scholarly journals Isolation and structure of a novel charged member of the red–pigment-concentrating hormone-adipokinetic hormone family of peptides isolated from the corpora cardiaca of the blowfly Phormia terraenovae (Diptera)

1990 ◽  
Vol 269 (2) ◽  
pp. 309-313 ◽  
Author(s):  
G Gäde ◽  
H Wilps ◽  
R Kellner
Keyword(s):  
Periplaneta Americana ◽  
Fat Body ◽  
Locusta Migratoria ◽  
Reversed Phase ◽  
American Cockroach ◽  
Red Pigment ◽  
Adipokinetic Hormone ◽  
Migratory Locust ◽  
Corpora Cardiaca ◽  
Adipokinetic Hormone Family

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.

scholarly journals A unique charged tyrosine-containing member of the adipokinetic hormone/red-pigment-concentrating hormone peptide family isolated and sequenced from two beetle species

1991 ◽  
Vol 275 (3) ◽  
pp. 671-677 ◽  
Author(s):  
G Gäde
Keyword(s):  
Periplaneta Americana ◽  
Locusta Migratoria ◽  
Structural Features ◽  
American Cockroach ◽  
Beetle Species ◽  
Red Pigment ◽  
Adipokinetic Hormone ◽  
Migratory Locust ◽  
Melolontha Melolontha ◽  
C Terminus

An identical neuropeptide was isolated from the corpora cardiaca of two beetle species, Melolontha melolontha and Geotrupes stercorosus. 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 sequence of this peptide, which is designated Mem-CC, is pGlu-Leu-Asn-Tyr-Ser-Pro-Asp-Trp-NH2. It is a new member of the adipokinetic hormone/red-pigment-concentrating hormone (AKH/RPCH) family of peptides with two unusual structural features: it is charged and contains a tyrosine residue at position 4, where all other family members have a phenylalanine residue. Structure-activity studies in the migratory locust (Locusta migratoria) and the American cockroach (Periplaneta americana) revealed that the peptide was poorly active, owing to its structural uniqueness.

Characterization and Amino Acid Composition of a Hypertrehalosaemic Neuropeptide from the Corpora cardiaca of the Cockroach, Nauphoeta cinerea

1987 ◽  
Vol 42 (3) ◽  
pp. 225-230 ◽  
Author(s):  
Gerd Gäde
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Periplaneta Americana ◽  
Fat Body ◽  
Reversed Phase ◽  
American Cockroach ◽  
Maximum Increase ◽  
Corpora Cardiaca ◽  
Nauphoeta Cinerea

Nauphoeta cinerea corpora cardiaca contain peptide material which is capable of eliciting strong hypertrehalosaemia (maximum increase: 27 mg carbohydrates/ml haemolymph) and fat body glycogen phosphorylase-activation (maximal: 70% of the total phosphorylase activity in the a-form) in the American cockroach, Periplaneta americana. It appears that comparable amounts of bioactive material are stored in the corpora cardiaca of N. cinerea and P. americana. Purifica­tion of a methanolic extract of corpora cardiaca from N. cinerea by reversed-phase HPLC revealed that the hypertrehalosaemic phosphorylase-activating activity is concentrated in a single peak. The amino acid composition of the purified neuropeptide material was determined after acid hydrolysis with HCl and methanesulfonic acid. The analyses demonstrated that the N. cinerea hypertrehalosaemic factor is a decapeptide which contains the following amino acid residues: Asp, Thr, Ser, Glu, Pro, Gly (2), Val, Phe, and Trp.

Adipokinetic Neuropeptides and Flight Metabolism in Three Moth Species of the Families Sphingidae, Saturniidae and Bombycidae

1995 ◽  
Vol 50 (5-6) ◽  
pp. 425-434 ◽  
Author(s):  
Walter Liebrich ◽  
Gerd Gäde
Keyword(s):  
Retention Time ◽  
Periplaneta Americana ◽  
Locusta Migratoria ◽  
Rest Period ◽  
Reversed Phase ◽  
Lipid Levels ◽  
Flight Behaviour ◽  
Corpora Cardiaca ◽  
Rp Hplc ◽  
Moth Species

Methanolic extracts from corpora cardiaca of three moth species, Hippoteon eson (Sphingidae), Imbrasia cytherea (Saturniidae) and Bombyx mori (Bombycidae) show adipokinetic activity in conspecific bioassays. Haemolymph carbohydrates in these moths are not affected. These extracts are also active in heterologous bioassays: haemolymph lipids are increased in Locusta migratoria, whereas a small effect on haemolymph carbohydrates was observed in Periplaneta americana. Therefore, locusts can be used to monitor adipokinetic activity in corpora cardiaca from moth extracts during isolation. The three moth species possess an adipokinetic peptide with the same retention time on reversed phase high performance liquid chromatography (RP -HPLC) as a peptide isolated previously from Manduca sexta, which was code-named Mas-AKH. H. eson contains a second active peak with a similar retention time on RP-HPLC as the hypertrehalosaemic peptide isolated previously from Helicoverpa zea , code-named Hez-HrTH. Both synthetic peptides, Mas-AKH and Hez-HrTH, produce an adipokinetic effect in the three experimental moth species. In H. eson, the haemolymph concentration of Mas-AKH or Hez-HrTH needed to elicit a maximum hyperlipaemic response is about 20 to 30 nᴍ.Flight behaviour in the three moth species is quite different: H. eson is a good hovering flyer, I. cytherea is a comparatively bad flyer and B. mori males show only degenerate flight movements during their mating dance. Haemolymph lipid levels in H. eson decrease drastically during 15 min of flight and return to pre-flight levels in a subsequent rest period. The amount of lipids metabolized during flight is 10.9 mg/gxhr. Haemolymph carbohydrate levels drop during flight, but remain low during the 45 min of recovery. Haemolymph lipids in “dancing” males of B. mori remain constant. In individuals, however, which have low initial lipid levels in the blood, lipid concentrations increase significantly in a subsequent 15 min rest period after “dancing”. Metabolic changes during flight in I. cytherea were not investigated due to this species’ poor flight performance.

Trehalose inhibits the release of adipokinetic hormones from the corpus cardiacum in the African migratory locust, Locusta migratoria, at the level of the adipokinetic cells

1997 ◽  
Vol 153 (2) ◽  
pp. 299-305 ◽  
Author(s):  
P C C M Passier ◽  
H G B Vullings ◽  
J H B Diederen ◽  
D J Van der Horst
Keyword(s):  
Fat Body ◽  
Locusta Migratoria ◽  
Inhibitory Effect ◽  
Dependent Manner ◽  
Corpus Cardiacum ◽  
High Concentration ◽  
High Potassium ◽  
Migratory Locust ◽  
Corpora Cardiaca

Abstract The effect of trehalose at various concentrations on the release of adipokinetic hormones (AKHs) from the adipokinetic cells in the glandular part of the corpus cardiacum of Locusta migratoria was studied in vitro. Pools of five corpora cardiaca or pools of five glandular parts of corpora cardiaca were incubated in a medium containing different concentrations of trehalose in the absence or presence of AKH-release-inducing agents. It was demonstrated that trehalose inhibits spontaneous release of AKH I in a dose-dependent manner. At a concentration of 80 mm, which is the concentration found in the hemolymph at rest, trehalose significantly decreased the release of AKH I induced by 100 μm locustatachykinin I, 10 μm 3-isobutyl-1-methylxanthine (IBMX) or high potassium concentrations. The specificity of the effect of trehalose was studied by incubating pools of corpora cardiaca with the non-hydrolyzable disaccharide sucrose or with glucose, the degradation product of trehalose, both in the presence and absence of 10 μm IBMX. Sucrose had no effect at all on the release of AKH I, whereas glucose strongly inhibited its release. The results point to the inhibitory effect of trehalose on the release of AKH I being exerted, at least partly, at the level of the adipokinetic cells, possibly after its conversion into glucose. The data presented in this study support the hypothesis that in vivo the relatively high concentration of trehalose (80 mm) at rest strongly inhibits the release of AKHs. At the onset of flight, the demand for energy substrates exceeds the amount of trehalose that can be mobilized from the fat body and consequently the trehalose concentration in the hemolymph decreases. This relieves the inhibitory effect of trehalose on the release of AKHs, which in turn mobilize lipids from the fat body. Journal of Endocrinology (1997) 153, 299–305

On the release and action of the hypertrehalosaemic hormone from the cockroach nauphoeta cinerea

1988 ◽  
Vol 43 (1-2) ◽  
pp. 108-116 ◽  
Author(s):  
Gerd Gäde
Keyword(s):  
Glycogen Phosphorylase ◽  
Periplaneta Americana ◽  
Fat Body ◽  
Neurosecretory Cells ◽  
American Cockroach ◽  
Corpora Cardiaca ◽  
Nauphoeta Cinerea ◽  
Dose Dependent Fashion ◽  
Dose Dependent

The corpora cardiaca of the cockroach Nauphoeta cinerea contain a hypertrehalosaemic hormone (HTH) which is chemically characterized as a blocked decapeptide. The synthetic HTH shows the same chromatographic behaviour as the material isolated from corpora cardiaca. The synthetic peptide causes hypertrehalosaemia and fat body glycogen phosphorylase-activation in N. cinerea as well as in the American cockroach, Periplaneta americana in a dose-dependent fashion. It is calculated that one gland from N. cinerea stores about 50 pmol of HTH. Roughly 10% of the total available hormone in the gland is released in vitro during exposure to an elevated potassium saline which causes depolarization of the neurosecretory cells

INHIBITORS OF CARBONIC ANHYDRASE IN THE AMERICAN COCKROACH, PERIPLANETA AMERICANA (L.)

1956 ◽  
Vol 34 (1) ◽  
pp. 68-74 ◽  
Author(s):  
Ann D. Anderson ◽  
Ralph B. March
Keyword(s):  
Carbonic Anhydrase ◽  
Periplaneta Americana ◽  
Fat Body ◽  
Aqueous Media ◽  
Carbonic Anhydrase Activity ◽  
American Cockroach ◽  
Tissue Homogenates ◽  
Organic Insecticides ◽  
Cell Fragments

Carbonic anhydrase activity has been demonstrated in vitro in preparations of the head, fat body, and gut of the American cockroach, Periplaneta americana (L.), and in the adult housefly, Musca domestica L. The insect factor, which is soluble in aqueous media and can be separated from the particulate cell fragments of insect tissue homogenates is heat labile and sensitive to cyanide inactivation. It is strongly inhibited by sulphanilamide, p-aminoethylphenyl-sulphonamide, and p-chlorphenylsulphonamide. No inhibition has been found with N-substituted sulphonamides or with any of the organic insecticides examined, including DDT, lindane, dieldrin, nicotine, rotenone, pyrethrins, and para-oxon. Sensitivity of carbonic anhydrase to sulphonamides having an intact—SO2NH2 group is also characteristic of mammalian preparations. The data indicate that inhibition of insect carbonic anhydrase cannot be an important factor in the mode of action of DDT or other organic insecticides.

scholarly journals A novel adipokinetic octapeptide found in the damselflies Pseudagrion inconspicuum and Ischnura senegalensis

1994 ◽  
Vol 302 (2) ◽  
pp. 539-543 ◽  
Author(s):  
M P Janssens ◽  
R Kellner ◽  
G Gde
Keyword(s):  
Synthetic Peptide ◽  
Natural Compound ◽  
Laser Desorption ◽  
Reversed Phase ◽  
Edman Degradation ◽  
The Novel ◽  
Laser Desorption Ionization ◽  
Corpus Cardiacum ◽  
Adipokinetic Hormone ◽  
Adipokinetic Hormone Family

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.

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