Molecular evolution and functional characterisation of insulin related peptides in molluscs: Contributions of Crassostrea gigas genomic and transcriptomic-wide screening

Cherif--Feildel, Maëva; Berthelin, Clothilde Heude; Adeline, Béatrice; Rivière, Guillaume; Favrel, Pascal; Kellner, K

doi:10.1016/j.ygcen.2018.10.019

Cited by 24 publications

(30 citation statements)

References 92 publications

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“…Numerous insulin-like peptides have been identified in mollusks, especially in gastropods (Smit et al 1988;Floyd et al 1999;Veenstra 2010;Ahn et al 2017) and bivalves (Cherif-Feildel et al 2018). These neuropeptides are involved in the growth and glucose metabolism (Ebberink et al 1989).…”

Section: Insulin-related Peptidementioning

confidence: 99%

In silico prediction of neuropeptides from the neural ganglia of Pacific abalone Haliotis discus hannai (Mollusca: Gastropoda)

Sharker

Sukhan

Kim

et al. 2020

The European Zoological Journal

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Neuropeptides play a central role in the regulation of reproduction, growth, development, and various other physiological processes. In our study, 26 neuropeptide precursors were identified from the pleuropedal and cerebral ganglia of Pacific abalone using transcriptome analysis. Of them, two (neuromacin and neuroglian) were potentially novel and two (myomodulin and FMRFamide) were involved in the reproductive regulation of mollusks. A BLAST search indicated that most of these neuropeptides exhibited the highest homologies with neuropeptides of other protostomian species. Myomodulin, FMRFamide, and molluscan insulin-related peptides shared 87%, 72%, and 88% sequence identities with homologous peptides of the tropical gastropod mollusk, Haliotis asinina. In silico analysis revealed that these identified neuropeptide precursors were likely to be extracellular secreted proteins. Alignment of multiple cerebrin, FFamide, and insulin-related peptide sequences illustrated that most of their biologically active residues were highly conserved with other invertebrate homologous neuropeptide residues. Three-dimensional (3D) structures of adipokinetic hormone, allatostain (A, B, and C), allatotropin, cerebrin, clionin, conopressin, elevenin, and neuromycin precursors in H. discus hannai exhibited a helix-loophelix structure. Based on phylogenetic analysis, buccalin A1 and A2, allatostain B, and FCAP neuropeptide precursors of Pacific abalone formed a clade with other gastropod and bivalve mollusks neuropeptide precursors. This study provides a novel insight for further functional studies of abalone and other gastropod mollusks.

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Section: Insulin-related Peptidementioning

confidence: 99%

In silico prediction of neuropeptides from the neural ganglia of Pacific abalone Haliotis discus hannai (Mollusca: Gastropoda)

Sharker

Sukhan

Kim

et al. 2020

The European Zoological Journal

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“…As a step toward addressing these questions, let us examine the insulin superfamily. This group of proteins includes ILPs with a typical proteomic structure of B and A chains linked by disulfide bonds (178). Peptides of the insulin family are found in protozoans (179) and metazoans-both vertebrates and invertebrates (180).…”

Section: Why Insulin-like?mentioning

confidence: 99%

The “IAG-Switch”—A Key Controlling Element in Decapod Crustacean Sex Differentiation

Levy

Sagi

2020

Front. Endocrinol.

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“…The dataset provides a list of hyperlinks to insulin-related peptides NCBI ID originating from various metazoan species (referenced as [1] , [2] , [3] , [4] , [5] , [6] , [7] , [8] , [9] , [10] , [11] , [12] , [13] , [14] , [15] , [16] , [17] , [18] , [19] , [20] , [21] , [22] , [23] , [24] , [25] , [26] , [27] , [28] , [29] , [30] , [31] , [32] , [33] , [34] , [35] , [36] , [37] , [38] , [39] , [40] , [41] , [42] , [43] , [44] , [45] , [46] , [47] , [48] , [49] ). For each sequence, the key motif of the A chain associated to the number and position of disulphide bonds was specified.…”

Section: Datamentioning

confidence: 99%

“…Moreover, the structural type (α, β or γ), the A chain motif, the total number of cysteins, the C peptide cleavage mode and the potential additional domains (D or E) are specified for each sequence. The data are associated with the research article “Molecular evolution and functional characterisation of insulin-related peptides in molluscs: contributions of Crassostrea gigas genomic and transcriptomic-wide screening” [1] . The table presented here can be found at http://dx.doi.org/10.17632/w4gr8zcpk5.4#file-21c0f6a5-a3e3-4a15-86e0-e5a696458866 .…”

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confidence: 99%

Data for evolutive analysis of insulin related peptides in bilaterian species

et al. 2019

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In bilaterian species, the amino acid sequence conservation between Insulin related peptides is relatively low except for the cysteine residues involved in the disulphide bonds. In the A chain, the conserved cystein residues are included in a signature motif. Investigating the variations in this motif would give insight into the phylogenetic history of the family. The table presented in this paper contains a large set of insulin-related peptides in bilateral phylogenetic groups (deuterostomian, ecdysozoan, lophotrochozoan). NCBI databases in silico wide screening combined with bibliographic researches provided a framework for identifying and categorising the structural characteristics of these insulin related peptides. The dataset includes NCBI IDs of each sequence with hyperlinks to FASTA format. Moreover, the structural type (α, β or γ), the A chain motif, the total number of cysteins, the C peptide cleavage mode and the potential additional domains (D or E) are specified for each sequence. The data are associated with the research article “Molecular evolution and functional characterisation of insulin-related peptides in molluscs: contributions of Crassostrea gigas genomic and transcriptomic-wide screening” [1]. The table presented here can be found at http://dx.doi.org/10.17632/w4gr8zcpk5.4#file-21c0f6a5-a3e3-4a15-86e0-e5a696458866.

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Molecular evolution and functional characterisation of insulin related peptides in molluscs: Contributions of Crassostrea gigas genomic and transcriptomic-wide screening

Cited by 24 publications

References 92 publications

In silico prediction of neuropeptides from the neural ganglia of Pacific abalone Haliotis discus hannai (Mollusca: Gastropoda)

In silico prediction of neuropeptides from the neural ganglia of Pacific abalone Haliotis discus hannai (Mollusca: Gastropoda)

The “IAG-Switch”—A Key Controlling Element in Decapod Crustacean Sex Differentiation

Data for evolutive analysis of insulin related peptides in bilaterian species

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