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

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)309-324
Number of pages16
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume135
Issue number2
DOIs
Publication statusPublished - Jun 1 2003

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Sea Anemones
Hydra
Cnidaria
Muscle Contraction
Polyps
Muscle
Peptides
Protein Precursors
Biological Assay
Bioassay
Amino Acid Sequence
Protein Isoforms
Complementary DNA
Immunohistochemistry
Neurons
Purification
Muscles
Antibodies
Tissue
Amino Acids

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Molecular Biology

Cite this

Identification of a new member of the GLWamide peptide family : Physiological activity and cellular localization in cnidarian polyps. / Takahashi, Toshio; Kobayakawa, Yoshitaka; Muneoka, Yojiro; Fujisawa, Yuko; Mohri, Shirou; Hatta, Masayuki; Shimizu, Hiroshi; Fujisawa, Toshitaka; Sugiyama, Tsutomu; Takahara, Michiyo; Yanagi, Kensuke; Koizumi, Osamu.

In: Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, Vol. 135, No. 2, 01.06.2003, p. 309-324.

Research output: Contribution to journalArticle

Takahashi, Toshio ; Kobayakawa, Yoshitaka ; Muneoka, Yojiro ; Fujisawa, Yuko ; Mohri, Shirou ; Hatta, Masayuki ; Shimizu, Hiroshi ; Fujisawa, Toshitaka ; Sugiyama, Tsutomu ; Takahara, Michiyo ; Yanagi, Kensuke ; Koizumi, Osamu. / Identification of a new member of the GLWamide peptide family : Physiological activity and cellular localization in cnidarian polyps. In: Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology. 2003 ; Vol. 135, No. 2. pp. 309-324.
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