Updated on 2022/12/05


Brain Research Institute Center for Bioresources Specially Appointed Assistant
Specially Appointed Assistant
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  • 博士(理学) ( 2010.3   新潟大学 )

Research Areas

  • Life Science / Genome biology

Research History

  • Niigata University   Brain Research Institute Center for Bioresources   Specially Appointed Assistant




  • Identification of L-3-hydroxykynurenine O-sulfate in the buccal gland secretion of the parasitic lamprey, Lethenteron japonicum Reviewed

    Shoji Odani, Naoko Ito, Mai Hasegawa, Toshio Uchiumi, Sumihiro Hase

    AMINO ACIDS   43 ( 6 )   2505 - 2512   2012.12

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:SPRINGER WIEN  

    Parasitic lampreys are known to secrete proteins having anticoagulant and vasodilator activities from the buccal glands during feeding on their host's blood. However, small molecules in the secretion have never been explored in detail. We examined the secretion of Japanese liver lamprey (Lethenteron japonicum) for small molecules and found an intensely fluorescent substance upon gel filtration. After purification by anion-exchange chromatography and reversed-phase HPLC, structure of the compound was determined to be l-3-hydroxykynurenine O-sulfate by NMR- and UV-spectrometry, complemented with enzymatic and chemical degradation. In vertebrates, the sulfate ester of 3-hydroxykynurenine is a compound that has been regarded as a urinary metabolite of tryptophan but not reported from normal tissues to date. Although the function of this molecule in the buccal glands remains to be elucidated, it is remarkable that the same substance was described in 1960s from two species of blood-sucking insects, Rhodnius prolixus and Triatoma infestans, suggesting its potential role in blood-feeding.

    DOI: 10.1007/s00726-012-1331-x

    Web of Science



  • Multiple gamma-glutamylation: A novel type of post-translational modification in a diapausing Artemia cyst protein Reviewed

    Mai Hasegawa, Yuka Ikeda, Hideaki Kanzawa, Mika Sakamoto, Mina Goto, Susumu Tsunasawa, Toshio Uchiumi, Shoji Odani


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    Authorship:Lead author   Language:English   Publishing type:Research paper (scientific journal)   Publisher:ACADEMIC PRESS INC ELSEVIER SCIENCE  

    A highly hydrophilic, glutamate-rich protein was identified in the aqueous phenol extract from the cytosolic fraction of brine shrimp (Artemia franciscana) diapausing cysts and termed Anemia phenol soluble protein (PSP). Mass spectrometric analysis revealed the presence of many protein peaks around m/z 11,000, separated by 129 atomic mass units; this value corresponds to that of glutamate, which is strongly suggestive of heterogeneous polyglutamylation. Polyglutamylation has long been known as the functionally important post-translational modification of tubulins, which carry poly(L-glutamic acid) chains of heterogeneous length branching off from the main chain at the gamma-carboxy groups of a few specific glutamate residues. In Artemia PSP, however, Edman degradation of enzymatic peptides revealed that at least 13, and presumably 16, glutamate residues were modified by the attachment of a single L-glutamate, representing a hitherto undescribed type of post-translational modification: namely, multiple gamma-glutamylation or the addition of a large number of glutamate residues along the polypeptide chain. Although biological significance of PSP and its modification is yet to be established, suppression of in vitro thermal aggregation of lactate dehydrogenase by glutamylated PSP was observed. (C) 2010 Elsevier Inc. All rights reserved.

    DOI: 10.1016/j.bbrc.2010.02.064

    Web of Science