Developmental and sex-dependent regulation of storage protein synthesis in the silkworm, Bombyx mori

Mine, Eriko; Izumi, Susumu; Katsuki, Motoya; Tomino, Shiro

doi:10.1016/0012-1606(83)90090-8

Cited by 72 publications

(46 citation statements)

References 27 publications

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“…The present observations in A. albistriga agree with the fact that SP1 protein synthesis closely correlates with SP1 transcription in the silkworm, B. mori (Izumi et al, 1981;Mine et al, 1983, Vanishree et al, 1999, 2005; wax moth, G. mellonella (Ray et al, 1987, Rajaratnam, 1996; tobacco hornworm, M. sexta (Webb and Riddiford 1988); tobacco cutworm, Heliothis virescens (Miller et al, 1990); autogenous mosquito, Aedes atropalpus (Zakharkin et al, 2001); fall webworm, Hyphantria cunea (Cheon et al, 2001); Indian meal moth, Plodia interpunctella (Zhu et al, 2002); diamondback moth, Plutella xylostella (Ashfaq, et al, 2005(Ashfaq, et al, , 2007; and honey bee, Apis mellifera (Cunha et al, 2005). The subepidermal (peripheral) part of the fat body is the site of the most active protein synthesis and there is no part in sequestration of protein granules as they are programmed to undergo cell death during larvalpupal transformation (Keeley, 1985;Haunderland et al, 1990;Wang and Haunerland, 1992;Muller et al, 2004).…”

Section: Archives Of Insect Biochemistry and Physiology October 2008supporting

confidence: 93%

“…In some species, such as M. sexta and H. cecropia, two or more isoforms of methionine-rich proteins have been found (Tojo et al, 1978; Wang and Hanuerland, 1992), which play a vital role in egg formation in female insects. In several lepidopteran species, the expression pattern of the SP parallels the protein titer in the hemolymph (Ray et al, 1987;Mine et al, 1983; Webb and Reiddiford, 1988). Because of their physiological significance and patterns of developmental control, insect SPs have become an attractive model for the study of gene regulation.…”

mentioning

confidence: 96%

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Expression and localization of storage protein 1 (SP1) in differentiated fat body tissues of red hairy caterpillar,Amsacta albistrigaWalker

Chandrasekar

Jae

Krishnan

2008

Arch Insect Biochem Physiol

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The accumulation and utilization of storage proteins are prominent events linked to the metamorphosis of holometabolous insects. The female-specific storage protein 1 (SP1) is the major storage protein found in the hemolymph and fat body of female larvae of the groundnut pest, Amsacta albistriga. Here we show SP1 expression and localization in differentiated fat body tissues using biochemical and immunohistochemistry scrutiny. Comparison of A. albistriga SP1 with that of other species with respect to amino acid composition and N-terminal sequences show that SP1 is a methonine-rich protein and its identity was confirmed by means of immunoblot analysis. Northern blot studies revealed that the SP1 gene demonstrates stage- and tissue-specific expression in the peripheral fat body cells during the mid-larval period of fifth instar of A. albistriga. During the larval pupal transformation, SP1 are sequestered mainly by the perivisceral fat body tissues, until they serve the purpose of supplying amino acids for the production of egg yolk proteins. Further, electron microscopic studies using immunogold tracer techniques confirmed the localization of crystalline SP1 reserves, stored in the perivisceral fat body tissues. Hence, the peripheral fat body is responsible for biosynthesis of storage proteins, whereas the perivisceral fat body is a specialized storage organ.

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Section: Archives Of Insect Biochemistry and Physiology October 2008supporting

confidence: 93%

mentioning

confidence: 96%

Expression and localization of storage protein 1 (SP1) in differentiated fat body tissues of red hairy caterpillar,Amsacta albistrigaWalker

Chandrasekar

Jae

Krishnan

2008

Arch Insect Biochem Physiol

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“…ScSP2 is a member of the aromatic amino acid-rich arylphorins, which contain large amounts of phenylalanine and tyrosine to support cuticle deposition (Webb and Riddiford, 1988). The properties of ScSP1 and ScSP2 are quite similar to those of their orthologs in B. mori (Tojo et al, 1980;Mine et al, 1983;Shimada et al, 1987). If repressed expression of ScSPs by an E. coli challenge results in a decrease in storage protein endocytosis by fat body cells before pupation, there will be some physiological and/or biochemical effects on the subsequent development of pupae and adults.…”

Section: Discussionmentioning

confidence: 92%

Prominent down‐regulation of storage protein genes after bacterial challenge in eri‐silkworm, Samia cynthia ricini

Meng

Omuro

Funaguma

et al. 2007

Arch Insect Biochem Physiol

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We constructed two independent cDNA libraries from the fat body of Escherichia coli- or Candida albicans-challenged eri-silkworm Samia cynthia ricini larvae. We performed comparative expressed sequence tag (EST) analysis of the two cDNA libraries and found that two putative storage protein genes, ScSP1 and ScSP2, were markedly repressed by E. coli injection as compared with C. albicans injection. By quantitative real-time RT-PCR analysis, we showed that ScSP1 mRNA significantly reduced to 1/32-1/3 in the fat body of the female larvae, and ScSP2 mRNA reduced to 1/7-1/3 and 1/22-1/5 in the females and males, respectively, 12-36 h after E. coli injection as compared with PBS injection. In addition, SDS-PAGE analysis revealed that the accumulation of both the ScSP proteins in the larval hemolymph apparently decreased up to 36 h after E. coli injection. However, the amounts of the two ScSP proteins returned to the same level as those in the larvae injected with PBS by 48 h after injection, showing that the reduction in ScSPs caused by the bacterial challenge was transient. Moreover, potential binding sites for the Drosophila Rel/NF-kappaB protein Dorsal were found in the 5' upstream regulatory regions of ScSP1 and ScSP2, suggesting the participation of the Rel/NF-kappaB proteins in controlling the bacterial suppression of the ScSP genes. These results suggested the hypothesis that S. c. ricini has a genetic program to shut down temporarily dispensable gene expression in order to induce an acute and efficient expression of immune-related genes. These findings may provide new insight into the innate immune system in lepidopteran insects.

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“…Numerous authors have reported the inhibitory effect of JH and JHA on the occurrence of specific hemolymph proteins, such as storage proteins (Tojo et al, 1981;Mine et al, 1983), and a group of ''30 K proteins'' named major hemolymph proteins (MHP) (Izumi et al, 1984;Bosquet and Fourche, 1987;Plantevin et al, 1987;Bosquet et al, 1989a,b). MHP and storage proteins constitute the two major protein components in the hemolymph of fifth instar silkworms (Tomino, 1985).…”

Section: Effect Of Fenoxycarb On Other Jh-regulated Parametersmentioning

confidence: 97%

Effects of ultralow doses of fenoxycarb on juvenile hormone-regulated physiological parameters in the silkworm,Bombyx mori L.

Monconduit¹,

Mauchamp²

1998

Arch. Insect Biochem. Physiol.

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Developmental and sex-dependent regulation of storage protein synthesis in the silkworm, Bombyx mori

Cited by 72 publications

References 27 publications

Expression and localization of storage protein 1 (SP1) in differentiated fat body tissues of red hairy caterpillar,Amsacta albistrigaWalker

Expression and localization of storage protein 1 (SP1) in differentiated fat body tissues of red hairy caterpillar,Amsacta albistrigaWalker

Prominent down‐regulation of storage protein genes after bacterial challenge in eri‐silkworm, Samia cynthia ricini

Effects of ultralow doses of fenoxycarb on juvenile hormone-regulated physiological parameters in the silkworm,Bombyx mori L.

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