scholarly journals The fruitfly Drosophila melanogaster contains a novel charged adipokinetic-hormone-family peptide

1990 ◽  
Vol 269 (2) ◽  
pp. 315-320 ◽  
Author(s):  
M H Schaffer ◽  
B E Noyes ◽  
C A Slaughter ◽  
G C Thorne ◽  
S J Gaskell

A member of the RPCH/AKH (red-pigment-concentrating hormone/adipokinetic hormone) family of arthropod neuropeptides was identified in the fruitfly Drosophila melanogaster, and its structure was determined by automated Edman degradation and m.s. using fast-atom-bombardment ionization and a tandem hybrid instrument capable of high sensitivity. The sequence of this peptide, which we call ‘DAKH’, is pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-NH2 (where pGlu is pyroglutamic acid and Trp-NH2 is tryptophan carboxyamide). H.p.l.c. analyses of extracts of the three body segments revealed that more than 80% of the peptide is contained in the thorax. Although DAKH is typical of family members in its general structure and distribution in the animal, it is unique in containing a residue which is charged under physiological conditions. The evolutionary significance of this change is considered.

1979 ◽  
Vol 34 (11) ◽  
pp. 1044-1046 ◽  
Author(s):  
Gerhard Sandmann ◽  
Karl-Josef Kunert ◽  
Peter Böger

Abstract Two strains of Scenedesmus acutus were found useful to study the influence of bleaching agents on either the greening process or the fully pigmented algal cell during growth. Both physiological conditions exhibit high sensitivity to bleaching herbicides. With this new assay, contrasting bleach­ing effects with the same compound can be found allowing differentiation of the herbicidal action of bleaching agents which apparently is a multifunctional one. Furthermore, the I50 can be determined rather rapidly in a simple graphical method by a Dixon plot. A subsequent application of bleaching herbicides to cultures of the fungus Phycomyces blakesleeanus rules out a possible specific action of the compounds assayed on chlorophyll or photosynthetic redox carriers. This latter assay can show whether or not the herbicides synthesis as is the case with difunon or SAN 9789.


1990 ◽  
Vol 269 (2) ◽  
pp. 309-313 ◽  
Author(s):  
G Gäde ◽  
H Wilps ◽  
R Kellner

A hypertrehalosaemic neuropeptide from the corpora cardiaca of the blowfly Phormia terraenovae has been isolated by reversed-phase h.p.l.c., and its primary structure was determined by pulsed-liquid phase sequencing employing Edman chemistry after enzymically deblocking the N-terminal pyroglutamate residue. The C-terminus was also blocked, as indicated by the lack of digestion when the peptide was incubated with carboxypeptidase A. The octapeptide has the sequence pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-NH2 and is clearly defined as a novel member of the RPCH/AKH (red-pigment-concentrating hormone/adipokinetic hormone) family of peptides. It is the first charged member of this family to be found. The synthetic peptide causes an increase in the haemolymph carbohydrate concentration in a dose-dependent fashion in blowflies and therefore is named ‘Phormia terraenovae hypertrehalosaemic hormone’ (Pht-HrTH). In addition, receptors in the fat-body of the American cockroach (Periplaneta americana) recognize the peptide, resulting in carbohydrate elevation in the blood. However, fat-body receptors of the migratory locust (Locusta migratoria) do not recognize this charged molecule, and thus no lipid mobilization is observed in this species.


1994 ◽  
Vol 302 (2) ◽  
pp. 539-543 ◽  
Author(s):  
M P Janssens ◽  
R Kellner ◽  
G Gde

A member of the adipokinetic hormone family of peptide was identified in the damselflies Pseudagrion inconspicuum and Ischnura senegalensis using a heterologous (in migratory locusts and American cockroaches) and a homologous (in P. inconspicuum) bioassay. After isolation of the peptide by reversed-phase h.p.i.c. of corpora cardiaca, its structure was determined by automated Edman degradation and matrix-assisted laser-desorption ionization m.s. The sequence of a blocked uncharged octapeptide was established: pGlu-Val-Asn-Phe-Thr-Pro-Gly-TrpNH2. One corpus cardiacum of P. inconspicuum contains about 2.4 pmol of this novel peptide. The synthetic peptide was chromatographically indistinguishable from the natural compound, and on injection in low quantities into the damselfly P. inconspicuum, haemolymph levels of lipids were increased. It is concluded that the novel peptide may be involved in controlling lipid mobilization during flight. Hence the peptide is designated Psi-AKH, Pseudagrion inconspicuum adipokinetic hormone.


2016 ◽  
Author(s):  
Kermit K. Murray ◽  
Robert K. Boyd ◽  
Marcos N. Eberlin ◽  
G. John Langley ◽  
Liang Li ◽  
...  

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