Mass spectrometric survey of peptides in cephalopods with an emphasis on the FMRFamide-related peptides

J. V. Sweedler, L. Li, P. Floyd, W. Gilly

Research output: Contribution to journalArticlepeer-review

Abstract

A matrix-assisted laser desorption/ionization (MALDI) mass spectrometric (MS) survey of the major peptides in the stellar, fin and pallial nerves and the posterior chromatophore lobe of the cephalopods Sepia officinalis, Loligo opalescens and Dosidicus gigas has been performed. Although a large number of putative peptides are distinct among the three species, several molecular masses are conserved. In addition to peptides, characterization of the lipid content of the nerves is reported, and these lipid peaks account for many of the lower molecular masses observed. One conserved set of peaks corresponds to the FMRFamide-related peptides (FRPs). The Loligo opalescens FMRFa gene has been sequenced. It encodes a 331 amino acid residue prohormone that is processed into 14 FRPs, which are both predicted by the nucleotide sequence and confirmed by MALDI MS. The FRPs predicted by this gene (FMRFa, FLRFa/FIRFa and ALSGDAFLRFa) are observed in all three species, indicating that members of this peptide family are highly conserved across cephalopods.

Original languageEnglish (US)
Pages (from-to)3565-3573
Number of pages9
JournalJournal of Experimental Biology
Volume203
Issue number23
StatePublished - 2000

Keywords

  • Cephalopod
  • Dosidicus gigas
  • FMRFamide
  • Loligo opalescens
  • MALDI
  • Mass spectrometry
  • Neuropeptide
  • Sepia officinalis

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Agricultural and Biological Sciences (miscellaneous)

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