji Masaoka, Takumi Miki, Seiji Nakayama, Chihiro Nogawa, Atsuto Notazawa, Fumito Ohmori, Isao Sarashina, Michio Suzuki, Ryousuke Takagi, Jun Takahashi, Takeshi Takeuchi, Naoki Yokoo, Nori Satoh, Haruhiko Toyohara, Tomoyuki Miyashita, Hiroshi Wada, Tetsuro Samata, Kazuyoshi Endo, Hiromichi Nagasawa, Shuichi Asakawa, Shugo Watabe, ZOOLOGICAL SCIENCE, ZOOLOGICAL SCIENCE, 30(10), 801 - 816, Oct. 2013 , Refereed
    Summary:In molluscs, shell matrix proteins are associated with biomineralization, a biologically controlled process that involves nucleation and growth of calcium carbonate crystals. Identification and characterization of shell matrix proteins are important for better understanding of the adaptive radiation of a large variety of molluscs. We searched the draft genome sequence of the pearl oyster Pinctada fucata and annotated 30 different kinds of shell matrix proteins. Of these, we could identified Perlucin, ependymin-related protein and SPARC as common genes shared by bivalves and gastropods; however, most gastropod shell matrix proteins were not found in the P. fucata genome. Glycinerich proteins were conserved in the genus Pinctada. Another important finding with regard to these annotated genes was that numerous shell matrix proteins are encoded by more than one gene; e.g., three ACCBP-like proteins, three CaLPs, five chitin synthase-like proteins, two N16 proteins (pearlins), 10 N19 proteins, two nacreins, four Pifs, nine shematrins, two prismalin-14 proteins, and 21 tyrosinases. This diversity of shell matrix proteins may be implicated in the morphological diversity of mollusc shells. The annotated genes reported here can be searched in P. fucata gene models version 1.1 and genome assembly version 1.0 (http://marinegenomics.oist.jp/pinctada_fucata). These genes should provide a useful resource for studies of the genetic basis of biomineralization and evaluation of the role of shell matrix proteins as an evolutionary toolkit among the molluscs.
  • Sequence of the Pearl Oyster Carbonic Anhydrase-Related Protein and Its Evolutionary Implications, Hiroshi Miyamoto, BIOCHEMICAL GENETICS, BIOCHEMICAL GENETICS, 50(3-4), 269 - 276, Apr. 2012 , Refereed
    Summary:Carbonic anhydrases are conserved in vertebrates and invertebrates, and a noncatalytic carbonic anhydrase-related protein VIII (CARP VIII) has been found in deuterostomes and the phylum Placozoa. I isolated a cDNA encoding a noncatalytic CARP from the mantle of the pearl oyster Pinctada fucata. The polypeptide (CARP-1) predicted from the nucleotide sequence shares 44-60% identity with known CARP VIII sequences, and its phylogenetic analysis showed that P. fucata formed a single group with deuterostome invertebrates. However, since CARP VIII sequences are not identified in protostomes, these results suggest that CARP-1 may have originated in molluscs independently from deuterostome CARP VIII sequences.
  • A novel nacre protein N19 in the pearl oyster Pinctada fucata, Masato Yano, Kouhei Nagai, Koichi Morimoto, Hiroshi Miyamoto, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 362(1), 158 - 163, Oct. 2007 , Refereed
    Summary:A novel 19 kDa protein, which was named N19, was isolated from the nacreous layer of the pearl oyster Pinetada fucata. N19 is one of predominant proteins found in the water-insoluble fraction of the nacreous layer. MALDI-TOF/TOF analysis indicated that the three trypsin-digested peptides (791.45, 824.42, and 1118.65 m/z) corresponded to the amino acid sequences predicted from a cDNA isolated from a mantle cDNA library of P. fucata. Northern blot analysis revealed that the N19 mRNA was a little more abundant in the pallial region than the edge region, in the mantle. In CaCO3 precipitation assay, the recombinant N19 protein inhibited the crystallization of CaCO3. These results indicate that N19 is localized in the nacre and plays a negative regulatory role in calcification in the pearl oyster. (C) 2007 Elsevier Inc. All rights reserved.
  • Tyrosinase localization in mollusc shells, Kouhei Nagai, Masato Yano, Koichi Morimoto, Hiroshi Miyamoto, COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 146(2), 207 - 214, Feb. 2007 , Refereed
    Summary:In molluscan shellfish, pigmentation is frequently observed in the calcified shell, but the molecular basis of this process is not understood. Here, we report two tyrosinase proteins (Pfty1 and Pfty2) found in the prismatic shell layer of the pearl oyster Pinctada fucata; this layer is recognized as the pigmented region in P. fucata. The protein sequences were deduced from the corresponding cDNAs and confirmed by MALDI-TOF/TOF analysis. The sequences suggest that both tyrosinases have two copper-binding sites in similar N-terminal domains that are homologous to tyrosinases of cephalopods and hemocyanins of gastropods. In turn, this suggests that bivalve tyrosinases are evolved from a common ancestral copper-binding protein in the mollusc. Pfty1 and Pfty2 were specifically expressed in the mantle, and their expression in the mantle is different from each other, suggesting that these tyrosinases have distinctive roles in melanogenesis in shells. (c) 2006 Elsevier Inc. All rights reserved.
  • Shematrin: A family of glycine-rich structural proteins in the shell of the pearl oyster Pinctada fucata, M Yano, K Nagai, K Morimoto, H Miyamoto, COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 144(2), 254 - 262, Jun. 2006 , Refereed
    Summary:Random sequencing of molecules from a cDNA library constructed from mantle mRNA of the pearl oyster Pinctada fucata was used to obtain information on organic matrix proteins in the shell. In the determined sequences, we identified 7 distinct cDNAs encoding similar glycine-rich domains. Complete sequence analysis of these cDNAs showed that the predicted sequences of the proteins, which we named shematrins, possessed similar domains comprising repeat sequences of two or more glycines, followed by a hydrophobic amino acid. In addition, in shematrin-1, -2 and -3, a repeat domain designated as XG(n)X (where X is a hydrophobic amino acid) was conserved. It is of further note that all the shematrin proteins have RKKKY, RRKKY or RRRKY as their C-terminal sequence. According to northern blot analysis, all shematrins are exclusively expressed in the mantle, and particularly in the edge region of the mantle-, furthermore, peptide fragments similar to shematrin-1 and -2 were detected in the prismatic layer of shells by MALDI-TOF/TOF MS analysis. These findings suggest that many of shematrins are synthesized in the mantle edge and secreted into the prismatic layer of the shell, where the protein family is thought to provide a framework for calcification. (c) 2006 Elsevier Inc. All rights reserved.
  • The carbonic anhydrase domain protein nacrein is expressed in the epithelial cells of the mantle and acts as a negative regulator in calcification in the mollusc Pinctada fucata, H Miyamoto, F Miyoshi, J Kohno, ZOOLOGICAL SCIENCE, ZOOLOGICAL SCIENCE, 22(3), 311 - 315, Mar. 2005 , Refereed
    Summary:Signals and organic matrix proteins secreted from the mantle are critical for the development of shells in molluscs. Nacrein, which is composed of a carbonic anhydrase domain and a Gly-X-Asn repeat domain, is one of the organic matrix proteins that accumulates in shells. In situ hybridization revealed that nacrein was expressed in the outer epithelial cells of the mantle of the pearl oyster Pinctada fucata. The recombinant nacrein protein inhibited the precipitation of calcium carbonate from a saturated solution containing CaCl2 and NaHCO3, indicating that it can act as a negative regulator for calcification in the shells of molluscs. Because deletion of the Gly-X-Asn repeat domain of nacrein had a significant effect on the ability of nacrein to inhibit the precipitation of calcium carbonate, it is conceivable that the repeat domain has a primary role in the inhibitory function of nacrein in shell formation. Together these studies suggest that nacrein functions as a negative regulator in calcification in the extrapallial space between the shell and the mantle by inhibiting the precipitation of CaCO3.
  • Various forms of carbonic anhydrase found in mollusc, Hiroshi Miyamoto, Yukihiko Naka, Kiyotaka Kajihara, ZOOLOGICAL SCIENCE, ZOOLOGICAL SCIENCE, 21(12), 1344 - 1344, Dec. 2004 , Refereed
  • Similarities in the structure of nacrein, the shell-matrix protein, in a bivalve and a gastropod, H Miyamoto, M Yano, T Miyashita, JOURNAL OF MOLLUSCAN STUDIES, JOURNAL OF MOLLUSCAN STUDIES, 69, 87 - 89, Feb. 2003 , Refereed
  • Isolation and characterization of an elongation factor-1 alpha gene in Porphyra yezoensis (Rhodophyta), S Fukuda, Y Kitade, H Miyamoto, S Nagashima, S Takahashi, T Ohba, K Asada, Kato, I, N Saga, JOURNAL OF APPLIED PHYCOLOGY, JOURNAL OF APPLIED PHYCOLOGY, 15(1), 81 - 86, Jan. 2003 , Refereed
    Summary:A gene of Porphyra yezoensis, coding for the translation elongation factor 1alpha (EF-1alpha), was isolated from a P. yezoensis genomic library. The coding of 1347 nucleotides encodes a polypeptide of 449 amino acids which exhibits sequence similarity as the known EF-1alpha. An intron is located in the 5' untranslated region. Comparison of the deduced amino acid sequence showed higher similarity to the Porphyra purpurea EF-1alpha tef-c (97%) than to the P. purpurea EF-1alpha tef-s (61%). The mRNA was detected both in the leafy gametophyte and filamentous sporophyte by RT-PCR. The nucleotide sequence data reported in this paper will appear in the DDBJ/EMBL/GenBank databases under accession number AB098024.
  • Analysis of genes expressed in the mantle of oyster Crassostrea gigas, H Miyamoto, M Hamaguchi, K Okoshi, FISHERIES SCIENCE, FISHERIES SCIENCE, 68(3), 651 - 658, Jun. 2002 , Refereed
    Summary:total of 347 cDNA were isolated from the mantle of the oyster Crassostrea gigas by the suppression subtractive hybridization method. By northern blot analysis, we found the mRNA sequences of the several cDNA were highly expressed in the mantle. A total of 61 sequences showed close similarities to known sequences, and they were classified into seven groups: (i) protein synthesis; (ii) cytoskeleton; (iii) signal transduction; (iv) extracellular matrix; (v) metabolism; (vi) transcription factors; and (vii) others. Number 64 cDNA was more similar to the actin of Placopecten magellanicus than C. gigas, indicating that C. gigas has two isotypes of actin genes. This work is the first step to clarify functional activities of the mantle at the molecular level.
  • Complementary DNA cloning and characterization of pearlin, a new class of matrix protein in the nacreous layer of oyster pearls, T Miyashita, R Takagi, M Okushima, S Nakano, H Miyamoto, E Nishikawa, A Matsushiro, MARINE BIOTECHNOLOGY, MARINE BIOTECHNOLOGY, 2(5), 409 - 418, Sep. 2000 , Refereed
    Summary:Calcified shell layer is composed of two polymorphs of CaCO3, aragonite or calcite, and an organic matrix. The organic matrix consists of EDTA-soluble and insoluble fractions. These fractions are thought to regulate the formation of the elaborate shell structure. After decalcification of powdered pearl with 0.3 M EDTA, an EDTA-insoluble fraction was extracted with 0.3 M EDTA/8 M urea. This extraction step enabled us to purify a new class of EDTA-insoluble protein, Pearlin, almost homogeneously. Pearlin has a molecular weight of about 15 kDa and contains a sulfated mucopolysaccharide. We cloned the complementary DNA coding for Pearlin and deduced its complete amino acid sequence. Sequence analysis reveals that Pearlin is composed of 129 amino acids with a high proportion of Gly (10.8%;), Tyr (10.0%), Cys (8.5%), Asn (7.7%), Asp (7.7%), and Arg (7.7%). Northern blot analysis showed that Pearlin messenger RNA was expressed specifically in mantle epithelium. From the sequencing data, Pearlin was shown to be quite different from the fibrous protein rich in Ala and Gly. The function of this protein in biomineralization is discussed.
  • Cloning and expression of the mouse Pse gene encoding a novel Ets family member, N Yamada, Y Tamai, H Miyamoto, M Nozaki, GENE, GENE, 241(2), 267 - 274, Jan. 2000 , Refereed
    Summary:Human prostate-specific Ets (hPSE) is a novel Ets transcription factor and is exclusively expressed in human prostate glandular epithelium. To explore the role of PSE, we cloned the mouse Pse (mPse) and examined its pattern of expression. A sequence analysis indicated that mPse contains a conserved carboxy-terminal ETS DNA-binding domain and central Pointed domain, and the overall amino acid sequence shares 86% identity with that of hPSE. The ETS DNA-binding domain is highly conserved between human and mouse (98.8% sequence identity) and is similar to Drosophila dets4 (76.7% identity), but not similar to other Ets factors. A Northern blotting analysis revealed that mPse shows organ-specific expression. An in situ hybridization analysis of the prostate and intestine showed that mPse transcripts were present in their epithelial cells, mPse transactivates the promoter of the MASPIN gene in transient transfection assay. These results suggest that mPse encodes a novel Ets family member and is expressed in epithelial cells of restricted organs. (C) 2000 Elsevier Science B.V. All rights reserved.
  • A carbonic anhydrase from the nacreous layer in oyster pearls, H Miyamoto, T Miyashita, M Okushima, S Nakano, T Morita, A Matsushiro, 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, 93(18), 9657 - 9660, Sep. 1996 , Refereed
    Summary:It is believed that the polymorphism observed in calcium carbonate crystals, such as aragonite and calcite in mollusk shells, is controlled by organic matrix proteins secreted from the mantle epithelia. However, the fine structures of these proteins are still unknown, and to understand the molecular mechanisms of mineralization process, detailed structural analyses of the organic matrix proteins are essential, For this, we have carried out purification, characterization, and cDNA cloning of nacrein, which is a soluble organic matrix protein in the nacreous layer of oyster pearls, Northern blot analysis showed that the nacrein transcript was specifically expressed in mantle pallial, Analysis of the deduced amino acid sequence revealed that the protein contained two functional domains: one was a carbonic anhydrase and another was a Gly-Xaa-Asn (Xaa = Asp, Asn, or Glu) repeat domain; however, the carbonic anhydrase domain was split into two subdomains with insertion of the Gly-Xaa-Asn repeat domain between them, Our findings suggest that nacrein actually functions as a matrix protein whose repeated Gly-Xaa-Asn domain possibly binds calcium and as a carbonic anhydrase that catalyzes the HCO3- formation, thus participating in calcium carbonate crystal formation of the nacreous layer.
  • Molecular characterization of the Drosophila Mo25 gene, which is conserved among Drosophila, mouse, and yeast, M Nozaki, Y Onishi, S Togashi, H Miyamoto, DNA AND CELL BIOLOGY, DNA AND CELL BIOLOGY, 15(6), 505 - 509, Jun. 1996 , Refereed
    Summary:To study the general physiological role of the Mo25 gene, which has been cloned from mouse cleavage-stage embryos, we isolated a Drosophila equivalent, dMo25, cDNA from an embryo cDNA library, The 2,222 nucleotides contained a single open reading frame encoding a polypeptide of 339 amino acid residues with a calculated molecular mass of 39,278 daltons, The deduced amino acid sequence of the dMo25 cDNA had 69.3% identity with mouse Mo25, A homology search revealed that these were similar to a protein encoded in an open reading frame near the calcineurin B subunit gene on chromosome XI in Saccharomyces cerevisiae. In particular, the carboxy-terminal region was highly conserved in Drosophila, mouse, and yeast. The dMo25 gene was mapped to the left arm of the third chromosome at 73AB, and 2.3- and 1,8-kb mRNA bands were detected during development and in adult Drosophila. Conservation of the gene structure and the wide expression profile indicated that the function of the gene is likely to be fundamental in many cell types as well as during development.
  • Genetic interactions of pokkuri with seven in absentia, tramtrack and downstream components of the sevenless pathway in R7 photoreceptor induction in Drosophila melanogaster, D Yamamoto, Nihonmatsu, I, T Matsuo, H Miyamoto, S Kondo, K Hirata, Y Ikegami, ROUXS ARCHIVES OF DEVELOPMENTAL BIOLOGY, ROUXS ARCHIVES OF DEVELOPMENTAL BIOLOGY, 205(5-6), 215 - 224, Feb. 1996 , Refereed
    Summary:The sevenless (sev) cascade plays an inductive role in formation of the R7 photoreceptor, whilst the pokkuli (pok) and tramtrack (ttk) gene products are known to repress R7 induction in developing ommatidia of Drosophila melanogaster. To elucidate how these positive and negative signalling mechanisms co-operate in the normal fate determination of R7, genetic interactions of mutations in the pok locus with ttk and downstream elements of sev including Gap1, raf1, rolled (rl) and seven in absentia (sina) were examined. The eye phenotype of a weak hypomorph, pok(15), was enhanced dominantly by Gap1(mip), a recessive mutation in a gene encoding a down-regulator of Ras1, producing multiple R7 in ommatidia. Ras1 has been reported to activate rl-encoded mitrogen-activated protein (MAP) kinase via Raf1 that is associated physically with Ras1. Ommatidia of raf1(c110) and rl(2)/rl(EMS64) typically lacked R7 and a few outer photoreceptors. The pok(1) mutation suppressed dominantly the raf1(c110) and rl2/rl(EMS64) eye phenotypes, allowing single R7 cells to develop in ommatidia. The raf1(c110) mutation improved adult viability of pok(1) homozygotes. An in vitro experiment demonstrated that MAP kinase phosphorylates Pok protein. Ttk is a transcriptional repressor which binds to the regulatory sequence upstream of the fushi-tarazu (ftz), even skipped (eve) and engrailed (en) coding region. A reduced activity in ttk resulted in enhancement of the pok phenotype. ttk mutations produced extra R7 cells even in sina homozygotes whilst the pok mutation did not. This result indicates that Ttk represses R7 induction downstream of the sites where Pok and Sina function.
  • CANOE ENCODES A NOVEL PROTEIN CONTAINING A GLGF/DHR MOTIF AND FUNCTIONS WITH NOTCH AND SCABROUS IN COMMON DEVELOPMENTAL PATHWAYS IN DROSOPHILA, H MIYAMOTO, NIHONMATSU, I, S KONDO, R UEDA, S TOGASHI, K HIRATA, Y IKEGAMI, D YAMAMOTO, GENES & DEVELOPMENT, GENES & DEVELOPMENT, 9(5), 612 - 625, Mar. 1995 , Refereed
    Summary:The canoe(misty1) (cno(mis1)) mutation was isolated by virtue of its severe rough eye phenotype from similar to 500 fly lines, each harboring a single autosomal insertion of a P element (Bm Delta w). Excision of the P element generated a lethal, null allele, cno(mis10), together with many revertants with normal eye morphology. Ommatidia homozygous for cno(mis10), produced in an otherwise wild-type eye by somatic recombination, typically contain a reduced number of outer photoreceptors. Some cno(mis1) homozygous adults bear extra macrochaetes on the head, notum, humerus and/or scutellum. cno(mis1) hemizygotes often show conspicuous wing phenotypes such as a notched blade and the loss of a cross vein. The sequence of cno cDNA clones isolated from an embryonic cDNA library revealed a long open reading frame that potentially encodes a 1893-amino-acid protein with the GLGF/DHR motif, a conserved sequence in Discs large, Dishevelled, and some other proteins associated with cellular junctions. Flies doubly mutant for cno(mis1) and scabrous(1) (sca(1)) and those for cno(mis1) and the split (spl) allele of Notch (N) always have rumpled wings curved downward. The spl; cno(mis1) double mutant flies also exhibit a ''giant socket'' phenotype. These phenotypes are rarely observed in flies singly mutant for either cno(mis1), sca(1) or spl. The wing vein gaps caused by Abruptex(1), a N allele producing an activated form of N protein, are dominantly suppressed by cno(mis1). Heterozygosity for shaggy and myospheroid promotes formation of extra wing veins in cno(mis1) homozygotes. The genetic interactions suggest that cno participates with members of the N pathway in regulating adhesive cell-cell interactions for the determination of cell fate.
  • MOLECULAR-CLONING OF A NOVEL MESSENGER-RNA SEQUENCE EXPRESSED IN CLEAVAGE STAGE MOUSE EMBRYOS, H MIYAMOTO, A MATSUSHIRO, M NOZAKI, MOLECULAR REPRODUCTION AND DEVELOPMENT, MOLECULAR REPRODUCTION AND DEVELOPMENT, 34(1), 1 - 7, Jan. 1993 , Refereed
    Summary:In an approach to study genes transcribed during early mouse development, a cDNA library was constructed from poly(A) RNA isolated from the 8-cell morula. The cDNA library was differentially screened with labelled cDNA probes synthesized on poly(A) RNA isolated from the 8-cell morula or unfertilized eggs. Six clones which increased in abundance in the 8-cell morula were selected and further analyzed. Sequencing analyses showed that some of these clones corresponded to RNA transcripts from B1 and B2 repetitive sequences, as well as mRNA for cytochrome C oxidase I and NADH dehydrogenase III derived from the mitochondrial genome. One clone was not identical to any known sequences. The unidentified sequence (MO25) was found at low levels in the unfertilized egg, but increased at the 2-cell stage. The predicted amino acid sequence revealed that the MO25 gene may encode a Ca2+ binding protein.
  • STRUCTURE AND EXPRESSION OF THE GENE ENCODING MOUSE T-COMPLEX POLYPEPTIDE (TCP-1), H KUBOTA, K WILLISON, A ASHWORTH, M NOZAKI, H MIYAMOTO, H YAMAMOTO, A MATSUSHIRO, T MORITA, GENE, GENE, 120(2), 207 - 215, Oct. 1992 , Refereed
    Summary:The nucleotide (nt) sequence of the structural gene (Tcp-1) encoding mouse t-complex polypeptide 1 (TCP-1) has been determined. The nt sequence extending to 10 043 bp shows that the Tcp-1 gene is divided into 12 exons, 11 introns and 5'-and 3'-flanking regions. The Tcp-1 gene has a tight cluster of major transcription start points (tsp). Two GC boxes, one CCAAT box and some other possible regulatory elements are located in the region upstream from the tsp, but no TATA box was found. Extending from the 5'-flanking region to the first intron, a CpG dinucleotide-rich cluster is located. In addition, Tcp-1 gene transcripts in mouse organs, embryos and cultured cells were analyzed by Northern blotting. The Tcp-1 mRNA is enriched not only in testes, but also in early post-implantation embryos and some cultured cell lines, as compared with mouse organs other than the testis. The amount of Tcp-1 mRNA in embryos decreases during development. These results suggest that the expression of the Tcp-1 gene may be regulated spatially and temporally in embryonic and adult mice by transcriptional control or by mRNA stability.
  • MOLECULAR-CLONING AND CHARACTERIZATION OF CDNA-ENCODING MOUSE CYTOKERATIN-NO-19, Y ICHINOSE, K HASHIDO, H MIYAMOTO, T NAGATA, M NOZAKI, T MORITA, A MATSUSHIRO, GENE, GENE, 80(2), 315 - 323, Aug. 1989 , Refereed

Books etc

  • Genetic and molecular analysis of a canoe, a pattern formation locus of Drosophila melanogaster, MIYAMOTO Hiroshi, Joint author,   1996

Conference Activities & Talks

  • Identification of calcareous tube protein genes in the serpulid Spirobranchus kraussii., MIYAMOTO Hiroshi, International congress of zoology.,   2016 11 14
  • Molecular analyses of cytoskeletal proteins expressed in the mantle of the pacific oyster Crassostrea gigas, International Marine Biotechnology Conference 2005,   2005 06 , International Marine Biotechnology Conference 2005
  • Analysis of carbonic anhydrase-like genes expressed in the mantle of mollusc, VIII International Congress on Medical and Applied Malacology,   2004 11 , VIII International Congress on Medical and Applied Malacology
  • Two novel glycine-rich proteins expressed in the mantle of the pacific oyster,   2004 09
  • A novel carbonic anhydrase found in pacific oyster Crassostrea gigas,   2004 09

Misc

  • Induction of prophages of enterohemorrhagic Escherichia coli O157 : H7 with norfloxacin, A Matsushiro, K Sato, H Miyamoto, T Yamamura, T Honda, JOURNAL OF BACTERIOLOGY, 181, 7, 2257, 2260,   1999 04
    Summary:Norfloxacin (NFLX) caused induction of prophages VT1 and VT2 of enterohemorrhagic Escherichia coli O157 at subinhibitory concentrations. In time course experiments, we observed the folloing, sequential events: upon induction, the phage genomes underwent multiplication; the amount of sa genes increased; and subsequently, large quantities of toxins VT1 and VT2 were produced. Further studies showed that the molecular mechanism of prophage induction is closely related to the RecA system since the prophage VT2 was not induced with NFLX in a recA mutant strain.
  • Sequence analysis of Stx2-converting phage VT2-Sa shows a great divergence in early regulation and replication regions, Hiroshi Miyamoto, Wataru Nakai, Naoto Yajima, Akemi Fujibayashi, Tomonori Higuchi, Koki Sato, Aizo Matsushiro, DNA Research, 6, 4, 235, 240,   1999 , 10.1093/dnares/6.4.235
    Summary:In enterohemorrhagic Escherichia coli, Shiga toxin is produced by lysogenic prophages. We have isolated the prophage VT2-Sa that is responsible for production of Shiga toxin type 2 protein, and determined the complete nucleotide sequence of this phage DNA. The entire DNA sequence consisted of 60,942 bp, exhibiting marked similarity to the 933W phage genome. However, several differences were observed in the immunity and replication regions, where cI, cI, cIII, N, cro, O, and P genes were present: Predicted amino acid sequences of N, cI, cro, O and P in the VT2-Sa genome did not show significant similarity to the counterparts of the 933W genome however its ci showed higher similarity to λ. Furthermore, O and P closely resembled those of phage HK022. These observations suggest that the various degrees of homology observed in the immunity and replication regions of VT2-Sa could have resulted from frequent recombination events among the lambdoid pliages, and that these regions play a key role as a functional unit for phage propagation in competition with other lambdoid phages.
  • A carbonic anhydrase from the nacreous layer in oyster pearls, H Miyamoto, T Miyashita, M Okushima, S Nakano, T Morita, A Matsushiro, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 93, 18, 9657, 9660,   1996 09 , 10.1073/pnas.93.18.9657
    Summary:It is believed that the polymorphism observed in calcium carbonate crystals, such as aragonite and calcite in mollusk shells, is controlled by organic matrix proteins secreted from the mantle epithelia. However, the fine structures of these proteins are still unknown, and to understand the molecular mechanisms of mineralization process, detailed structural analyses of the organic matrix proteins are essential, For this, we have carried out purification, characterization, and cDNA cloning of nacrein, which is a soluble organic matrix protein in the nacreous layer of oyster pearls, Northern blot analysis showed that the nacrein transcript was specifically expressed in mantle pallial, Analysis of the deduced amino acid sequence revealed that the protein contained two functional domains: one was a carbonic anhydrase and another was a Gly-Xaa-Asn (Xaa = Asp, Asn, or Glu) repeat domain; however, the carbonic anhydrase domain was split into two subdomains with insertion of the Gly-Xaa-Asn repeat domain between them, Our findings suggest that nacrein actually functions as a matrix protein whose repeated Gly-Xaa-Asn domain possibly binds calcium and as a carbonic anhydrase that catalyzes the HCO3- formation, thus participating in calcium carbonate crystal formation of the nacreous layer.
  • Molecular characterization of the Drosophila Mo25 gene, which is conserved among Drosophila, mouse, and yeast, M Nozaki, Y Onishi, S Togashi, H Miyamoto, DNA AND CELL BIOLOGY, 15, 6, 505, 509,   1996 06
    Summary:To study the general physiological role of the Mo25 gene, which has been cloned from mouse cleavage-stage embryos, we isolated a Drosophila equivalent, dMo25, cDNA from an embryo cDNA library, The 2,222 nucleotides contained a single open reading frame encoding a polypeptide of 339 amino acid residues with a calculated molecular mass of 39,278 daltons, The deduced amino acid sequence of the dMo25 cDNA had 69.3% identity with mouse Mo25, A homology search revealed that these were similar to a protein encoded in an open reading frame near the calcineurin B subunit gene on chromosome XI in Saccharomyces cerevisiae. In particular, the carboxy-terminal region was highly conserved in Drosophila, mouse, and yeast. The dMo25 gene was mapped to the left arm of the third chromosome at 73AB, and 2.3- and 1,8-kb mRNA bands were detected during development and in adult Drosophila. Conservation of the gene structure and the wide expression profile indicated that the function of the gene is likely to be fundamental in many cell types as well as during development.
  • Genetic interactions of pokkuri with seven in absentia, tramtrack and downstream components of the sevenless pathway in R7 photoreceptor induction in Drosophila melanogaster, D Yamamoto, Nihonmatsu, I, T Matsuo, H Miyamoto, S Kondo, K Hirata, Y Ikegami, ROUXS ARCHIVES OF DEVELOPMENTAL BIOLOGY, 205, 5-6, 215, 224,   1996 02 , 10.1007/BF00365799
    Summary:The sevenless (sev) cascade plays an inductive role in formation of the R7 photoreceptor, whilst the pokkuli (pok) and tramtrack (ttk) gene products are known to repress R7 induction in developing ommatidia of Drosophila melanogaster. To elucidate how these positive and negative signalling mechanisms co-operate in the normal fate determination of R7, genetic interactions of mutations in the pok locus with ttk and downstream elements of sev including Gap1, raf1, rolled (rl) and seven in absentia (sina) were examined. The eye phenotype of a weak hypomorph, pok(15), was enhanced dominantly by Gap1(mip), a recessive mutation in a gene encoding a down-regulator of Ras1, producing multiple R7 in ommatidia. Ras1 has been reported to activate rl-encoded mitrogen-activated protein (MAP) kinase via Raf1 that is associated physically with Ras1. Ommatidia of raf1(c110) and rl(2)/rl(EMS64) typically lacked R7 and a few outer photoreceptors. The pok(1) mutation suppressed dominantly the raf1(c110) and rl2/rl(EMS64) eye phenotypes, allowing single R7 cells to develop in ommatidia. The raf1(c110) mutation improved adult viability of pok(1) homozygotes. An in vitro experiment demonstrated that MAP kinase phosphorylates Pok protein. Ttk is a transcriptional repressor which binds to the regulatory sequence upstream of the fushi-tarazu (ftz), even skipped (eve) and engrailed (en) coding region. A reduced activity in ttk resulted in enhancement of the pok phenotype. ttk mutations produced extra R7 cells even in sina homozygotes whilst the pok mutation did not. This result indicates that Ttk represses R7 induction downstream of the sites where Pok and Sina function.
  • CANOE ENCODES A NOVEL PROTEIN CONTAINING A GLGF/DHR MOTIF AND FUNCTIONS WITH NOTCH AND SCABROUS IN COMMON DEVELOPMENTAL PATHWAYS IN DROSOPHILA, H MIYAMOTO, NIHONMATSU, I, S KONDO, R UEDA, S TOGASHI, K HIRATA, Y IKEGAMI, D YAMAMOTO, GENES & DEVELOPMENT, 9, 5, 612, 625,   1995 03 , 10.1101/gad.9.5.612
    Summary:The canoe(misty1) (cno(mis1)) mutation was isolated by virtue of its severe rough eye phenotype from similar to 500 fly lines, each harboring a single autosomal insertion of a P element (Bm Delta w). Excision of the P element generated a lethal, null allele, cno(mis10), together with many revertants with normal eye morphology. Ommatidia homozygous for cno(mis10), produced in an otherwise wild-type eye by somatic recombination, typically contain a reduced number of outer photoreceptors. Some cno(mis1) homozygous adults bear extra macrochaetes on the head, notum, humerus and/or scutellum. cno(mis1) hemizygotes often show conspicuous wing phenotypes such as a notched blade and the loss of a cross vein. The sequence of cno cDNA clones isolated from an embryonic cDNA library revealed a long open reading frame that potentially encodes a 1893-amino-acid protein with the GLGF/DHR motif, a conserved sequence in Discs large, Dishevelled, and some other proteins associated with cellular junctions. Flies doubly mutant for cno(mis1) and scabrous(1) (sca(1)) and those for cno(mis1) and the split (spl) allele of Notch (N) always have rumpled wings curved downward. The spl; cno(mis1) double mutant flies also exhibit a ''giant socket'' phenotype. These phenotypes are rarely observed in flies singly mutant for either cno(mis1), sca(1) or spl. The wing vein gaps caused by Abruptex(1), a N allele producing an activated form of N protein, are dominantly suppressed by cno(mis1). Heterozygosity for shaggy and myospheroid promotes formation of extra wing veins in cno(mis1) homozygotes. The genetic interactions suggest that cno participates with members of the N pathway in regulating adhesive cell-cell interactions for the determination of cell fate.
  • Molecular cloning of a novel mRNA sequence expressed in cleavage stage mouse embryos., Molecular Reproduction & Development, 34, 01

Research Grants & Projects

  • The Other Research Programs, Mechanism of calcification in invertebrates
  • The Other Research Programs, Signal transduction regulating cell differentiation