Processing of the FMRFamide Precursor Protein in the Snail Lymnaea stagnalis: Characterization and Neuronal Localization of a Novel Peptide, ‘SEEPLY’
Ημερομηνία
1993Συγγραφέας
![ORCID logo](https://orcid.org/sites/default/files/images/orcid_16x16.png)
Wan Li, K.
Bright, K. E.
Yeoman, M.
Geraerts, W. P. M.
Benjamin, P. R.
Burke, J. F.
ISSN
0953-816XSource
European Journal of NeuroscienceVolume
5Pages
1003-1016Google Scholar check
Keyword(s):
Metadata
Εμφάνιση πλήρους εγγραφήςΕπιτομή
In the pulmonate snail Lymnaea stagnalis, FMRFamide‐like neuropeptides are encoded by a multi‐exon genomic locus which is subject to regulation at the level of mRNA splicing. We aim to understand the post‐translational processing of one resulting protein precursor encoding the tetrapeptide FMRFamide and a number of other putative peptides, and determine the distribution of the final peptide products in the central nervous system (CNS) and periphery of Lymnaea. We focused on two previously unknown peptide sequences predicted by molecular cloning to be encoded in the tetrapeptide protein precursor consecutively, separated by the tetrabasic cleavage site RKRR. Here we report the isolation and structural characterization of a novel non‐FMRFamide‐like peptide, the 22 amino acid peptide SEQPDVDDYLRDWLQSEEPLY. The novel peptide is colocalized with FMRFamide in the CNS in a number of identified neuronal systems and their peripheral motor targets, as determined by in situ hybridization and immunocytochemistry. Its detection in heart excitatory motoneurons and in nerve fibres of the heart indicated that the novel peptide may play a role, together with FMRFamide, in heart regulation in the snail. The second predicted peptide, STEAGGQSEEMTHRTA (16 amino acids), was at very low abundance in the CNS and was only occasionally detected. Our current findings, suggestive of a distinct pattern of post‐translational processing, allowed the reassessment of a previously proposed hypothesis that the two equivalent sequences in the Aplysia FMRFamide gene constitute a molluscan homologue of vertebrate corticotrophin releasing factor‐like peptides. Copyright © 1993, Wiley Blackwell. All rights reserved
Collections
Cite as
Related items
Showing items related by title, author, creator and subject.
-
Article
Addressing the Functional Determinants of FAK during Ciliogenesis in Multiciliated Cells
Antoniades, Ioanna; Stylianou, Panayiota; Christodoulou, Neophytos; Skourides, Paris A. (2017)We previously identified focal adhesion kinase (FAK) as an important regulator of ciliogenesis in multiciliated cells. FAK and other focal adhesion (FA) proteins associate with the basal bodies and their striated rootlets ...
-
Article
Split-Inteins for Simultaneous, site-specific conjugation of Quantum Dots to multiple protein targets In vivo
Charalambous, Anna; Antoniades, Ioanna; Christodoulou, Neophytos; Skourides, Paris A. (2011)Background: Proteins labelled with Quantum Dots (QDs) can be imaged over long periods of time with ultrahigh spatial and temporal resolution, yielding important information on the spatiotemporal dynamics of proteins within ...
-
Article
The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of ciliogenesis
Kypri, Elena; Christodoulou, A.; Maimaris, G.; Lethan, M.; Markaki, M.; Lysandrou, C.; Lederer, C. W.; Tavernarakis, N.; Geimer, S.; Pedersen, L. B.; Santama, Niovi (2014)Nucleotide-binding proteins Nubp1 and Nubp2 are MRP/MinD-type P-loop NTPases with sequence similarity to bacterial division site-determining proteins and are conserved, essential proteins throughout the Eukaryotes. They ...