Comparative peptidomics of Caenorhabditis elegans versus C. briggsae by LC–MALDI-TOF MS

Husson, Steven; Landuyt, Bart; Nys, Thomas; Baggerman, Geert; Boonen, Kurt; Clynen, Elke; Lindemans, Marleen; Janssen, Tom; Schoofs, Liliane

doi:10.1016/j.peptides.2008.07.021

Cited by 43 publications

(30 citation statements)

References 46 publications

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“…In 2005, McVeigh and co-workers performed a systematic BLAST analysis of EST databases to investigate FLP sequence diversity within the phylum Nematoda identifying more than 500 FLPs across 46 species (13). The FLP complement of other nematodes seems to be generally similar to that of C. elegans (13, 30, 44). This finding is confirmed by a very recent study of McCoy and colleagues, who re-investigated the available genome and transcriptome resources for 17 pathogenic nematodes (24).…”

Section: Flp Repertoire Of Nematodesmentioning

confidence: 91%

The FMRFamide-Like Peptide Family in Nematodes

et al. 2014

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In the three decades since the FMRFamide peptide was isolated from the mollusk Macrocallista nimbosa, structurally similar peptides sharing a C-terminal RFamide motif have been identified across the animal kingdom. FMRFamide-like peptides (FLPs) represent the largest known family of neuropeptides in invertebrates. In the phylum Nematoda, at least 32 flp-genes are classified, making the FLP system of nematodes unusually complex. The diversity of the nematode FLP complement is most extensively mapped in Caenorhabditis elegans, where over 70 FLPs have been predicted. FLPs have shown to be expressed in the majority of the 302 C. elegans neurons including interneurons, sensory neurons, and motor neurons. The vast expression of FLPs is reflected in the broad functional repertoire of nematode FLP signaling, including neuroendocrine and neuromodulatory effects on locomotory activity, reproduction, feeding, and behavior. In contrast to the many identified nematode FLPs, only few peptides have been assigned a receptor and there is the need to clarify the pathway components and working mechanisms of the FLP signaling network. Here, we review the diversity, distribution, and functions of FLPs in nematodes.

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Section: Flp Repertoire Of Nematodesmentioning

confidence: 91%

The FMRFamide-Like Peptide Family in Nematodes

et al. 2014

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“…A number of these have also been identified in C. elegans including: AF1, AF2, AF8, AF9, AF15, AF21, AF22 and AF24. A recent LC-MALDI-TOF MS study has identified 37 FLPs in C. elegans encoded by 19 flp genes, most of which were also identified in Caenorhabditis briggsae demonstrating that FLPs are strongly conserved between the two species (Husson et al 2008). A total of over 70 FLPs from around 33 genes have been identified in C. elegans (Husson et al 2005;Kim and Li.…”

Section: Nematodesmentioning

confidence: 99%

A review of FMRFamide- and RFamide-like peptides in metazoa

2009

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Neuropeptides are a diverse class of signalling molecules that are widely employed as neurotransmitters and neuromodulators in animals, both invertebrate and vertebrate. However, despite their fundamental importance to animal physiology and behaviour, they are much less well understood than the small molecule neurotransmitters. The neuropeptides are classified into families according to similarities in their peptide sequence; and on this basis, the FMRFamide and RFamide-like peptides, first discovered in molluscs, are an example of a family that is conserved throughout the animal phyla. In this review, the literature on these neuropeptides has been consolidated with a particular emphasis on allowing a comparison between data sets in phyla as diverse as coelenterates and mammals. The intention is that this focus on the structure and functional aspects of FMRFamide and RFamide-like neuropeptides will inform understanding of conserved principles and distinct properties of signalling across the animal phyla.

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“…In contrast to many of the neuropeptides/hormones in mammals that evolved from ancient versions [12], the mammalian UII gene has not been reported until this study to have homologous peptide systems in invertebrates. This lack is surprising as prohormone databases for insects, worms and crustaceans have rapidly grown, especially due to the recent advent of high throughput genetic sequencing and peptide prediction and identification methods [13], [14], [15], [16], [17], [18], [19], [20], [21]. According to the latest evolutionary analysis, the UII peptide system is thought to have appeared early in vertebrate evolution [22], after the divergence of deuterostomes and protostomes.…”

Section: Introductionmentioning

confidence: 99%

Urotensin II in Invertebrates: From Structure to Function in Aplysia californica

et al. 2012

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Neuropeptides are ancient signaling molecules that are involved in many aspects of organism homeostasis and function. Urotensin II (UII), a peptide with a range of hormonal functions, previously has been reported exclusively in vertebrates. Here, we provide the first direct evidence that UII-like peptides are also present in an invertebrate, specifically, the marine mollusk Aplysia californica. The presence of UII in the central nervous system (CNS) of Aplysia implies a more ancient gene lineage than vertebrates. Using representational difference analysis, we identified an mRNA of a protein precursor that encodes a predicted neuropeptide, we named Aplysia urotensin II (apUII), with a sequence and structural similarity to vertebrate UII. With in-situ hybridization and immunohistochemistry, we mapped the expression of apUII mRNA and its prohormone in the CNS and localized apUII-like immunoreactivity to buccal sensory neurons and cerebral A-cluster neurons. Mass spectrometry performed on individual isolated neurons, and tandem mass spectrometry on fractionated peptide extracts, allowed us to define the posttranslational processing of the apUII neuropeptide precursor and confirm the highly conserved cyclic nature of the mature neuropeptide apUII. Electrophysiological analysis of the central effects of a synthetic apUII suggests it plays a role in satiety and/or aversive signaling in feeding behaviors. Finding the homologue of vertebrate UII in the numerically small CNS of an invertebrate animal model is important for gaining insights into the molecular mechanisms and pathways mediating the bioactivity of UII in the higher metazoan.

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Comparative peptidomics of Caenorhabditis elegans versus C. briggsae by LC–MALDI-TOF MS

Cited by 43 publications

References 46 publications

The FMRFamide-Like Peptide Family in Nematodes

The FMRFamide-Like Peptide Family in Nematodes

A review of FMRFamide- and RFamide-like peptides in metazoa

Urotensin II in Invertebrates: From Structure to Function in Aplysia californica

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