ArticleJournal of the American Society for Mass Spectrometry2015
Peptidomics of Neuropeptidergic Tissues of the Tsetse Fly Glossina morsitans morsitans.
Article in Journal of the American Society for Mass Spectrometry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 24 citations in OpenAlex.
- Current Challenges and Future Directions in Peptidomics.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Expression analysis of peptidergic enteroendocrine cells in the silkworm Bombyx mori.Cell and tissue research · 2022Article
- Bacterial-mediated RNAi and functional analysis of Natalisin in a moth.Scientific reports · 2021Article
- Seasonal variation in UVA light drives hormonal and behavioural changes in a marine annelid via a ciliary opsin.Nature ecology & evolution · 2021Article
- The Adipokinetic Peptides in Diptera: Structure, Function, and Evolutionary Trends.Frontiers in endocrinology · 2020Article
- Regulation of Feeding and Metabolism by Neuropeptide F and Short Neuropeptide F in Invertebrates.Frontiers in endocrinology · 2019Review
- Enhancing vector refractoriness to trypanosome infection: achievements, challenges and perspectives.BMC microbiology · 2018Article
- Omics approaches to study juvenile hormone synthesis.Current opinion in insect science · 2018Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neuropeptides and peptide hormones are essential signaling molecules that regulate nearly all physiological processes. The recent release of the tsetse fly genome allowed the construction of a detailed in silico neuropeptide database (International Glossina Genome Consortium, Science 344, 380-386 (2014)), as well as an in-depth mass spectrometric analysis of the most important neuropeptidergic tissues of this medically and economically important insect species. Mass spectrometric confirmation of predicted peptides is a vital step in the functional characterization of neuropeptides, as in vivo peptides can be modified, cleaved, or even mispredicted. Using a nanoscale reversed phase liquid chromatography coupled to a Q Exactive Orbitrap mass spectrometer, we detected 51 putative bioactive neuropeptides encoded by 19 precursors: adipokinetic hormone (AKH) I and II, allatostatin A and B, capability/pyrokinin (capa/PK), corazonin, calcitonin-like diuretic hormone (CT/DH), FMRFamide, hugin, leucokinin, myosuppressin, natalisin, neuropeptide-like precursor (NPLP) 1, orcokinin, pigment dispersing factor (PDF), RYamide, SIFamide, short neuropeptide F (sNPF) and tachykinin. In addition, propeptides, truncated and spacer peptides derived from seven additional precursors were found, and include the precursors of allatostatin C, crustacean cardioactive peptide, corticotropin releasing factor-like diuretic hormone (CRF/DH), ecdysis triggering hormone (ETH), ion transport peptide (ITP), neuropeptide F, and proctolin, respectively. The majority of the identified neuropeptides are present in the central nervous system, with only a limited number of peptides in the corpora cardiaca-corpora allata and midgut. Owing to the large number of identified peptides, this study can be used as a reference for comparative studies in other insects. Graphical Abstract ᅟ.
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