Isolation of two AKH‐related peptides from cicadas

Veenstra, Jan A.; Hagedorn, Henry H.

doi:10.1002/arch.940290406

Cited by 18 publications

(11 citation statements)

References 9 publications

(11 reference statements)

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“…However, in the main fraction, the AKH from N. glauca was unequivocally detected by its characteristic sodium and potassium adduct masses in MALDI‐MS studies and its sequence was assigned by ESI MS; comparative retention studies on RP‐HPLC with other AKH peptides confirmed it as being an octapeptide, Anaim‐AKH (primary sequence shown in Table 2), which had previously been isolated from A. imperator (Gäde et al ., 1994). An identical N ‐terminal sequence, but extended at the C ‐terminus by the amino acid residues Gly and Asn, is found in a number of homopteran cicada species and denoted Placa‐HrTH (Table 2) (Gäde & Janssens, 1994; Raina et al ., 1995; Veenstra & Hagedorn, 1995). Although the AKH peptides of P. apterus , denoted Pyrap‐AKH and Peram‐CAH‐II, are also octapeptides, they differ from Anaim‐AKH by three and four amino acid substitutions, respectively (Table 2).…”

Section: Resultssupporting

confidence: 92%

Substrate usage and its regulation during flight and swimming in the backswimmer, Notonecta glauca

GÄde

Auerswald

Predel

et al. 2004

Physiological Entomology

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Abstract. The metabolites that are generally used by insects during exercise are present in quite different concentrations in the haemolymph of the backswimmer Notonecta glauca L. Lipids are most abundant (between 10 and 20 mg/mL), whereas carbohydrates (2–3 mg/mL) and proline (approximately 1 mg/mL) are at very low concentrations. Injection of an extract of conspecific corpora cardiaca causes pronounced hyperlipaemia in the backswimmer. A neuropeptide with the same effect was isolated from the corpora cardiaca in a single high‐performance liquid chromatography (HPLC) step; the primary sequence was deduced from mass spectrometric measurements (matrix‐assisted laser desorption/ionization‐time of flight and electrospray quadrupol time‐of‐flight mass spectrometry) of whole corpora cardiaca, and the mass was confirmed in the HPLC fraction that had adipokinetic activity. The biologically active octapeptide has the sequence pGlu‐Val‐Asn‐Phe‐Ser‐Pro‐Ser‐Trp amide, which was characterized previously from the corpora cardiaca of the Emperor dragonfly, Anax imperator, and denoted Anaim‐adipokinetic hormone (AKH). The synthetic Anaim‐AKH peptide causes lipid mobilization when injected at a dose of 1 pmol into N. glauca. When other synthetic AKH members that occur in Hemiptera are injected into N. glauca at the same dose, the hyperlipaemic responses are significantly lower than after injection of Anaim‐AKH. Because only lipids increase upon activity, such as continuous swimming for 1 h or during a 1‐h rest period after a 3‐min flight episode in the laboratory, it is assumed that Anaim‐AKH serves as a true adipokinetic hormone in the backswimmer during bouts of natural swimming and flight.

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Section: Resultssupporting

confidence: 92%

Substrate usage and its regulation during flight and swimming in the backswimmer, Notonecta glauca

GÄde

Auerswald

Predel

et al. 2004

Physiological Entomology

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“…Concerning other Hemiptera, the database is very small, with AKHs isolated and sequenced from only two cicadomorphan families, namely the Cicadidae (five species) and Cercopidae (one species). Studies on Cicadidae reveal that five cicada species each contain two decapeptides designated as Placa‐HrTH‐I and II; enigmatically, these peptides are separable by HPLC yet they have the same mass and primary sequence (pEVNFSPSWGN amide); thus, a hither‐to unknown post‐translational modification is suspected (Gäde & Janssens, 1994; Raina et al , 1995; Veenstra & Hagedorn, 1995). In Locris arithmetica (family Cercopidae), the AKHs Peram‐CAH‐I and Pyrap‐AKH are present (Gäde, 2008).…”

Section: Discussionmentioning

confidence: 99%

The adipokinetic hormones of Heteroptera: a comparative study

Kodrı́k

Marco

Šimek

et al. 2010

Physiological Entomology

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The adipokinetic hormones (AKHs) from 15 species of heteropteran Hemiptera (encompassing eight families, six superfamilies and three infraorders) have been isolated and structurally identified using liquid chromatography coupled with mass spectrometry. None of the structures are novel and all are octapeptides. These peptide sequence data are used, together with the previously available AKH sequence data on Heteroptera, to create a larger dataset for comparative analyses. This results, in total, in AKH sequences from 30 species (spanning 13 families), which are used in a matrix confronted with the current hypotheses on the phylogeny of Heteroptera. The expanded dataset shows that all heteropterans have octapeptide AKHs; three species have two AKHs, whereas the overwhelming majority have only one AKH. From a total of 11 different AKH peptides known from Heteroptera to date, three AKHs occur frequently: Panbo‐red pigment‐concentrating hormone (RPCH) (×10), Schgr‐AKH‐II (×6) and Anaim‐AKH (×4). The heteropteran database also suggests that particular AKH variants are family‐specific. The AKHs of Heteroptera: Pentatomomorpha (all terrestrial) are not present in Nepomorpha (aquatic) and Gerromorpha: Gerridae (semiaquatic); AKHs with a Val in position 2 are absent in the Pentatomomorpha (only AKHs with Leu2 are present), whereas Val2 predominates in the nonterrestrial species. An unexpected diversity of AKH sequences is found in Nepomorpha, Nepoidea, Nepidae and Nepinae, whereas Panbo‐RPCH (which has been identified in all infraorders of decapod crustaceans) is present in all analysed species of Pentatomidae and also in the only species of Tessaratomidae investigated. The molecular evolution of Heteroptera with respect to other insect groups and to crustaceans is discussed

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“…This modification is unique because it is not the common O-glycosylation of serine or threonine, or N-glycosylation of asparagine residues, instead the hexose is thought to be linked by C-glycosylation to the C-2 atom of the indole ring of tryptophan (as shown to occur in human ribonuclease [12]). Another, as yet unidentified, modification for an AKH member isolated from the corpora cardiaca of cicadas has also been postulated independently by three research groups [13][14][15].…”

Section: Introductionmentioning

confidence: 88%

Unique translational modification of an invertebrate neuropeptide: a phosphorylated member of the adipokinetic hormone peptide family

GÄde

Šimek

Clark

et al. 2006

Biochemical Journal

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Separation of an extract of corpora cardiaca from the protea beetle, Trichostetha fascicularis, by single-step RP (reverse-phase)-HPLC and monitoring of tryptophan fluorescence resulted in two distinctive peaks, the material of which mobilized proline and carbohydrates in a bioassay performed using the beetle. Material from one of these peaks was; however, inactive in the classical bioassays of locusts and cockroaches that are used for detecting peptides belonging to the AKH (adipokinetic hormone) family. After enzymatically deblocking the N-terminal pyroglutamic acid (pGlu) residue in the peptide material and sequencing by Edman degradation, a partial sequence was obtained: (pGlu)-Ile-Asn-Met-Thr-Xaa-Gly-Trp. The complete sequence was deduced from ESI-MS(n) (electrospray ionization multi-stage-MS); position six was identified as a phosphothreonine residue and the C-terminus is amidated. The peptide, code-named Trifa-CC, was chemically synthesized and used in confirmatory experiments to show that the primary structure had been correctly assigned. To our knowledge, this is the first report of a phosphorylated invertebrate neuropeptide. Synthetic Trifa-CC co-elutes with the natural peptide, found in the gland of the protea beetle, after RP-HPLC. Moreover, the natural peptide can be dephosphorylated by alkaline phosphatase and the product of that reaction has the same retention time as a synthetic nonphosphorylated octapeptide which has the same sequence as Trifa-CC. Finally, synthetic Trifa-CC has hypertrehalosaemic and hyperprolinaemic biological activity in the protea beetle, but even high concentrations of synthetic Trifa-CC are inactive in locusts and cockroaches. Hence, the correct peptide structure has been assigned. Trifa-CC of the protea beetle is an unusual member of the AKH family that is unique in its post-translational modification. Since it increases the concentration of carbohydrates and proline in the haemolymph when injected into the protea beetle, and since these substrates are also used during flight, we hypothesize that Trifa-CC controls the mobilization of these metabolites in the protea beetle.

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Isolation of two AKH‐related peptides from cicadas

Cited by 18 publications

References 9 publications

Substrate usage and its regulation during flight and swimming in the backswimmer, Notonecta glauca

Substrate usage and its regulation during flight and swimming in the backswimmer, Notonecta glauca

The adipokinetic hormones of Heteroptera: a comparative study

Unique translational modification of an invertebrate neuropeptide: a phosphorylated member of the adipokinetic hormone peptide family

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