Abstract
Neuropeptides, as neurotransmitters and neuromodulators, have a variety of physiological functions in the mollusk. Here, a PRQFVamide-related peptide gene was cloned from cuttlefish Sepiella japonica (designated as SjPRQFVRP, GenBank Accession No: OK999997). The full length of SjPRQFVRP is 1748 bp, including an open reading frame (ORF) of 738 bp encoding 245 amino acids. The putative precursor protein comprises one signal peptide and four different mature pentapeptides: fourteen copies of PMEFLamide, three copies of RMEFLamide, one copy of AMEFLamide and GMEFLamide. Multiple alignments showed SjPRQFVRP shared 71% identity with that of Octopus vulgaris and supported the phylogenetic analysis. The spatio-temporal expression pattern showed that SjPRQFVRP mRNA was widely expressed among the 13 tissues and primarily abundantly expressed in the brain and optic lobe during the whole development stage. In situ hybridization data indicated that SjPRQFVRP was detected in the vertical lobe, subvertical lobe, anterior basal lobe, anterior pedal lobe, and optic lobes of the brain. Subcellular localization analysis revealed that the SjPRQFVRP protein was localized in the cytoplasm of HEK293 cells. Collectively, the results will provide a foundation for further exploring the mechanism of SjPRQFVRP function in cephalopods.
Highlights
Neuropeptides are signaling molecular produced and released primarily by neurons and engaged in diverse physiological processes (Wang et al, 2015)
The amino acid sequences of PRQFVamide downloaded from the National Center for Biotechnology Information (NCBI) database from the other four representative species and the SjPRQFVRP were used for alignment analysis
The results indicated that SjPRQFVRP shared 71% identity to the PRQFVamide-like of O. vulgaris (XP 029646280.1), and 47, 46, 45% identity to those of M. yessoensis (OWF49118.1), A. californica (NP 001191529.1), and D. reticulatum (ARS01374.1), respectively
Summary
Neuropeptides are signaling molecular produced and released primarily by neurons and engaged in diverse physiological processes (Wang et al, 2015). Since the first neuropeptide eledoisin was sequenced from octopus Eledone moschata (Erspamer and Anastasi, 1962), neuropeptides have been extensively studied in multiple invertebrates, including mollusks (Price and Greenberg, 1977; Pulst et al, 1988), nematodes (Davenport et al, 1988; Keating et al, 1995), and arthropods (Marder et al, 1986; Nambu et al, 1988). These neuropeptides have been linked to various physiological and behavioral processes such as learning and memory (Beets et al, 2012), metabolism (Kaufmann and Brown, 2008; Wang et al, 2013), longevity (Waterson et al, 2014), and reproduction (Garrison et al, 2012). FMRFamide (Phe-MetArg-Phe-NH2) and FMRFamide-related peptides (FaRPs) were identified in Loligo pealei (Burbach et al, 2013), Sepia officinalis (Chrachri, 2020), and Sepia pharaonis (Zhu et al, 2020); GnRH (Gonadotropin-releasing hormone) was reported in S. officinalis (Di Cristo et al, 2009), Sepia lycidas (Murata et al, 2021) and S. pharaonis (Song et al, 2021); APGWamide (Ala-Pro-GlyTrp-NH2) was reported in Octopus vulgaris (Di Cristo et al, 2005), and Idiosepius pygmaeus (Sirinupong et al, 2011); Small cardioactive peptide (sCAP) was identified in Octopus minor (Iwakoshi et al, 2000), O. vulgaris (Kanda and Minakata, 2006), and Sepiella japonica (Li et al, 2019)
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