Identification of a new member of the GLWamide peptide family: Physiological activity and cellular localization in cnidarian polyps

Toshio Takahashi, Yoshitaka Kobayakawa, Yojiro Muneoka, Yuko Fujisawa, Shirou Mohri, Masayuki Hatta, Hiroshi Shimizu, Toshitaka Fujisawa, Tsutomu Sugiyama, Michiyo Takahara, Kensuke Yanagi, Osamu Koizumi

研究成果: ジャーナルへの寄稿学術誌査読

44 被引用数 (Scopus)


KPNAYKGKLPIGLWamide, a novel member of the GLWamide peptide family, was isolated from Hydra magnipapillata. The purification was monitored with a bioassay: contraction of the retractor muscle of a sea anemone, Anthopleura fuscoviridis. The new peptide, termed Hym-370, is longer than the other GLWamides previously isolated from H. magnipapillata and another sea anemone, A. elegantissima. The amino acid sequence of Hym-370 is six residues longer at its N-terminal than a putative sequence previously deduced from the cDNA encoding the precursor protein. The new longer isoform, like the shorter GLWamides, evoked concentration-dependent muscle contractions in both H. magnipapillata and A. fuscoviridis. In contrast, Hym-248, one of the shorter GLWamide peptides, specifically induced contraction of the endodermal muscles in H. magnipapillata. This is the first case in which a member of the hydra GLWamide family (Hym-GLWamides) has exhibited an activity not shared by the others. Polyclonal antibodies were raised to the common C-terminal tripeptide GLWamide and were used in immunohistochemistry to localize the GLWamides in the tissue of two species of hydra, H. magnipapillata and H. oligactis, and one species of sea anemone, A. fuscoviridis. In each case, nerve cells were specifically labeled. These results suggest that the GLWamides are ubiquitous among cnidarians and are involved in regulating the excitability of specific muscles.

ジャーナルComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
出版ステータス出版済み - 6月 1 2003

!!!All Science Journal Classification (ASJC) codes

  • 水圏科学
  • 動物科学および動物学
  • 分子生物学
  • 生化学
  • 生理学


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