Kyushu University Academic Staff Educational and Research Activities Database
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NOZOMU OKINO Last modified date:2021.06.15

Associate Professor / Molecular Bioscience
Department of Bioscience and Biotechnology
Faculty of Agriculture

Graduate School
Undergraduate School

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 Reseacher Profiling Tool Kyushu University Pure
Academic Degree
Country of degree conferring institution (Overseas)
Field of Specialization
Marine Resource Chemistry, Biochemistry, Microbiology
ORCID(Open Researcher and Contributor ID)
Total Priod of education and research career in the foreign country
Outline Activities
My research projects are as follows:
1. Search and Utilization of New Marine Resources
(1). Molecular cloning and functional analyses of genes from marine microbes and marine invertebrates
(2). Utilization of marine bacteria for glycobiology and glycotechnology
(3). Purification and characterization of novel sphingolipid-degrading enzyme inhibitors from marine resources
(4). Isolation, characterization and cDNA cloning of novel sphingolipid-degrading enzymes and tumor-specific lectin from marine invertebrates (jellyfish, starfish etc.)
(5). Purification, characterization and gene cloning of sphingolipid-degrading enzymes from marine bacteria
2. Molecular Mechanism for Inversion of Pathogens and Expression of Their Phathogenecity
(1). Expression cloning of hemolysin related to fish disease
(2). Functional analyses of bacterial sphingolipid-degrading enzymes
3. Glycobiology and Sphingolipid Technology
(1). Isolation of sphingolipid-degrading bacteria from patients with atopic dermatitis
(2). A novel but highly conserved gene family of neutral/alkaline ceramidases
(3). Molecular evolution of endoglycoceramidase
(4). Sphingolipid-mediated signal transduction
Research Interests
  • Analysis of sphingolipid metabolizing enzymes
    keyword : Sphingolipid, enzyme, ceramide
    2003.04Analysis of sphingolipid metabolizing enzymes.
  • Marine Biotechnology
    keyword : Poly unsaturated fatty acid, Lipid binding protein
    2003.04Analysis of sphingolipid metabolizing enzymes.
Academic Activities
1. Biological Function and the Survival of Humans
Discovery of a New Ceramidase Family
Nozomu Okino
1. Makoto Ito, Nozomu Okino, Motohiro Tani, New insight into the structure, reaction mechanism, and biological functions of neutral ceramidase, Biochimica et Biophysica Acta, 1841, 682–691, 2014.05.
2. The critical reason for production of ceramidase in Pseudomonas aeruginosa
Nozomu Okino.
1. Nozomu Okino, Mengbai Li, Qingjun Qu, Tomoko Nakagawa, Yasuhiro Hayashi, Mitsufumi Matsumoto, Yohei Ishibashi, Makoto Ito, Two bacterial glycosphingolipid synthases responsible for the synthesis of glucuronosylceramide and alpha-galactosylceramide, Journal of Biological Chemistry, 10.1074/jbc.RA120.013796, 295, 31, 10709-10725, 2020.07, Bacterial glycosphingolipids such as glucuronosylceramide and galactosylceramide have been identified as ligands for invariant natural killer T cells and play important roles in host defense. However, the glycosphingolipid synthases required for production of these ceramides have not been well-characterized. Here, we report the identification and characterization of glucuronosylceramide synthase (ceramide UDP-glucuronosyltransferase [Cer-GlcAT]) in Zymomonas mobilis, a Gram-negative bacterium whose cellular membranes contain glucuronosylceramide. On comparing the gene sequences that encode the diacylglycerol GlcAT in bacteria and plants, we found a homologous gene that is widely distributed in the order Sphingomonadales in the Z. mobilis genome. We first cloned the gene and expressed it in Escherichia coli, followed by protein purification using nickel-Sepharose affinity and gel filtration chromatography. Using the highly enriched enzyme, we observed that it has high glycosyltransferase activity with UDP-glucuronic acid and ceramide as sugar donor and acceptor substrate, respectively. Cer-GlcAT deletion resulted in a loss of glucuronosylceramide and increased the levels of ceramide phosphoglycerol, which was expressed in WT cells only at very low levels. Furthermore, we found sequences homologous to Cer-GlcAT in Sphingobium yanoikuyae and Bacteroides fragilis, which have been reported to produce glucuronosylceramide and α-galactosylceramide, respectively. We expressed the two homologs of the cer-glcat gene in E. coli and found that each gene encodes Cer-GlcAT and Cer-galactosyltransferase, respectively. These results contribute to the understanding of the roles of bacterial glycosphingolipids in host-bacteria interactions and the function of bacterial glycosphingolipids in bacterial physiology..
2. Nozomu Okino, Hiroyoshi Wakisaka, Yohei Ishibashi, Makoto Ito, Visualization of Endoplasmic Reticulum and Mitochondria in Aurantiochytrium limacinum by the Expression of EGFP with Cell Organelle-Specific Targeting/Retaining Signals, Marine Biotechnology, 10.1007/s10126-018-9795-7, 1-11, 2018.01.
3. Nozomu Okino, Makoto Ito, Molecular mechanism for sphingosine-induced Pseudomonas ceramidase expression through the transcriptional regulator SphR, Scientific Reports, 6, 38797, 2016.12.
4. Inoue T, Okino N, Kakuta Y, Hijikata A, Okano H, Goda HM, Tani M, Sueyoshi N, Kambayashi K, Matsumura H, Kai Y, Ito M., Mechanistic insights into the hydrolysis and synthesis of ceramide by neutral ceramidase., J Biol Chem, 284(14):9566-9577, 2009.04.
5. N. Okino and M. Ito, Ceramidase Enhances Phospholipase C-induced Hemolysis by Pseudomonas aeruginosa, J. Biol. Chem. , 282, 6021-6030, 2007.03.
6. H. Monjusho, N. Okino, M. Tani, M. Maeda, M. Yoshida, and M. Ito, A Neutral Ceramidase Homologue of Dictyostelium discoideum Exhibits an Acidic pH Optimum, Biochem. J., 10.1042/BJ20030652, 376, 473-479, 376, pp473-479, 2003.12.
7. X. He, N. Okino, R. Dhami, A. Dagan, S. Gatt, H. Schulze, K. Sandhoff, and E. H. Schuchman, Purification and Characterization of Recombinant, Human Acid Ceramidase, J. Biol. Chem., 278, pp32978-32986, 2003.08.
8. N. Okino, X. He, S. Gatt, K. Sandhoff, M. Ito, and E. H. Schuchman, The Reverse Activity of Human Acid Ceramidase, J. Biol. Chem., 10.1074/jbc.M303310200, 278, 32, 29948-29953, 278, pp29948-29953, 2003.08.
Works, Software and Database
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1. Nozomu Okino, Makoto Ito, Identification and functional analysis of the bacterial glucuronosylceramide synthase, 11th Asian Community of Glycoscience and Glycotechnology Conference, 2019.11.
2. Hayato Nyunoya, Nozomu Okino, Yohei Ishibashi, Makoto Ito, Evaluation of delta5 desaturase activity in marine fish cells, Marine Biotechnology Conference 2019, 2019.09.
3. Nozomu Okino, Hiroyoshi Wakisaka, Yohei Ishibashi, Makoto Ito, Visualization of endoplasmic reticulum and mitochondria in Aurantiochytrium limacinum ATCC MYA-1381, First International Conference on Labyrinthulean Protists (ICoLP), 2019.08.
4. Nozomu Okino, Mengbai Li, Yohei Ishibashi, Makoto Ito, Identification and functional characterization of ceramide UDP-glucronosyltransferase in Zymomonas mobilis, 60th International Converence on the Bioscience of Lipids, 2019.06.
5. Nozomu Okino, Makoto Ito, Identification and functional analysis of diacylglycerol glucuronosyltransferase in Pseudomonas aeruginosa, 2nd Japan-Korea Lipid Joint Symposium, 2018.09.
6. Nozomu Okino, Makoto Ito, Transcriptional regulation of Pseudomonas ceramidase through the sphingosine-specific transcriptional regulator SphR
, 58th International Conference on the Bioscience of Lipids, 2017.09.
7. 沖野 望, Yoshimitsu Kakuta, 鵜木(加藤)陽子, 大坪 怜央, 石橋 洋平, 小林 宇太郎, makoto kimura, 伊東 信, Crystal structures of unique glycosphingolipid-degrading enzymes, The 7thACGG conference, 2015.11.
8. 沖野 望, 伊東 信, Marine biotechnology: New understanding and developments, PKNU – KU Joint Symposium SMART Oceans and Fisheries, 2015.10.
9. 沖野 望, 伊東 信, Identification of a transcriptional regulator SphR for ceramidase expression in Pseudomonas aeruginosa, 第10回スフィンゴテラピィ研究会, 2015.06.
Educational Activities
Faculty of Agriculture
(Animal Production Science)

Marine Resource Chemistry
Science English I,II

Graduate School
(Bioscience and Biotechnology)
Advanced Marine Biochemistry
Molecular Biosciences