| Title | Isolation and identification of a novel Ala-Pro-Gly-Trp-amide-related peptide inhibiting the motility of the mature oviduct in the cuttlefish, Sepia officinalis. |
| Publication Type | Journal Article |
| Year of Publication | 1997 |
| Authors | Henry, J, Favrel, P, Boucaud-Camou, E |
| Journal | Peptides |
| Volume | 18 |
| Issue | 10 |
| Pagination | 1469-74 |
| Date Published | 1997 |
| ISSN | 0196-9781 |
| Keywords | Amino Acid Sequence, Animals, Chromatography, High Pressure Liquid, Dipeptides, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, Female, Mollusca, Muscle Contraction, Neuropeptides, Optic Lobe, Nonmammalian, Oviducts, Protein Processing, Post-Translational, Seasons, Sequence Analysis, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
| Abstract | A novel myotropic neuropeptide was isolated from 110 optic lobes (OL) of mature females of the cuttlefish Sepia officinalis L. by mean of high performance liquid chromatography (HPLC). The peptide inhibits the motility of the oviduct by decreasing the tonus, the frequency and the amplitude of the contractions. The primary structure of the peptide was determined as Gly-Trp-NH2. This new dipeptide is closely related to the Ala-Pro-Gly-Trp-NH2 family first identified in gastropod molluscs. On the perfused oviduct, GWa appeared to be 3000 times more potent than APGW-amide. The processing of synthetic APGWa into GWa by diaminopeptidyl activity has been clearly observed in OL extract. Nevertheless, the analysis in MALDI-MS of HPLC OL fractions did not reveal any APGWa related peptides of the known: APGWa, KPGWa, RPGWa and TPGWa. GWa could be processed from a not yet identified APGWa related peptide. |
| Alternate Journal | Peptides |
| PubMed ID | 9437704 |