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Archives of Insect Biochemistry and Physiology

Subscription journal
ISSN (Print) 0739-4462 - ISSN (Online) 1520-6327
Published by John Wiley and Sons

[1587 journals]

Editorial Board
AMINO ACID DEPRIVATION‐INDUCED EXPRESSION OF ASPARAGINE SYNTHETASE REGULATES THE GROWTH AND SURVIVAL OF CULTURED SILKWORM CELLS
- Abstract: Expression of Bombyx mori Asparagine synthetase (BmASNS), one gene that encodes an enzyme catalyzing asparagine biosynthesis, is transcriptionally induced following amino acid deprivation. Previous transcriptional analysis of the BmASNS gene showed the involvement of Polycomb proteins, epigenetic repressors, in suppressing BmASNS expression in a cell cycle‐dependent manner. However, the role of BmAsns protein in these cellular processes remains unclear. The present study thus exploited the potential function of BmAsns protein in cultured silkworm cells. Our results showed that ectopic overexpression of BmASNS gene effectively inhibited cell growth in silkworm cells, whereas its overexpression could rescue cell growth upon amino acid deprivation treatment. We found that the cells expressing BmAsns protein were capable of influencing the formation of autophagic vacuoles stimulated by amino acid deprivation. We speculated that the recovery of cell growth by overexpressed BmAsns protein is due to the rapid turnover of autophagic vacuoles in the cells. To further assess the effects of BmAsns on cell development, we used RNA interference to silence BmASNS expression in silkworm cells in the presence or absence of amino acids. Our results revealed a significant change of cell proliferation as well as cell cycle distribution after knockdown of BmASNS. Importantly, silkworm cells lacking BmASNS under the condition of amino acid deprivation showed severely impaired proliferation. Altogether, we concluded that the up‐regulated expression of BmASNS would be able to protect cells from impairment induced by amino acid deprivation, which in turn facilitates cell growth and survival.
FOUR SERINE PROTEASE cDNAS FROM THE MIDGUT OF Plutella xylostella AND THEIR PROTEINASE ACTIVITY ARE INFLUENCED BY THE ENDOPARASITOID, Cotesia vestalis
- Abstract: Serine proteinases, which include trypsins and chymotrypsins, play numerous roles in lepidopteran larvae, such as digestion, zymogen activation, and immune defense. Studies of lepidopteran serine proteinases could increase understanding of their feeding preference (polyphagous and monophagous) and facilitate identification of protease inhibitors, which can be engineered for pest management. In this paper, four full‐length cDNAs encoding one chymotrypsin and three trypsins were cloned from larval midguts of the diamondback moth, Plutella xylostella. Real‐time quantitative polymerase chain reaction (PCR) analysis showed all four serine protease genes were downregulated after P. xylostella was parasitized by the parasitoid wasp Cotesia vestalis. Trypsin and chymotrypsin enzymatic activities within the midgut of nonparasitized and C. vestalis‐parasitized P. xylostella larvae were examined using N‐a‐benzoyl‐arg p‐nitroanilide and N‐succinyl‐ala‐ala‐pro‐phe p‐nitroanilide as substrates. Trypsin and chymotrypsin activities were decreased in parasitized larvae as compared to untreated larvae, with the effect being more pronounced over time. Chymotrypsin activity in particular exhibited a significant decrease in activity. The correlation of decreased enzymatic activity and transcript abundance suggests parasitization induced downregulation of serine proteinase gene transcripts.
VENOM COMPONENTS OF Asobara japonica IMPAIR CELLULAR IMMUNE RESPONSES OF HOST Drosophila melanogaster
- Abstract: The endoparasitoid wasp Asobara japonica has highly poisonous venom: the host Drosophila larvae are killed by envenomation at a dose that is naturally injected by the female wasp at parasitism. This insecticidal venom is neutralized, however, because A. japonica introduces lateral oviduct components soon after venom injection at oviposition. Although the venom and lateral oviduct components of this parasitoid have been partially characterized, how the venom components favor successful development of wasp eggs and larvae in the host remains ambiguous. Here, we demonstrated that A. japonica venom did not affect host humoral immune responses, determined as expression of antimicrobial peptide (AMP) genes, but significantly diminished two cellular responses, spreading and phagocytosis, by host hemocytes. Moreover, venom components drastically elevated a serine protease‐like activity 4 h after its injection. The lateral oviduct components did not negate the detrimental effects of the venom on host cellular immunities, but significantly reduced the venom‐induced elevation of protease activity. Both active factors in venom and lateral oviduct components were roughly characterized as heat‐labile substances with a molecular mass of at least 10 kDa. Finally, venom of A. japonica, with a wide host range, was found to be much more toxic than that of Asobara rossica, which has a limited host range. These results reveal that A. japonica venom toxicity allows exploitation of a broader range of host insects because it is essential to overcome cellular immune responses of the host for successful parasitism.
REGULATION OF AMYLASE, CELLULASE AND CHITINASE SECRETION IN THE DIGESTIVE TRACT OF THE TWO-SPOTTED FIELD CRICKET, Gryllus bimaculatus
- Abstract: The secretion of amylase and cellulase in Gryllus bimaculatus is determined by increased food intake, whereby shortly after molting food consumption increases. About half of the standing amylase concentration (activity) in the endothelial cells can be secreted within 30 min. The peak of amylase and cellulase secretion that occurs in the photophase is related to the feeding peak in the previous scotophase. The secretion of chitinase on the other hand is primarily controlled by the molting cycle. Only amylase secretion was affected by calcium in the incubation medium, suggesting an apocrine release mechanism. Refeeding experiments (after 5 days without food) suggest that the release of amylase in response to a nutrient in the lumen (glucose) is not due to simple stimulation of exocytosis, but rather a stimulation of synthesis.

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