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dc.contributor.authorSantama, Niovien
dc.contributor.authorWheeler, C. H.en
dc.contributor.authorSkingsley, D. R.en
dc.contributor.authorYeoman, M. S.en
dc.contributor.authorBright, K.en
dc.contributor.authorKaye, I.en
dc.contributor.authorBurke, J. F.en
dc.contributor.authorBenjamin, P. R.en
dc.creatorSantama, Niovien
dc.creatorWheeler, C. H.en
dc.creatorSkingsley, D. R.en
dc.creatorYeoman, M. S.en
dc.creatorBright, K.en
dc.creatorKaye, I.en
dc.creatorBurke, J. F.en
dc.creatorBenjamin, P. R.en
dc.date.accessioned2019-11-04T12:52:37Z
dc.date.available2019-11-04T12:52:37Z
dc.date.issued1995
dc.identifier.issn0953-816X
dc.identifier.urihttp://gnosis.library.ucy.ac.cy/handle/7/53364
dc.description.abstractWe are interested in analysing the detailed modulation of defined neuronal systems by multiple neuropeptides encoded in the FMRFamide locus of the snail Lymnaea. Cloning of the FMRFamide gene has predicted the existence of two novel peptides previously unknown from biochemical analysis, the pentapeptides EFLRlamideand QFYRlamide. These peptides may form part of a new family of peptides sharing the sequence motif –FXRlamide. In this paper we adopt a novel approach to first identify and characterize –FXRlamide‐like peptides in extracts from the central nervous system of Lymnaea. By a combination of high‐performance liquid chromatography (HPLC) and continuous‐flow fast atom bombardment mass spectrometry, we identify three novel peptides: EFLRlamide, pQFYRlamide and pQFLRlamide. The first two are those predicted in exon II of the FMRFamide locus whereas the last is, interestingly, a product which cannot be derived from post‐translational modification of the predicted peptides but must be encoded by as yet unidentified nucleotide sequences. A specific antibody raised to EFLRlamide, and immuno reactive to all three peptides, revealed EFLRlamide‐like expression throughout the central nervous system in the same cells where exon II is transcribed and the peptide SEEPLY (a post‐translational product of exon II) was localized. Additional cells, however, were also identified. Immunoreactivity was mapped in a number of identified neurons in the central nervous system, including two heart cardio excitatory motoneurons, the Ehe cells (E heart excitors of the visceral ganglion) and penialmotoneurons in the right cerebral ganglion. The peripheral tissues (heart and penial complex) that the serespective classes of neurons innervate also exhibited EFLRlamide immunoreactivity. The central and peripheral localization of EFLRlamide‐like immunoreactivity suggested that EFLRlamide/pQFYRlamide may have an important physiological role in both these peripheral systems as well as in the central nervous system. This was confirmed by physiological experiments that showed that EFLRlamide and pQFYRlamide inhibited many centralneurons and in particular the Bgp neurons in the right parietal ganglion. EFLRlamide had complex biphasic effects on the frequency of heart‐beat: an initial inhibitory response was followed by a long‐lasting increase in the rate of beating. Taken together with earlier work, this study now completes the analysis and localization of the full set of post‐translational products of the FMRFamide precursor in Lymnaea and supplies further evidence towards the characterization of the physiological systems which such peptides may modulate in concert. Copyright © 1995, Wiley Blackwell. All rights reserveden
dc.sourceEuropean Journal of Neuroscienceen
dc.source.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-0028799747&doi=10.1111%2fj.1460-9568.1995.tb01059.x&partnerID=40&md5=1d8c225e52b63fbca00fe2971c68c45e
dc.subjectarticleen
dc.subjectpriority journalen
dc.subjectexonen
dc.subjectprotein analysisen
dc.subjectImmunohistochemistryen
dc.subjectnonhumanen
dc.subjecthigh performance liquid chromatographyen
dc.subjectantibodyen
dc.subjectimmunoreactivityen
dc.subjectAnimalen
dc.subjectanimal tissueen
dc.subjectExonsen
dc.subjectMolecular Sequence Dataen
dc.subjecttissue distributionen
dc.subjecthearten
dc.subjectprotein localizationen
dc.subjectin situ hybridizationen
dc.subjectNeuronsen
dc.subjectfast atom bombardment mass spectrometryen
dc.subjectSupport, Non-U.S. Gov'ten
dc.subjectcentral nervous systemen
dc.subjectAmino Acid Sequenceen
dc.subjectModels, Geneticen
dc.subjectProtein Processing, Post-Translationalen
dc.subjectsnailen
dc.subjectFMRFamideen
dc.subjectLymnaeaen
dc.subjectneuropeptideen
dc.subjectneuropeptidesen
dc.subjectNeurotransmittersen
dc.subjectphenylalanylmethionylarginylphenylalaninamide like peptideen
dc.subjectmotoneuronen
dc.subjectphenylalanylmethionylarginylphenylalaninamideen
dc.subjectautonomic ganglionen
dc.subjectbrain ganglionen
dc.subjectBrain Mappingen
dc.subjectfast‐atom bombardment mass spectrometryen
dc.subjectGenetic Codeen
dc.subjectheart excitationen
dc.subjectimmunocytochernistryen
dc.subjectinvertebrate neuronen
dc.subjectneurochemistryen
dc.titleIdentification, Distribution and Physiological Activity of Three Novel Neuropeptides of Lymnaea: FLRlamide and pQFYRlamide Encoded by the FMRFamide Gene, and a Related Peptideen
dc.typeinfo:eu-repo/semantics/article
dc.identifier.doi10.1111/j.1460-9568.1995.tb01059.x
dc.description.volume7
dc.description.startingpage234
dc.description.endingpage246
dc.author.facultyΣχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences
dc.author.departmentΤμήμα Βιολογικών Επιστημών / Department of Biological Sciences
dc.type.uhtypeArticleen
dc.source.abbreviationEur.J.Neurosci.en
dc.contributor.orcidSantama, Niovi [0000-0002-8370-8674]
dc.gnosis.orcid0000-0002-8370-8674


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