Age-dependent changes of fat body stores and the regulation of fat body lipid synthesis and mobilisation by adipokinetic hormone in the last larval instar of the cricket, Gryllus bimaculatus

2008 ◽  
Vol 54 (10-11) ◽  
pp. 1404-1412 ◽  
Author(s):  
Anurag N. Anand ◽  
Matthias W. Lorenz
1983 ◽  
Vol 38 (1-2) ◽  
pp. 112-125 ◽  
Author(s):  
Franz Römer ◽  
Ilona Eisenbeis

The mode of growth of several tissues in Gryllus bimaculatus was investigated during postembryonic development by cytophotometric methods. In contrast to the situation in holo- metabolous insects, the tissues growing by endomitosis reach only moderate levels of polyploidy. In this case the growth of tissues is achieved by mitotic divisions of small cells with subsequent polyploidization. The time courses of DNA synthesis were measured within the 3rd and, for comparison, the 8th larval instar by incorporation of labelled thymidine followed by autoradiography. Hemocytes, cells of the regeneration crypts of the midgut, gonads and nervous tissue showed a continuous incorporation rate; by contrast, DNA synthesis in other tissues was confined to a given time within the moulting cycle. The changes in moulting hormone titre of the 3rd larval instar were investigated. The quantities of ecdysone and 20-OH-ecdysone were estimated by radioimmunoassay, and the hormones were identified by high pressure liquid chromatography (HPLC). The titre changes in time with at least 2 distinct maxima. The DNA synthesis periods are correlated with the hormone peaks, that of epidermis and tracheae with the first peak, and that of pylorus, ileum, rectum, Malpighian tubules and fat body with the second. DNA synthesis in prothoracic glands and oenocytes exhibits a time course that is the inverse of the hormone-secretion time course. The question whether moulting hormones have an influence on DNA synthesis is discussed.


Peptides ◽  
2014 ◽  
Vol 58 ◽  
pp. 65-73 ◽  
Author(s):  
Marek Gołębiowski ◽  
Magdalena Cerkowniak ◽  
Aleksandra Urbanek ◽  
Małgorzata Słocińska ◽  
Grzegorz Rosiński ◽  
...  

Endocrinology ◽  
2012 ◽  
Vol 153 (7) ◽  
pp. 3111-3122 ◽  
Author(s):  
Takahiro Konuma ◽  
Nobukatsu Morooka ◽  
Hiromichi Nagasawa ◽  
Shinji Nagata

Adipokinetic hormone (AKH) is a peptide hormone that regulates the nutritional state in insects by supporting the mobilization of lipids. In the present study, we manipulated AKH signaling to evaluate how metabolic state regulates feeding in an orthopteran insect, the two-spotted cricket, Gryllus bimaculatus. This was accomplished by RNA interference (RNAi) targeting the receptor gene for AKH [G. bimaculatus AKHR (GrybiAKHR)]. We found that the knockdown of GrybiAKHR by AKHR-double-stranded RNA treatment decreased the levels of 1,2-diacylglycerol and trehalose in the hemolymph, whereas it increased the level of triacylglycerol in the fat body. In addition, the knockdown of GrybiAKHR enhanced starvation resistance and increased food intake. Furthermore, direct observation of GrybiAKHRRNAi crickets revealed that the knockdown of GrybiAKHR increased feeding frequency but did not alter meal duration, whereas locomotor activity decreased. The increased frequency of feeding by GrybiAKHRRNAi crickets eventually resulted in an increase of food intake. These data demonstrate that the regulation of the metabolic state by AKH signaling affects feeding frequency, probably through nutritional control.


Author(s):  
Rahma R. Z. Mahdy ◽  
Shaimaa A. Mo’men ◽  
Marah M. Abd El-Bar ◽  
Emad M. S. Barakat

Abstract Background Insect lipid mobilization and transport are currently under research, especially lipases and lipophorin because of their roles in the production of energy and lipid transport at a flying activity. The present study has been conducted to purify intracellular fat body lipase for the first time, from the last larval instar of Galleria mellonella. Results Purification methods by combination of ammonium sulfate [(NH4)2SO4] precipitation and gel filtration using Sephadex G-100 demonstrated that the amount of protein and the specific activity of fat body lipase were 0.008633 ± 0.000551 mg/ml and 1.5754 ± 0.1042 μmol/min/mg protein, respectively, with a 98.9 fold purity and recovery of 50.81%. Hence, the sephadex G-100 step was more effective in the purification process. SDS-PAGE and zymogram revealed that fat body lipase showed two monomers with molecular weights of 178.8 and 62.6 kDa. Furthermore, biochemical characterization of fat body lipase was carried out through testing its activities against several factors, such as different temperatures, pH ranges, metal ions, and inhibitors ending by determination of their kinetic parameters with the use of p-nitrophenyl butyrate (PNPB) as a substrate. The highest activities of enzyme were determined at the temperature ranges of 35–37 °C and 37–40 °C and pH ranges of 7–9 and 7–10. The partially purified enzyme showed significant stimulation by Ca2+, K+, and Na+ metal ions indicating that fat body lipase is metalloproteinase. Lipase activity was strongly inhibited by some inhibitors; phenylmethylsulfonyl fluoride (PMSF), ethylene-diaminetetractic acid (EDTA), and ethylene glycoltetraacetic acid (EGTA) providing evidence of the presence of serine residue and activation of enzymes by metal ions. Kinetic parameters were 0.316 Umg− 1 Vmax and 301.95 mM Km. Conclusion Considering the purification of fat body lipase from larvae and the usage of some inhibitors especially ion chelating agents, it is suggested to develop a successful control of Galleria mellonella in near future by using lipase inhibitors.


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.


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