Tomomitsu Hatakeyama

Summary

Affiliation: Nagasaki University
Country: Japan

Publications

  1. ncbi request reprint Antibacterial activity of peptides derived from the C-terminal region of a hemolytic lectin, CEL-III, from the marine invertebrate Cucumaria echinata
    Tomomitsu Hatakeyama
    Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Nagasaki 852 8521
    J Biochem 135:65-70. 2004
  2. doi request reprint cDNA cloning and expression of Contractin A, a phospholipase A2-like protein from the globiferous pedicellariae of the venomous sea urchin Toxopneustes pileolus
    Tomomitsu Hatakeyama
    Biomolecular Chemistry Laboratory, Graduate School of Engineering, Nagasaki University, Bunkyo machi 1 14, Nagasaki 852 8521, Japan Electronic address
    Toxicon 108:46-52. 2015
  3. doi request reprint cDNA cloning and characterization of a rhamnose-binding lectin SUL-I from the toxopneustid sea urchin Toxopneustes pileolus venom
    Tomomitsu Hatakeyama
    Biomolecular Chemistry Laboratory, Graduate School of Engineering, Nagasaki University, Bunkyo machi 1 14, Nagasaki 852 8521, Japan Electronic address
    Toxicon 94:8-15. 2015
  4. doi request reprint Equilibrium dialysis using chromophoric sugar derivatives
    Tomomitsu Hatakeyama
    Laboratory of Biomolecular Chemistry, Graduate School of Engineering, Nagasaki University, 1 14 Bunkyo machi, Nagasaki, 852 8521, Japan
    Methods Mol Biol 1200:165-71. 2014
  5. ncbi request reprint Alteration of the carbohydrate-binding specificity of a C-type lectin CEL-I mutant with an EPN carbohydrate-binding motif
    Tomomitsu Hatakeyama
    Biomolecular Chemistry Laboratory, Graduate School of Engineering, Nagasaki University, 1 14 Bunkyo machi, Nagasaki 852 8521, Japan
    Protein Pept Lett 20:796-801. 2013
  6. ncbi request reprint C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-III containing ricin-type -trefoil folds
    Tomomitsu Hatakeyama
    Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Nagasaki, Japan
    J Biol Chem 282:37826-35. 2007
  7. ncbi request reprint Effects of Ca2+ on refolding of the recombinant hemolytic lectin CEL-III
    Keigo Hisamatsu
    Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Nagasaki, Japan
    Biosci Biotechnol Biochem 73:1203-5. 2009
  8. pmc Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process
    Hideaki Unno
    From the Laboratory of Biomolecular Chemistry, Graduate School of Engineering, Nagasaki University, 1 14 Bunkyo machi, Nagasaki 852 8521, Japan
    J Biol Chem 289:12805-12. 2014
  9. ncbi request reprint Structure-activity relationship of an antibacterial peptide, maculatin 1.1, from the skin glands of the tree frog, Litoria genimaculata
    Takuro Niidome
    Department of Materials Science, Graduate School of Science and Technology, Nagasaki University, Nagasaki 852 8521, Japan
    J Pept Sci 10:414-22. 2004
  10. ncbi request reprint Characterization of recombinant CEL-I, a GalNAc-specific C-type lectin, expressed in Escherichia coli using an artificial synthetic gene
    Tomomitsu Hatakeyama
    Department of Applied Chemistry, Faculty of Engineering, and Division of Biochemistry, Faculty of Fisheries, Nagasaki University, 1 14 Bunkyo machi, Nagasaki 852 8521
    J Biochem 135:101-7. 2004

Collaborators

Detail Information

Publications33

  1. ncbi request reprint Antibacterial activity of peptides derived from the C-terminal region of a hemolytic lectin, CEL-III, from the marine invertebrate Cucumaria echinata
    Tomomitsu Hatakeyama
    Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Nagasaki 852 8521
    J Biochem 135:65-70. 2004
    ..These results also suggest that the hydrophobic region of CEL-III, from which P332 and its analogs were derived, may play some role in the interaction with target cell membranes to trigger hemolysis...
  2. doi request reprint cDNA cloning and expression of Contractin A, a phospholipase A2-like protein from the globiferous pedicellariae of the venomous sea urchin Toxopneustes pileolus
    Tomomitsu Hatakeyama
    Biomolecular Chemistry Laboratory, Graduate School of Engineering, Nagasaki University, Bunkyo machi 1 14, Nagasaki 852 8521, Japan Electronic address
    Toxicon 108:46-52. 2015
    ....
  3. doi request reprint cDNA cloning and characterization of a rhamnose-binding lectin SUL-I from the toxopneustid sea urchin Toxopneustes pileolus venom
    Tomomitsu Hatakeyama
    Biomolecular Chemistry Laboratory, Graduate School of Engineering, Nagasaki University, Bunkyo machi 1 14, Nagasaki 852 8521, Japan Electronic address
    Toxicon 94:8-15. 2015
    ....
  4. doi request reprint Equilibrium dialysis using chromophoric sugar derivatives
    Tomomitsu Hatakeyama
    Laboratory of Biomolecular Chemistry, Graduate School of Engineering, Nagasaki University, 1 14 Bunkyo machi, Nagasaki, 852 8521, Japan
    Methods Mol Biol 1200:165-71. 2014
    ....
  5. ncbi request reprint Alteration of the carbohydrate-binding specificity of a C-type lectin CEL-I mutant with an EPN carbohydrate-binding motif
    Tomomitsu Hatakeyama
    Biomolecular Chemistry Laboratory, Graduate School of Engineering, Nagasaki University, 1 14 Bunkyo machi, Nagasaki 852 8521, Japan
    Protein Pept Lett 20:796-801. 2013
    ..Additional mutations in the recombinant CEL-I binding site may further increase its specificity for mannose, and should provide insights into designing novel carbohydrate-recognition proteins...
  6. ncbi request reprint C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-III containing ricin-type -trefoil folds
    Tomomitsu Hatakeyama
    Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Nagasaki, Japan
    J Biol Chem 282:37826-35. 2007
    ..Binding of GalNAc also induced a slight change in the main chain structure of domain 3, which could be related to the conformational change upon binding of specific carbohydrates to induce oligomerization of the protein...
  7. ncbi request reprint Effects of Ca2+ on refolding of the recombinant hemolytic lectin CEL-III
    Keigo Hisamatsu
    Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Nagasaki, Japan
    Biosci Biotechnol Biochem 73:1203-5. 2009
    ..This suggests that Ca(2+) supported correct folding of the carbohydrate-binding domains of rCEL-III, leading to effective binding to the cell surface and subsequent self-oligomerization...
  8. pmc Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process
    Hideaki Unno
    From the Laboratory of Biomolecular Chemistry, Graduate School of Engineering, Nagasaki University, 1 14 Bunkyo machi, Nagasaki 852 8521, Japan
    J Biol Chem 289:12805-12. 2014
    ....
  9. ncbi request reprint Structure-activity relationship of an antibacterial peptide, maculatin 1.1, from the skin glands of the tree frog, Litoria genimaculata
    Takuro Niidome
    Department of Materials Science, Graduate School of Science and Technology, Nagasaki University, Nagasaki 852 8521, Japan
    J Pept Sci 10:414-22. 2004
    ..These results indicate that the entire chain length of Mac is necessary for full activity, and the basicity of the peptides greatly affects the activity...
  10. ncbi request reprint Characterization of recombinant CEL-I, a GalNAc-specific C-type lectin, expressed in Escherichia coli using an artificial synthetic gene
    Tomomitsu Hatakeyama
    Department of Applied Chemistry, Faculty of Engineering, and Division of Biochemistry, Faculty of Fisheries, Nagasaki University, 1 14 Bunkyo machi, Nagasaki 852 8521
    J Biochem 135:101-7. 2004
    ..Howeger, there is a subtle difference in the properties between the two proteins probably due to the additional methionine residue at the N-terminus of rCEL-I...
  11. doi request reprint Identification of the amino acid residues involved in the hemolytic activity of the Cucumaria echinata lectin CEL-III
    Keigo Hisamatsu
    Laboratory of Biomolecular Chemistry, Nagasaki University, Nagasaki, Japan
    Biochim Biophys Acta 1830:4211-7. 2013
    ..This lectin is composed of two carbohydrate-recognition domains (domains 1 and 2) and an oligomerization domain (domain 3) that facilitates CEL-III assembly in the target cell membrane to form ion-permeable pores...
  12. ncbi request reprint Characterization of a recombinant C-type lectin, rCEL-IV, expressed in Escherichia coli cells using a synthetic gene
    Tomomitsu Hatakeyama
    Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, 1 14 Bunkyo machi, Nagasaki 852 8521, Japan
    Biochim Biophys Acta 1760:318-25. 2006
    ....
  13. pmc Galactose recognition by a tetrameric C-type lectin, CEL-IV, containing the EPN carbohydrate recognition motif
    Tomomitsu Hatakeyama
    Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Nagasaki 852 8521, Japan
    J Biol Chem 286:10305-15. 2011
    ..These findings suggest that the specificity for oligosaccharides may be largely affected by interactions with amino acid residues in the binding site other than those determining the monosaccharide specificity...
  14. ncbi request reprint Roles of the valine clusters in domain 3 of the hemolytic lectin CEL-III in its oligomerization and hemolytic abilities
    Keigo Hisamatsu
    Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Bunkyo machi 1 14, Nagasaki 852 8521, Japan
    Protein Pept Lett 16:411-4. 2009
    ..The results suggest the involvement of these valine clusters in CEL-III oligomerization and hemolytic activity...
  15. ncbi request reprint Characterization of the {alpha}-helix region in domain 3 of the haemolytic lectin CEL-III: implications for self-oligomerization and haemolytic processes
    Keigo Hisamatsu
    Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Bunkyo machi 1 14, Nagasaki 852 8521, Japan
    J Biochem 143:79-86. 2008
    ..These results suggest that the alpha-helix region, particularly its alternate Val residues are important for oligomerization of CEL-III in target cell membranes, which is also required for a subsequent haemolytic action...
  16. pmc Crystallization and preliminary crystallographic study of oligomers of the haemolytic lectin CEL-III from the sea cucumber Cucumaria echinata
    Hideaki Unno
    Laboratory of Biomolecular Chemistry, Graduate School of Engineering, Nagasaki University, 1 14 Bunkyo machi, Nagasaki 852 8521, Japan
    Acta Crystallogr Sect F Struct Biol Cryst Commun 69:416-20. 2013
    ..2 Å resolution, respectively, using synchrotron radiation and the former was found to belong to space group C2. Self-rotation functional analysis of the soluble oligomer crystal suggested that it might be composed of heptameric CEL-III...
  17. ncbi request reprint An assay for carbohydrate-binding activity of lectins using polyamidoamine dendrimer conjugated with carbohydrates
    Tomomitsu Hatakeyama
    Biomolecular Chemistry Laboratory, Graduate School of Engineering, Nagasaki University, Nagasaki, Japan
    Biosci Biotechnol Biochem 76:1999-2001. 2012
    ..It is suggested that various lectins can also be measured using sugar-PDs to which different carbohydrates are attached...
  18. ncbi request reprint Amino acid sequence and carbohydrate-binding analysis of the N-acetyl-D-galactosamine-specific C-type lectin, CEL-I, from the Holothuroidea, Cucumaria echinata
    Tomomitsu Hatakeyama
    Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Japan
    Biosci Biotechnol Biochem 66:157-63. 2002
    ..3 x 10(4) M(-1), and the maximum number of bound NP-GalNAc was estimated to be 1.6 by an equilibrium dialysis experiment...
  19. ncbi request reprint Mitogenic activity of CEL-I, an N-acetylgalactosamine (GalNAc)-specific C-type lectin, isolated from the marine invertebrate Cucumaria echinata (Holothuroidea)
    Zedong Jiang
    Division of Biochemistry, Faculty of Fisheries, Nagasaki University, Nagasaki, Japan
    Biosci Biotechnol Biochem 74:1613-6. 2010
    ..These results suggest that CEL-I is a potent mitogenic lectin with the ability to stimulate both T and B cells...
  20. doi request reprint CEL-I, an N-acetylgalactosamine (GalNAc)-specific C-type lectin, induces nitric oxide production in RAW264.7 mouse macrophage cell line
    Tomohiro Yamanishi
    Nagasaki University, Bunkyo Machi, Japan
    J Biochem 146:209-17. 2009
    ..These results suggest that CEL-I induces NO production in RAW264.7 cells through the protein-cell interaction rather than the binding to the specific carbohydrate chains on the cell surface...
  21. ncbi request reprint CEL-I, an invertebrate N-acetylgalactosamine-specific C-type lectin, induces TNF-alpha and G-CSF production by mouse macrophage cell line RAW264.7 cells
    Tomohiro Yamanishi
    Division of Biochemistry, Faculty of Fisheries and Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, 1 14 Bunkyo machi, Nagasaki 852 8521, Japan
    J Biochem 142:587-95. 2007
    ..These results suggest that the intracellular signal transduction through the activation of MAP kinase system is involved in CEL-I-induced cytokine secretion...
  22. ncbi request reprint Oligomerization process of the hemolytic lectin CEL-III purified from a sea cucumber, Cucumaria echinata
    Hiromiki Kuwahara
    Department of Applied Chemistry, Faculty of Engineering, Nagasaki University Bunkyo machi Nagasaki 852 8521, Japan
    J Biochem 131:751-6. 2002
    ....
  23. doi request reprint Effects of amino acid mutations in the pore-forming domain of the hemolytic lectin CEL-III
    Tomonao Nagao
    a Biomolecular Chemistry Laboratory, Graduate School of Engineering, Nagasaki University, Nagasaki, Japan
    Biosci Biotechnol Biochem 80:1966-9. 2016
    ....
  24. pmc Identification, Characterization, and X-ray Crystallographic Analysis of a Novel Type of Mannose-Specific Lectin CGL1 from the Pacific Oyster Crassostrea gigas
    Hideaki Unno
    Graduate School of Engineering, Nagasaki University, 1 14 Bunkyo machi, Nagasaki 852 8521, Japan
    Sci Rep 6:29135. 2016
    ..These characteristics of CGL1 may be helpful as a research tool and for clinical applications. ..
  25. ncbi request reprint Effects of detergents on the oligomeric structures of hemolytic lectin CEL-III as determined by small-angle X-ray scattering
    Shuichiro Goda
    Biomolecular Chemistry Laboratory, Graduate School of Engineering, Nagasaki University, Japan
    Biosci Biotechnol Biochem 77:679-81. 2013
    ..Without detergents in solution, these heptamers further assembled into larger 21mer oligomers, comprising three heptamers held together by relatively weak hydrophobic interactions...
  26. doi request reprint Mannose-recognition mutant of the galactose/N-acetylgalactosamine-specific C-type lectin CEL-I engineered by site-directed mutagenesis
    Hiromi Moriuchi
    Laboratory of Biomolecular Chemistry, Graduate School of Engineering, Nagasaki University, 1 14 Bunkyo machi, Nagasaki 852 8521, Japan
    Biochim Biophys Acta 1850:1457-65. 2015
    ..Therefore, we examined the effects of an additional mutation in the carbohydrate-binding site on the specificity of the lectin...
  27. ncbi request reprint Cytotoxicity of a GalNAc-specific C-type lectin CEL-I toward various cell lines
    Takuya Kuramoto
    Division of Biochemistry, Faculty of Fisheries, and Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, 1 14 Bunkyo machi, Nagasaki 852 8521, Japan
    J Biochem 137:41-50. 2005
    ..Our results demonstrated that CEL-I showed a potent cytotoxic effect, especially on MDCK cells, by causing plasma membrane disorder without induction of apoptosis...
  28. doi request reprint Manno-oligosaccharide-binding ability of mouse RegIV/GST-fusion protein evaluated by complex formation with the carbohydrate-containing polyamidoamine dendrimer
    Yuta Kato
    a Biomolecular Chemistry Laboratory, Graduate School of Engineering, Nagasaki University, Nagasaki, Japan
    Biosci Biotechnol Biochem 78:1906-9. 2014
    ..Binding was inhibited by manno-oligosaccharides but not by mannose or other tested carbohydrates, suggesting that the binding site may have an extended structure in contrast with typical C-type lectins...
  29. ncbi request reprint Crystallization and preliminary crystallographic study of an invertebrate C-type lectin, CEL-I, from the marine invertebrate Cucumaria echinata
    Tomomitsu Hatakeyama
    Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, 1 14 Bunkyo machi, Nagasaki 852 8521, Japan
    Acta Crystallogr D Biol Crystallogr 58:143-4. 2002
    ..38 (3), b = 69.94 (3), c = 76.69 (3) A, beta = 136.46 (2) degrees. Diffraction data were collected to 2.0 A resolution using synchrotron radiation. The asymmetric unit contains one CEL-I molecule...
  30. pmc Crystal structure of the histidine-containing phosphotransfer protein ZmHP2 from maize
    Hajime Sugawara
    Laboratory for Communication Mechanisms, RIKEN Plant Science Center, 1 7 22 Suehiro cho, Tsurumi ku, Yokohama 230 0045, Japan
    Protein Sci 14:202-8. 2005
    ..In bacteria, it is replaced by glutamine or glutamate that form a hydrogen bond to Ndelta atoms of the phospho-accepting histidine. It may play a key role in the complex formation of ZmHP2 with receiver domains...
  31. ncbi request reprint Characteristic recognition of N-acetylgalactosamine by an invertebrate C-type Lectin, CEL-I, revealed by X-ray crystallographic analysis
    Hajime Sugawara
    Research Center for Structural and Functional Proteomics, Institute for Protein Research, Osaka University, 3 2 Yamada Oka, Suita, Osaka 565 0871, Japan
    J Biol Chem 279:45219-25. 2004
    ..Mutational analyses, in which Gln70 and/or Arg115 were replaced by alanine, confirmed that these residues contributed to GalNAc recognition in a cooperative manner...
  32. ncbi request reprint Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism
    Tatsuya Uchida
    Research Center for Structural and Functional Proteomics, Institute for Protein Research, Osaka University, 3 2 Yamadaoka, Suita, Osaka 565 0871
    J Biol Chem 279:37133-41. 2004
    ..This conformational change may be responsible for oligomerization of CEL-III molecules and hemolysis in the erythrocyte membranes...
  33. ncbi request reprint Characterization of functional domains of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata
    Yoshiaki Kouzuma
    Laboratory of Biochemistry, Faculty of Agriculture, Graduate School, Kyushu University, Hakozaki 6 10 1 Higashi ku, Fukuoka 812 8581
    J Biochem 134:395-402. 2003
    ..These results suggest that after binding to cell surface carbohydrate chains, CEL-III oligomerizes through C-terminal domains, leading to the formation of ion-permeable pores by hydrophobic interaction with the cell membrane...