On the Delayed Pupation of the Fleshfly, Sarcophaga Peregrina Robineau-Desvoidy

Ohtaki, Tetsuya

doi:10.7883/yoken1952.19.97

Cited by 119 publications

(40 citation statements)

References 6 publications

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“…The flesh fly (Sarcophaga peregrina) was reared by the method of Ohtaki [ 5 ] . The physiological age of the insect was controlled easily by wet/dry treatment.…”

Section: Animalsmentioning

confidence: 99%

Regulation of the Expression of Cathepsin B in Sarcophaga Peregrina (Flesh Fly) at the Translational Level During Metamorphosis

Yano

Takahashi

Kurata

et al. 1995

European Journal of Biochemistry

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Previously, we reported that cathepsin B of pupal hemocytes participates in dissociation of the fat body of Sarcophaga larvae at metamorphosis. In this study, we demonstrated that the amount of cathepsin B in hemocytes was controlled at the translational level, i.e. larval hemocytes stored a significant amount of untranslated cathepsin B mRNA. When the larvae pupated, translation of the mRNA commenced, resulting in accumulation of cathepsin B. Our results indicate that the 3'-untranslated region (3'-UTR) of this mRNA is necessary for the repression of its translation in a rabbit reticulocyte lysate. We detected the 3'-UTR binding protein in the lysate of larval hemocytes, but not in the pupal hemocytes. The role of this protein in the translation of cathepsin B mRNA is discussed.Keywords: translational regulation; cathepsin B ; RNA binding; 3' untranslated region; flesh fly.In holometabolous insects, metamorphosis involves dramatic morphological changes. This is a scrap and build process in which most larval tissues are broken down and adult structures develop from the imaginal discs. Previously, we demonstrated that larval fat bodies are dissociated to adipocytes when incubated with pupal hemocytes in vitro, but not with larval hemocytes [l, 21. This system mimics decomposition of the fat body in v i v a Subsequent studies revealed that cathepsin B was released from pupal hemocytes when they interacted with larval fat bodies, and that this enzyme alone digested the basement membrane of the larval fat body, resulting in its dissociation [I]. Thus, it was confirmed that cathepsin B is a key enzyme necessary for fat body dissociation.Sarcophaga cathepsin B was purified from pupal hemocytes to near homogeneity, and shown to have unique substrate specificity [3]. Immunoblotting and immunofluorescence studies showed that the amount of cathepsin B increased markedly on pupation, and that the enzyme was stored in certain granules within hemocytes [l]. A cDNA clone of Surcophaga cathepsin B was subsequently isolated [4].As the content of cathepsin B in larval hemocytes is very low compared to that in pupal hemocytes, we have been interested in the mechanism responsible for efficient biosynthesis of cathepsin B in pupal hemocytes. This paper reports findings which suggest that the biosynthesis of Sarcophaga cathepsin B in pupal hemocytes is regulated at the translational level. We showed that the translational repression of cathepsin B mRNA in vitro required its 3'-untranslated region (3'-UTR). Furthermore, we detected a 3'-UTR-specific binding protein only in extracts of larval hemocytes, suggesting that this protein is a translational repressor of cathepsin B mRNA. MATERIALS AND METHODS Animals.The flesh fly (Sarcophaga peregrina) was reared by the method of Ohtaki [ 5 ] . The physiological age of the insect was controlled easily by wet/dry treatment. When third-instar larvae were transferred from wet to dry conditions, pupation began 16 h later. Third-instar larvae and early pupae were used for the experiments. Embr...

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“…The flesh fly (Sarcophaga peregrina) was reared by the method of Ohtaki [ 5 ] . The physiological age of the insect was controlled easily by wet/dry treatment.…”

Section: Animalsmentioning

confidence: 99%

Regulation of the Expression of Cathepsin B in Sarcophaga Peregrina (Flesh Fly) at the Translational Level During Metamorphosis

Yano

Takahashi

Kurata

et al. 1995

European Journal of Biochemistry

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“…In flesh flies, pupariation is inhibited when mature larvae are subjected to wet conditions (water treatment), but their development resumes after the larvae were transferred to dry conditions (Ohtaki, 1966;Moribayashi et al, 1996Moribayashi et al, , 2002Yoder et al, 2006). Ohtaki (1986) and Moribayashi et al (1992) showed that the terminal organ located at the anterior end of the first segment of the larval body recognizes water, and this organ then transmits a signal to prevent the release of ecdysteroids that promote pupariation.…”

Section: Introductionmentioning

confidence: 99%

Alteration of the pupal diapause program and regulation of larval duration by photoperiod in the flesh fly Sarcophaga similis Meade (Diptera: Sarcophagidae)

Goto

Numata

2009

Appl. Entomol. Zool.

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Using a water treatment technique that extends the larval period of flesh flies, we investigated the effect of photoperiodic exposure on the alteration of the pupal diapause program and regulation of larval duration in the flesh fly Sarcophaga similis Meade (Diptera: Sarcophagidae). Exposure to only 4 cycles of long days successfully altered the developmental program from diapause to nondiapause, and short days altered the nondiapause developmental program to a diapause program. Larvae recognized all photoperiods of 14L10D, 15L9D, and 16L8D as long days, but their diapause-averting effects were different, i.e., 16L8D showed the strongest effect, 14L10D showed the weakest, and 15L9D showed an intermediate effect. These results indicate that larvae can discriminate long days quantitatively. S. similis also showed a clear photoperiodic response in the larval stage, i.e., larvae reared under short-day conditions pupariated later than those reared under long-day conditions. When diapause-destined larvae were exposed to 3 cycles of long days, some larvae altered their developmental program from diapause to nondiapause and pupariated significantly earlier than individuals destined to diapause.

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“…Larvae were held under these conditions for 3 days at 25°C with frequent (3-5 times/day) water changes. This "wet" treatment temporarily inhibits the release of ecdysteroids until the larvae are placed in dry conditions, thereby synchronizing pupariation (Ohtaki, 1966).…”

Section: Insect Rearingmentioning

confidence: 99%

Characterization and biochemical analyses of venom from the ectoparasitic waspNasonia vitripennis (Walker) (hymenoptera: Pteromalidae)

Rivers

Uçkan

Ergın

2005

Arch. Insect Biochem. Physiol.

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During parasitism, the ectoparasitic wasp Nasonia vitripennis (Walker) (Hymenoptera: Pteromalidae) induces a developmental arrest in host pupae that is sustained until the fly is either consumed by developing larvae or the onset of death. Bioassays using fluids collected from the female reproductive system (calyx, alkaline gland, acid gland, and venom reservoir) indicated that the venom gland and venom reservoir are the sources of the arrestant and inducer(s) of death. Infrared spectroscopic analyses revealed that crude venom is acidic and composed of amines, peptides, and proteins, which apparently are not glycosylated. Reversed phase high performance liquid chromatography (HPLC) and sodium dodecyl polyacrylamide gel electrophoresis (SDS-PAGE) confirmed the proteinaceous nature of venom and that it is composed mostly of mid to high molecular weight proteins in the range of 13 to 200.5 kilodaltons (kDa). Ammonium sulfate precipitation and centrifugal size exclusion membranes were used to isolate venom proteins. SDS-PAGE protein profiles of the isolated venom fractions displaying biological activity suggest that multiple proteins contribute to arresting host development and eliciting death. Additionally, HPLC fractionation coupled with use of several internal standards implied that two of the low molecular weight proteins were apamin and histamine. However, in vitro assays using BTI-TN-5B1-4 cells contradict the presence of these agents. Abbreviations used: HPLC = high performance liquid chromatography; I.R. = infrared spectroscopy; kDa = kilodalton; LC 99 = lethal concentration to kill 100% of population; LD = light-dark; MWCO = molecular weight cutoff; SDS-PAGE = sodium dodecyl sulfate polyacrylamide gel electrophoresis; TFA = trifluoroacetic acid; VRE = venom reservoir equivalent.

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On the Delayed Pupation of the Fleshfly, Sarcophaga Peregrina Robineau-Desvoidy

Cited by 119 publications

References 6 publications

Regulation of the Expression of Cathepsin B in Sarcophaga Peregrina (Flesh Fly) at the Translational Level During Metamorphosis

Regulation of the Expression of Cathepsin B in Sarcophaga Peregrina (Flesh Fly) at the Translational Level During Metamorphosis

Alteration of the pupal diapause program and regulation of larval duration by photoperiod in the flesh fly Sarcophaga similis Meade (Diptera: Sarcophagidae)

Characterization and biochemical analyses of venom from the ectoparasitic waspNasonia vitripennis (Walker) (hymenoptera: Pteromalidae)

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