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 language | English |
|---|---|
| Pages (from-to) | 309-324 |
| Number of pages | 16 |
| Journal | Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology |
| Volume | 135 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Jun 1 2003 |
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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 journal › Article
}
TY - JOUR
T1 - Identification of a new member of the GLWamide peptide family
T2 - Physiological activity and cellular localization in cnidarian polyps
AU - Takahashi, Toshio
AU - Kobayakawa, Yoshitaka
AU - Muneoka, Yojiro
AU - Fujisawa, Yuko
AU - Mohri, Shirou
AU - Hatta, Masayuki
AU - Shimizu, Hiroshi
AU - Fujisawa, Toshitaka
AU - Sugiyama, Tsutomu
AU - Takahara, Michiyo
AU - Yanagi, Kensuke
AU - Koizumi, Osamu
PY - 2003/6/1
Y1 - 2003/6/1
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=12444288125&partnerID=8YFLogxK
U2 - 10.1016/S1096-4959(03)00088-5
DO - 10.1016/S1096-4959(03)00088-5
M3 - Article
C2 - 12798941
AN - SCOPUS:12444288125
VL - 135
SP - 309
EP - 324
JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
SN - 0305-0491
IS - 2
ER -