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Dragonfly Erythemis simplicicollis contains a novel adipokinetic neuropeptide
Author(s) -
Gäde Gerd,
Kellner Roland
Publication year - 1999
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(1999)40:2<99::aid-arch4>3.0.co;2-4
Subject(s) - adipokinetic hormone , edman degradation , peptide , biology , hemolymph , biochemistry , cockroach , peptide sequence , neuropeptide , gene , receptor , ecology
We have isolated a novel member of the adipokinetic hormone family of peptides from a methanolic extract of corpora cardiaca of the libellulid dragonfly Erythemis simplicicollis by using a single‐step reversed‐phase high performance liquid chromatography method and monitoring biological activity in various heterologous bioassays and a homologous one. The sequence, as determined by Edman degradation and mass spectrometry, was of an uncharged blocked octapeptide: pGlu‐Leu‐Asn‐Phe‐Thr‐Pro‐Ser‐Trp amide. The structure was confirmed by chemical synthesis. The synthetic peptide increased hemolymph lipids in the dragonfly and was active in another libellulid ( Orthetrum julia‐falsum ) as well, but to a lesser extent than the conspecific peptide Lia‐AKH, which is an isoform of the novel peptide differing by a Val (instead of Leu) at position 2. Since lipids are apparently used as substrate for muscle contraction during flight of Erythemis simplicicollis and the native peptide induces lipid mobilization, this novel peptide is denoted Ers‐AKH. Arch. Insect Biochem. Physiol. 40:99–106, 1999. © 1999 Wiley‐Liss, Inc.