کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2800100 | 1568899 | 2014 | 15 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Identification of the first neuropeptides from the Amphipoda (Arthropoda, Crustacea) Identification of the first neuropeptides from the Amphipoda (Arthropoda, Crustacea)](/preview/png/2800100.png)
• Transcriptome data for the Amphipoda were mined for putative neuropeptides.
• Peptide-encoding transcripts from three species were identified.
• 139 Distinct mature peptides were predicted – the first from the Amphipoda.
• Atypical orcokinin, PDH and SIFamide isoforms were discovered.
• The data provide the first resource for studying peptidergic control in amphipods.
Despite being used as models in the field of ecotoxicology, including use in studies of endocrine disruption, little is known about the hormonal systems of amphipods, particularly their peptidergic signaling systems. Here, transcriptome shotgun assembly (TSA) sequences were used to predict the structures of the first neuropeptides from members of this crustacean order. Using a well-established workflow, BLAST searches of the extant amphipod TSA data were conducted for putative peptide-encoding transcripts. The pre/preprohormones deduced from the identified TSA sequences were then used to predict the mature structures of amphipod neuropeptides. In total, 43 putative peptide-encoding transcripts were identified from three amphipods, Echinogammarus veneris, Hyalella azteca and Melita plumulosa. Collectively, 139 distinct mature peptides (110 from E. veneris alone) were predicted from these TSA sequences. The identified peptides included members of the adipokinetic hormone/red pigment concentrating hormone, allatostatin A, allatostatin B, allatostatin C, bursicon α, bursicon β, crustacean hyperglycemic hormone, diuretic hormone 31, FLRFamide, molt-inhibiting hormone, myosuppressin, neuroparsin, neuropeptide F, orcokinin, pigment dispersing hormone (PDH), proctolin, RYamide, SIFamide, sulfakinin and tachykinin-related peptide families. Of particular note were the identifications of orcokinins possessing SFDEIDR– rather than the typical NFDEIDR– amino-termini, e.g. SFDEINRSNFGFN, a carboxyl-terminally amidated orcokinin, i.e. SFDEINRSNFGFSamide, PDHs longer than the stereotypical 18 amino acids, e.g. NSELLNTLLGSKSLAALRAAamide, and a 13 rather than 12 amino acid long SIFamide, i.e. GPYRKPPFNGSIFamide. These data not only provide the first descriptions of native amphipod neuropeptides, but also represent a new resource for initiating investigations of peptidergic signaling in the Amphipoda.
Journal: General and Comparative Endocrinology - Volume 206, 15 September 2014, Pages 96–110