The occurrence of a premature form of egg-specific protein in vitellogenic follicles ofBombyx mori

Indrasith, Leslie S.; Sasaki, Takuji; Yaginuma, Toshinobu; Yamashita, Okitsugu

doi:10.1007/bf00692723

Cited by 36 publications

(26 citation statements)

References 21 publications

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“…The temporary elevation of specific activity during purification of the proteinase suggests the removal of the hypothetical endogenous inhibitor(s). Recently, a trypsin-like protease was purified from Bornhyx eggs [34]. This enzyme was rather specific for egg-specific protein, with limited sites of cleavage.…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of a cysteine proteinase from silkworm eggs

Kageyama

Takahashi

1990

European Journal of Biochemistry

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Eggs of the silkworm, Bombyx mori, contain a high level of a proteinase which is most active in acidic pH region. The proteinase was purified from an extract of eggs by a six-step procedure which included conventional chromatographic fractionations. The molecular mass of the proteinase was estimated to be 350 kDa by gel filtration and 47 kDa by electrophoresis on sodium dodecyl sulfate/polyacrylamide gels, suggesting an octameric structure. The amino acid composition was found to resemble that of mammalian lysosomal cysteine proteinases, in particular cathepsin L. The NH2-terminal 10-residue sequence is Val-Gln-Phe-Phe-Asp-Leu-Val-Lys-Glu-Glu-.The enzyme appears to be a member of the class of cysteine proteinases since it was strongly inhibited by sulfkydrylreactive compounds and N-[N-(1,3-trans-carboxyoxiran-2-carbonyl)-~-leucyl]-agmatine (E-64). The enzyme hydrolyzed various protein substrates, such as hemoglobin, vitellogenin, vitellin, and lipophorin, with maximal activity around pH 3 -3.5. The specificity of the cleavage sites in the oxidized B chain of insulin was rather well defined and there was high affinity for hydrophobic residues at the P2 and P3 positions. The cysteine proteinase is thought to be involved in protein degradation during embryonic development of silkworm eggs.Silkworm eggs contain high levels of yolk proteins such as vitellin and egg-specific protein [l]. Since these proteins are known to be utilized during embryogenesis, proteinases are thought to be involved in the catabolism of such proteins [2]. Proteinases from insect cells and tissues have been studied by various authors [3, 41. However, at least in part because of the difficulties in obtaining sufficient starting material, the information about these enzymes is much less extensive than that which has been published about mammalian proteinases. lntracellular proteinases, such as cathepsins B, H, L, and D, are present in mammalian lysosomes and play a significant role in the intracellular degradation of proteins [5]. The occurrence of these proteinases in insects is still unproven and remains to be clarified.We reported previously that silkworm eggs contain high levels of activity associated with cysteine proteinases [6]. In our efforts to learn more about the role of proteinases in the developing embryo, we have purified and characterized a cysteine proteinase from silkworm eggs. It is unusual in its high molecular mass and its maximum activity around pH 3.0. The amino acid composition and proteolytic specificity, however, are rather similar to those of other cysteine proteinases such as cathepsin L. EXPERIMENTAL PROCEDURES MaterialsEggs of the silkworm (Bombyx mori) were obtained by extraction from the fully matured ovaries of female moths. They were stored frozen at -20°C until use. Bovine hemoglobin was purchased from Worthington, synthetic chromogenic peptides, synthetic oligopeptides, microbial inhibitors were obtained from the Protein Research Foundation, Osaka; DEAE-cellulose (DE-32) from Whatman, DEAE-Toyopearl from Toso...

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Section: Discussionmentioning

confidence: 99%

Purification and characterization of a cysteine proteinase from silkworm eggs

Kageyama

Takahashi

1990

European Journal of Biochemistry

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“…Shekari et al (2008) found similar results after treatment of Xanthogaleruca luteola larvae with a plant extract. One of the main reasons for reduction in ovarian size in treated insects by JH, JHA, or growth regulator of plant origin, is the lack of materials supplied through hemolymph to the growing ovaries (Telfer et al 1981) or due to the lack of materials made by the ovaries themselves (Indrasith et al 1988). The lack of compounds like proteins, lipids, and carbohydrates may lead to abnormal oogenesis (Kunkel and Nordin 1985;Kanost et al 1990).…”

Section: Resultsmentioning

confidence: 99%

Physiological and Biochemical Effect of Pyriproxyfen on Indian Meal Moth Plodia Interpunctella (Hübner) (Lepidoptera: Pyralidae)

Ghasemi¹,

Sendi²,

Ghadamyari³

2010

Journal of Plant Protection Research

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Insect growth regulators generally have a selective effect on the target insects and have practically no apparent side effect on non-target organisms especially vertebrates. Hence, insect growth regulators could be a suitable choice to control pests in stored products. Ten-day-old larvae of Indian meal moth Plodia interpunctella (Hübner) were expressed to the juvenile hormone analogue pyriproxyfen in order to have an effect on growth, metamorphosis, reproduction, lipid and protein contents of ovaries. The larvae were treated by 0.02, 0.04, 0.08, 0.16, and 0.3 ppm of JHA in an artificial diet where controls received acetone alone. The results indicated significant differences in duration of growth, mean longevity of hatched adults, percentage of emerged normal adults, abnormal pupae, hatched larvae and mean oviposition ratein addition to the lipid and protein of ovaries compared to the controls. An inhibition concentration of fifty (IF 50 ) for prevention of emerging adults was recorded 0.134 ppm. Pyriproxyfen caused significant defects in the legs and wings of some adults and sever morphological changes in the ovaries of emerged adults. The results showed that pyriproxyfen may be applied as an insecticide to decrease the damage caused by Indian meal moth on stored products. Pyriproxyfen can be used with low side effects to humans.

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“…In contrast, the mechanisms of degradation of yolk proteins have received considerably less attention. Several enzymes that participate in hydrolysis of yolk proteins in insect embryos have been recently described (8)(9)(10)(11). However, the origin of these enzymes and the time of their delivery into yolk bodies are unknown.…”

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confidence: 99%

“…The mosquito VCP is different from proteases known to hydrolyze yolk proteins in insect embryos: an acidic cathepsin B-like protease of Drosophila and a thiol protease or cathepsin L-like protease of Bombyx (8)(9)(10)(11). Similar to mosquito VCP, all these proteases are deposited as proenzymes in yolk bodies of eggs and activated in embryos.…”

mentioning

confidence: 99%

An extraovarian protein accumulated in mosquito oocytes is a carboxypeptidase activated in embryos.

Cho

Deitsch

Raikhel

1991

Proc. Natl. Acad. Sci. U.S.A.

102

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We report a phenomenon previously unknown for oviparous animals; in Aedes aegypti mosquitoes a serine carboxypeptidase is synthesized extraovarially and then internalized by oocytes. The cDNA encoding mosquito vitellogenic carboxypeptidase (VCP) was cloned and sequenced. The VCP cDNA hybridizes to a 1.5-kilobase mRNA present only in the fat body of vitellogenic females. The deduced amino acid sequence of VCP shares significant homology with members of the serine carboxypeptidase family. Binding assays using a serine protease inhibitor, [3H~diisopropyl fluorophosphate, showed that VCP is activated in eggs at the onset of embryonic development. Activation of VCP is associated with the reduction in its size from 53 kDa (inactive proenzyme) to 48 kDa (active enzyme). The active, 48-kDa, form ofVCP is maximally present at the middle of embryonic development and disappears by the end.

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The occurrence of a premature form of egg-specific protein in vitellogenic follicles ofBombyx mori

Cited by 36 publications

References 21 publications

Purification and characterization of a cysteine proteinase from silkworm eggs

Purification and characterization of a cysteine proteinase from silkworm eggs

Physiological and Biochemical Effect of Pyriproxyfen on Indian Meal Moth Plodia Interpunctella (Hübner) (Lepidoptera: Pyralidae)

An extraovarian protein accumulated in mosquito oocytes is a carboxypeptidase activated in embryos.

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