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Identification of SepCRP analogues in the cuttlefish Sepia officinalis: a novel family of ovarian regulatory peptides.

TitreIdentification of SepCRP analogues in the cuttlefish Sepia officinalis: a novel family of ovarian regulatory peptides.
Type de publicationJournal Article
Year of Publication2005
AuteursBernay, B, Baudy-Floc'h, M, Zanuttini, B, Gagnon, J, Henry, J
JournalBiochem Biophys Res Commun
Date Published2005 Dec 16
Mots-clésAmino Acid Sequence, Animals, Cells, Cultured, Conserved Sequence, Female, Intercellular Signaling Peptides and Proteins, Molecular Sequence Data, Oocytes, Organ Specificity, Ovary, Oviposition, Sepia, Sequence Analysis, Protein, Sequence Homology, Amino Acid, Tissue Distribution

In the cuttlefish, Sepia officinalis, the ovary appears to be one of the main sources of regulatory peptides involved in the successive steps of egg-laying. Following the identification of the SepCRP-1, which is a peptide extracted from ovary and involved in egg capsule secretion, investigations were focused on the identification of related peptides. Seven related-Sepia Capsule Releasing Peptides (R-SepCRPs) were identified by means of mass spectrometry and characterized using MS/MS spectra and/or Edman degradation. Finally, primary structures were verified by the comparison of MS/MS spectra from endogenic and synthetic peptides. This new ovarian peptide family exhibits a conserved SLXKD tag involved in the biological activity. LC-MS/MS screening clearly demonstrates that R-SepCRPs are restricted to the female genital tract. Expressed during vitellogenesis, they are released by vitellogenic follicles and full-grown oocytes (FGO) in the genital coelom. Biological activities suggest that R-SepCRPs would be responsible for the storage of FGO before mating and would take part in the mechanical secretion of egg capsule products, as previously described for SepCRP-1.

Alternate JournalBiochem. Biophys. Res. Commun.
Identifiant (ID) PubMed16256953