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Journal of Experimental Biology, Vol 202, Issue 21 2961-2973, Copyright © 1999 by Company of Biologists

JOURNAL ARTICLES

Egg-laying hormone peptides in the aplysiidae family

L Li, RW Garden, PD Floyd, TP Moroz, JM Gleeson, JV Sweedler, L Pasa-Tolic and RD Smith
Department of Chemistry and Beckman Institute, University of Illinois, Urbana, IL 61801, USA. sweedler@bozo.scs.uiuc.edu

The neuropeptidergic bag cells of the marine mollusc Aplysia californica are involved in the egg-laying behavior of the animal. These neurosecretory cells synthesize an egg-laying hormone (ELH) precursor protein, yielding multiple bioactive peptides, including ELH, several bag cell peptides (BCP) and acidic peptide (AP). While immunohistochemical studies have involved a number of species, homologous peptides have been biochemically characterized in relatively few Aplysiidae species. In this study, a combination of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MS) and electrospray ionization Fourier transform ion cyclotron resonance MS is used to characterize and compare the ELH peptides from related opisthobranch molluscs including Aplysia vaccaria and Phyllaplysia taylori. The peptide profiles of bag cells from these two Aplysiidae species are similar to that of A. californica bag cells. In an effort to characterize further several of these peptides, peptides from multiple groups of cells of each species were extracted, and microbore liquid chromatography was used to separate and isolate them. Several MS-based sequencing approaches are applied to obtain the primary structures of bag cell peptides and ELH. Our studies reveal that (&agr;)-BCPs are 100 % conserved across all species studied. In addition, the complete sequences of (&egr;)-BCP and ELH of A. vaccaria were determined. They show a high degree of homology to their counterparts in A. californica, with only a few amino acid residue substitutions.
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 J. Exp. Biol.Home page
J. Sweedler, L Li, P Floyd, and W Gilly
Mass spectrometric survey of peptides in cephalopods with an emphasis on the FMRFamide-related peptides
J. Exp. Biol., January 12, 2000; 203(23): 3565 - 3573.
[Abstract] [PDF]


© The Company of Biologists Ltd 1999