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B. Mori (b + mori)
Selected AbstractsProgrammed cell death of the ovarian nurse cells during oogenesis of the silkmoth Bombyx moriDEVELOPMENT GROWTH & DIFFERENTIATION, Issue 7 2006Vicky E. Mpakou In the present study, we describe the features of programmed cell death of the ovarian nurse cells occurring during vitellogenesis of the silkmoth Bombyx mori. At developmental stage 5, the nurse cells occupy one-half of the follicular volume and obtain a rather spherical shape, while the nurse cell nuclei appear large and elongated, forming impressive projections. At the following stage, stage 6, the nurse cells decrease in size and their shape becomes elliptic. The nuclei remain elongated, being also characterized by large lobes. The lobes of the ramified nurse cell nuclei seem to retain the nucleus in the center of the cell during the dumping of the nurse cell cytoplasm into the growing oocyte. At stage 7, membrane enclosed vacuoles can be easily detected into the nurse cells cytoplasm. Ultrastructural analysis and fluorescent microscopy using mono-dansyl-cadaverine staining of these vacuoles also reveal that they represent autolysosomes. Caspase activity is detected during stage 7, as it is demonstrated by using the Red-VAD-FMK staining reagent. At developmental stages 8 and 9, the nurse cells exhibit chromatin condensation, DNA fragmentation and caspase activity. Finally, during the following stage 10, the nuclear remnants are assembled into apoptotic vesicles, which, after being phagocytosed, are observed in the cytoplasm of adjacent follicle cells. We propose that apoptosis and autophagy operate synergistically during vitellogenesis of B. mori, in order to achieve an efficient and rapid clearance of the degenerated nurse cell cluster. [source] An ecdysteroid-inducible insulin-like growth factor-like peptide regulates adult development of the silkmoth Bombyx moriFEBS JOURNAL, Issue 5 2009Naoki Okamoto Insulin-like growth factors (IGFs) play essential roles in fetal and postnatal growth and development of mammals. They are secreted by a wide variety of tissues, with the liver being the major source of circulating IGFs, and regulate cell growth, differentiation and survival. IGFs share some biological activities with insulin but are secreted in distinct physiological and developmental contexts, having specific functions. Although recent analyses of invertebrate genomes have revealed the presence of multiple insulin family peptide genes in each genome, little is known about functional diversification of the gene products. Here we show that a novel insulin family peptide of the silkmoth Bombyx mori, which was purified and sequenced from the hemolymph, is more like IGFs than like insulin, in contrast to bombyxins, which are previously identified insulin-like peptides in B. mori. Expression analysis reveals that this IGF-like peptide is predominantly produced by the fat body, a functional equivalent of the vertebrate liver and adipocytes, and is massively released during pupa,adult development. Studies using in vitro tissue culture systems show that secretion of the peptide is stimulated by ecdysteroid and that the secreted peptide promotes the growth of adult-specific tissues. These observations suggest that this peptide is a Bombyx counterpart of vertebrate IGFs and that functionally IGF-like peptides may be more ubiquitous in the animal kingdom than previously thought. Our results also suggest that the known effects of ecdysteroid on insect adult development may be in part mediated by IGF-like peptides. [source] Linkage and mapping analysis of a non-susceptibility gene to densovirus (nsd-2) in the silkworm, Bombyx moriINSECT MOLECULAR BIOLOGY, Issue 2 2003D. O. Ogoyi Abstract Nonsusceptibility to Bombyx mori densovirus type 2 (BmDNV-2) is controlled by a recessive non-susceptibility gene, nsd-2 (non-susceptibility to DNV-2) in B. mori. Taking advantage of a lack of crossing over in females, reciprocal backcrossed F1 (BF1) progeny were used for linkage analysis and mapping of nsd-2 using silkworm strains C124 and 902, which are classified as being highly susceptible and non-susceptible to DNV-2, respectively. BF1 larvae were inoculated twice with DNV-2 virus at the first and second instar stages. DNA was extracted from each of the surviving fifth instar larvae and analysed by RFLP inheritance patterns using probes specific to each of the 28 linkage groups of B. mori. Our results indicated that the non-susceptibility gene was linked to linkage group 17, since all surviving larvae showed the homozygous profile of strain 902 in their genotype. The other linkage groups showed mixtures of heterozygous and homozygous genotypes, indicating an independent assortment. A linkage map of 30.6 cM was constructed for linkage group 17 with nsd-2 mapped at 24.5 cM and three closely linked cDNA markers were identified. [source] In vivo production of recombinant protein by a baculovirus vector inoculated perorally to the prefinal instar larvae of Bombyx mori L. (Lep., Bombycidae) aided by an optical brightener, Tinopal UNPA-GXJOURNAL OF APPLIED ENTOMOLOGY, Issue 9 2002T. Arakawa Host larvae were fed a diet containing 0.3% (w/w) Tinopal on day 1 in the 4th instar and then fed a diet contaminated by budded particles of NPV (1.0 × 106 TCID50 U/larva) that was pathogenic to B. mori (BmNPV) on day 2 (inoculation schedule 1). Another set of host larvae was fed a diet containing BmNPV budded particles (2.5 × 106 TCID50 U/larva) together with 0.3% (w/w) Tinopal on day 1 in the 4th instar (inoculation schedule 2). Host larvae treated by both schedules died of viral infection. The operation of schedule 2 is simpler than that of schedule 1, although the former required higher doses of the virus for satisfactory infection. We inoculated a baculovirus vector carrying human serum albumin (HSA) gene into 4th instar B. mori larvae by schedule 1. Recombinant HSA was detected in the homogenate of host larvae 4 days after inoculation. The peroral inoculation of BmNPV budded particles aided by Tinopal may thus lead to industrial pharmaceutical production using a baculovirus vector for large numbers of insect hosts. [source] The expression patterns of a eukaryotic initiation factor 3 subunit H in the silk glands in Bombyx moriARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY (ELECTRONIC), Issue 1 2010Jia-Lin Wang Abstract Eukaryotic initiation factor 3 subunit H has been characterized in many organisms, and it has been found to play many roles including help regulate translation initiation. In this work, we studied the tissue distribution and expression profiles of Bombyx mori (B. mori) eIF3 subunit H (BmeIF3h). BmeIF3h was prominently expressed in silk glands, with anterior silk glands (ASGs), middle silk glands (MSGs), and posterior silk glands (PSGs) all expressing BmeIF3h. The expression levels of BmeIF3h in MSGs and PSGs were higher than that in ASGs during 0 d and 2 d of the 5th instar larvae. The expression levels of BmeIF3h in MSGs and PSGs were up-regulated once the silk glands began to synthesize silk protein during the feeding stage of the 4th instar larvae. Immunohistochemistry showed that BmeIF3h was distributed in the cytoplasm of MSGs cells and in both the nucleus and the cytoplasm of PSGs cells. These data suggest that BmeIF3h had different action behaviors in the MSGs and PSGs related to the production of the silk glue proteins and silk fibre proteins, respectively. © 2010 Wiley Periodicals, Inc. [source] Expression profiling of novel bacteria-induced genes from the silkworm, Bombyx moriARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY (ELECTRONIC), Issue 3 2010Hiromitsu Tanaka Abstract In this study, we have newly identified three bacteria-induced genes from the silkworm Bombyx mori by quantitative reverse transcriptase-polymerase chain reaction. One of these, eukaryotic initiation factor 4E-1 (eIF4E-1), is assumed to encode an eIF4E family, which plays a role in the initiation of translation as a mRNA cap-binding protein. The second gene is BmFOXG1, belonging to a family of forkhead transcription factors, FOXG1. The third gene is MBF2-related (MBF2-R) whose product has high homology to a co-activator protein MBF2 from B. mori. Although BmFOXG1 was up-regulated in the fat body in response to three kinds of bacteria, Escherichia coli, Staphylococcus aureus, and Bacillus subtilis, eIF4E-1 and MBF2-R were up-regulated by E. coli and B. subtilis, but not S. aureus, suggesting that bacteria possessing meso-diaminopimelic acid-containing peptidoglycan but not lysine-containing peptidoglycan activate eIF4E-1 and MBF2-R, probably through a conserved immune deficiency pathway. We further profiled the expression of three genes in different tissues and a silkworm cell line, NIAS-Bm-aff3, in response to bacteria, and at different times after bacterial challenge in the fat body. © 2010 Wiley Periodicals, Inc. [source] Biochemical characterization of rab proteins from Bombyx mori,ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY (ELECTRONIC), Issue 2 2009Tomohide Uno Abstract The small GTPases known as Rab proteins are key regulators of membrane trafficking. We used RT-PCR to isolate cDNA clones of insect-specific Rab proteins (BRabN1 and BRabN2) showing low homology with known Rab proteins from other animals, from mRNA of Bombyx mori. These 2 Rabs were produced in Escherichia coli and purified. BRabN1 bound [3H]-GDP and [35S]-GTP,S with dissociation constants of 0.087 × 10,6,M and 1.02 × 10,6,M, respectively, whereas those of BRabN2 were 0.546 × 10,6,M and 1.02 × 10,6,M, respectively. Binding of [35S]-GTP,S to BRabN1 and N2 was inhibited by GDP and GTP. The GTP-hydrolysis activities of BRabN1 and N2 were 154 and 35.5,mmol/min/mole, respectively, and bound [35S]-GTP,S was exchanged efficiently with GTP. BRabN1 also showed ATPase activity and exchange of [35S]-GTP,S with ATP. Monoclonal antibodies against BRabN1 and N2 did not recognize any other Rab proteins, and Western blotting using the anti-BRabN1 antibody revealed a single band in the testis of B. mori. These results suggest that BRabN1 and N2 of B. mori bind GTP, convert from the GTP-bound state to the GDP-bound state by intrinsic GTP hydrolysis activity, and return to the GTP-bound state with the exchange, and that BRabN1 is specifically expressed in testis. Arch. Insect Biochem. Physiol. 2008. © 2008 Wiley-Liss, Inc. [source] Different Ca2+ signalling cascades manifested by mastoparan in the prothoracic glands of the tobacco hornworm, Manduca sexta, and the silkworm, Bombyx moriARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY (ELECTRONIC), Issue 2 2007Skarlatos G. Dedos Abstract Application of the tetradecapeptide mastoparan to the prothoracic glands (PGs) of the tobacco hornworm, Manduca sexta, and the silkworm, Bombyx mori, resulted in increases in intracellular Ca2+ ([Ca2+]i). In M. sexta, Gi proteins are involved in the mastoparan-stimulated increase in [Ca2+]i. However, there is no involvement of Gi proteins in the mastoparan-stimulated increase in [Ca2+]i in prothoracic gland cells from B. mori. Unlike in M. sexta prothoracic glands, in B. mori prothoracic glands mastoparan increases [Ca2+]i even in the absence of extracellular Ca2+. Pharmacological manipulation of the Ca2+ signalling cascades in the prothoracic glands of both insect species suggests that in M. sexta prothoracic glands, mastoparan's first site of action is influx of Ca2+ through plasma membrane Ca2+ channels while in B. mori prothoracic glands, mastoparan's first site of action is mobilization of Ca2+ from intracellular stores. In M. sexta, the combined results indicate the presence of mastoparan-sensitive plasma membrane Ca2+ channels, distinct from those activated by prothoracicotropic hormone or the IP3 signalling cascade, that coordinate spatial increases in [Ca2+]i in prothoracic gland cells. We propose that in B. mori, mastoparan stimulates Ca2+ mobilization from ryanodine-sensitive intracellular Ca2+ stores in prothoracic gland cells. Arch. Insect Biochem. Physiol. 65:52,64, 2007. © 2007 Wiley-Liss, Inc. [source] | |||||||||||||