1. An FMRFamide-related decapeptide isolated from the anterior byssus retractor muscle (ABRM) of the bivalve mollusc, Mytilus edulis, was shown to have D-Leu as the second amino acid residue. 2. The excitatory effects of the peptide (Mytilus-FFRFamide) on the ABRM were not changed appreciably by substituting an L-Leu residue for the D-Leu residue.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1016/0742-8413(92)90049-d | DOI Listing |
J Comp Neurol
May 2002
Department of Biological Sciences, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin 53201, USA.
FMRFamide-related peptides (FaRPs) are a large group of neuropeptides containing a common RFamide C-terminus; they have been identified in vertebrates and invertebrates. We have isolated the cDNA that encodes three FaRPs in the tobacco hornworm, Manduca sexta, including the amidated decapeptide F10. The larger FaRPs are the partially processed precursors of F10, a neuropeptide belonging to the myosuppressin family of peptides.
View Article and Find Full Text PDFJ Neurocytol
December 1998
Department of Experimental Zoology, Utrecht University, The Netherlands.
The distribution and actions of FMRFamide-related peptides (FaRPs) in the corpora cardiaca of the locust Locusta migratoria were studied. Antisera to FMRFamide and SchistoFLRFamide (PDVDHVFLRFamide) label neuronal processes that impinge on glandular cells in the glandular lobe of the corpora cardiaca known to produce adipokinetic hormones. Electron microscopic immunocytochemistry revealed that these FaRP-containing processes form synaptoid contacts with the glandular cells.
View Article and Find Full Text PDFBiochem Biophys Res Commun
February 1997
Comparative Neuroendocrinology Research Group, Queen's University of Belfast, Northern Ireland.
To date, 9 FMRFamide-related peptides (FaRPs) have been identified in Caenorhabditis elegans. Eight of these peptides are encoded on the flp-1 gene. However, AF2 (KHEYLRFamide) which was not co-encoded was the most abundant FaRP identified in ethanolic extracts.
View Article and Find Full Text PDFColor patterning in cephalopod molluscs involves activation of a peripheral chromatophore system that is under neuromuscular control. The complex behavior of individual chromatophores is mediated by a specific set of muscles, the chromatophore muscles, that receive direct innervation from the central nervous system. To date, glutamate is the only excitatory transmitter that has been proposed to act at the chromatophore neuromuscular junction of cephalopods.
View Article and Find Full Text PDFNeuropeptides
May 1995
Department of Zoology, University of Toronto, Ontario, Canada.
In the oviduct of Locusta migratoria, a FMRFamide-related peptide, PDVDHVFLRFamide (SchistoFLRFamide) acts as a neuromodulator, inhibiting spontaneous and induced muscle contraction. In this study, we have used N-terminal truncated peptides to show that PDVDHVFLRFamide has separated binding and activation regions. VFLRFamide is the minimum sequence required for binding, whereas HVFLRFamide is the minimum sequence for inhibitory biological activity.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!