Novel excitatory neuropeptides isolated from a prosobranch gastropod, Thais clavigera: The molluscan counterpart of the annelidan GGNG peptides.
The GGNG peptides are excitatory neuropeptides identified from earthworms, leeches and polychaeta. Two structurally related peptides were purified and characterized from a mollusk, Thais clavigera (prosobranch gastropod). The peptides designated as Thais excitatory peptide-1 (TEP-1) (KCSGKWAIHACWGGN-NH2) and TEP-2 (KCYGKWAMHACWGGN-NH2) are pentadecapeptides having one disulfide bond and C-terminal GGN-NH2 structures, which are shared by most GGNG peptides. TEP augmented the motilities of Thais esophagus and penial complex. TEP-like immunoreactivity is distributed in both the neurons of the central nervous system and nerve endings in the penial complex. Thus, the involvement of TEP in the contraction of the digestive and reproductive systems is suggested. Substitution of amino acids in TEP revealed that two tryptophan residues in TEP are important for maintaining bioactivity.
Morishita
F
F
Department of Biological Science, Graduate School of Science, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima, Hiroshima 739-8526, Japan. fumi425@hiroshima-u.ac.jp
Minakata
H
H
Takeshige
K
K
Furukawa
Y
Y
Takata
T
T
Matsushima
O
O
Mukai
S T
ST
Saleuddin
A S M
AS
Horiguchi
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001048:Aplysia; D002851:Chromatography, High Pressure Liquid; D004947:Esophagus / Q000187:drug effects; D005260:Female; D049851:Gastropoda / Q000737:chemistry; D005835:Genitalia / Q000187:drug effects; D008297:Male; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry / Q000302:isolation & purification / Q000502:physiology*; D010456:Peptides, Cyclic / Q000276:immunology; D014018:Tissue Distribution
D009479:Neuropeptides; D010456:Peptides, Cyclic; C107510:leech excitatory peptide, Hirudo nipponia