A New Diapause Hormone Molecule of the Silkworm, Bombyx mori.

Sato, Yukihiro; Nakazawa, Yoshitaka; Menjo, Nobuo; Imai, Kunio; Komiya, Takashi; Saito, Hiroyuki; Shin, Masaru; Ikeda, Motoko; Sakakibara, Kiyoshi; Isobe, Mitsuaki; Yamashita, Okitsugu

doi:10.2183/pjab.68.75

Cited by 30 publications

(19 citation statements)

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“…The suboesophageal ganglion (SG) was first identified in the silkworm Bombyx mori as a neuroendocrine organ that secretes diapause hormone (DH), which is responsible for induction of embryonic diapause (4)(5)(6). Recently, B. mori DH (Bom-DH) has been isolated and shown to be a 24-aa peptide amide (7,8). Another function of the silkworm SG is to secrete the pheromone biosynthesisactivating neuropeptide (PBAN), which stimulates the biosynthesis of a sex pheromone, bombykol, in pheromone glands of female moths (9)(10)(11).…”

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“…However, it remains unknown whether these neuropeptides are products of a common precursor polyprotein that is encoded by a single gene. We have recently cloned cDNA encoding DH by using oligonucleotide probes, which facilitates the analysis ofthe mode of neuropeptide biosynthesis in SG of B. mori (8).…”

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“…A cDNA library of SG-first thoracic ganglion complexes of the Asagiri race was constructed into Agt1O (23). A degenerate 35-mer [ACIGAIAT-GAAIGAIGAI(T/A)(C/G)IGAI(C/A)GIGGIGCICA] and a nondegenerate 72-mer oligonucleotide (ACCGACATGAAG-GATGAGTCTGACCGTGGAGCCCACTCTGAGCGTG-GTGCTCTGTGCTTCGGCCCCCGCCTG), which were deduced from the DH structure were synthesized (8), radiolabeled with [y32P]ATP by using T4 polynucleotide kinase, and then used for screening by hybridization.…”

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“…Peptides were synthesized as amidated forms by using an ABI 431A peptide synthesizer (Applied Biosystems) according to a fluoren-9-ylmethoxycarbonyl protocol and by a handmade peptide synthesizer employing butoxycarbonyl chemistry (7,8). Synthetic Bom-PBAN-I (10) was kindly provided by A. Suzuki (University ofTokyo).…”

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Precursor polyprotein for multiple neuropeptides secreted from the suboesophageal ganglion of the silkworm Bombyx mori: characterization of the cDNA encoding the diapause hormone precursor and identification of additional peptides.

Sato

Oguchi

Menjo

et al. 1993

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

214

114

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Peptidergic neurons, which serve as source of various endocrine neuropeptides, were identified in the suboesophageal ganglion (SG) and brain of insects. In the silkworm Bombyx mori, SG is known to secrete two neuropeptides, diapause hormone (DH) responsible for induction ofembryonic diapause and pheromone biosynthesis-activating neuropeptide, which share a pentapeptide amide, Phe-Xaa-Pro-Arg-Leu-NH2 (Xaa = Gly or Ser), at the C terminus. We have isolated cDNA clones for DH from the cDNA library of SG by using oligonucleotide probes. The molecular characterization of the cDNA reveals that the mRNA encodes an open reading frame consisting of 192 aa residues in which the 24-aa DH peptide is localized at the N-terminal region just after the signal peptide. A homology search proposed that the cDNA encodes pheromone biosynthesis-activating neuropeptide and three other neuropeptides [a-, (3-, and y-SG neuropeptide (SGNP)] in the region following DH, all of which are flanked by possible tryptic cleavage sites and share the Phe-Xaa-Pro-Arg-Leu-Gly sequence at the C terminus. Northern hybridization analysis clearly showed that the gene expression was limited to SG. We chemically synthesized a-, p-, and y-SGNP and used them to identify components in extracts of SG and to examine biological functions. a-and y-SGNP were identified in extracts of SG, and the synthetic P-and y-SGNP expressed weak DH activity.These results indicate that DH, along with four other neuropeptides, is generated from a common precursor polyprotein that is encoded by a single mRNA transcribed in neurosecretory cells of SG.

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Precursor polyprotein for multiple neuropeptides secreted from the suboesophageal ganglion of the silkworm Bombyx mori: characterization of the cDNA encoding the diapause hormone precursor and identification of additional peptides.

Sato

Oguchi

Menjo

et al. 1993

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

214

114

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“…The two PBAN genes identified to date encode not only the PBAN peptide but also four additional neuropeptides having the common C-terminal pentapeptide motif (FXPRL-amide) that is needed for pheromonotropic activity and is common with insect pyrokinin and myotropin peptide families. It is not clear if all five peptides are involved in the control of pheromone production, but one of them has been identified as the egg diapause hormone in Bombyx mori (32).…”

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Chemistry of sex attraction.

Roelofs

1995

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

149

102

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The (Fig. 1). The phenomenon of virgin female moths attracting large numbers of male moths was noted long before it was understood that a trail of chemicals could be so effective over great distances. In 1882 J. A. Lintner, the first state entomologist in New York, described (1) a spectacle of 50 large male Promethea moths being attracted to a female moth placed in his office window, which in turn attracted a large crowd of people on the sidewalk. He not only acknowledged the role of chemicals in this process and the existence of "smell organs"The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.but also foresaw the potential use of these chemicals for insect control. He writes (1):It is the existence of these organs that many of the Families of Lepidoptera, especially among the moths, owe the continuance of the species. They operate in the association of the sexes, with such an irrestible and far-reaching force as to exceed our conception and to be marvelous to our eyes. ... Can not chemistry come to the aid of the economic entomologist in furnishing at moderate cost, the odorous substances needed? Is the imitation of some of the more powerful animal secretions impracticable?This statement sums up much of the research that has been conducted on the chemistry of sex attraction in insects over the past few decades. Research efforts have focused on the overt chemical signals used in the mating process, with the driving force and financial backing for much of the research due to the potential for use of synthetic pheromone chemicals in pest control programs. This effort has resulted in the identification of sex attractants for >1600 insect species from >90 families in nine orders, with an emphasis on Lepidoptera (2). The variety and complexity of chemical structures (>300 reported structures) observed among the various insect orders attest to the insect's amazing ability to sequester and synthesize unique structures and blends, mainly composed of acetogenins and mevalogenins. These essential signaling chemicals of the "sex attractant" communication system are interesting but represent only the more obvious chemicals involved in complex systems of synchronous emitters and receivers. Rather than review all data on this enormous topic, this paper will discuss some of the chemistry involved in various aspects of the sex pheromone communication system in insects.OVERT CHEMICAL SIGNALS The sex pheromone communication system basically involves the release of specific chemicals from a pheromone producer (emitter), the transmission of these chemicals in the environment to a receiver, and the processing of these signals to mediate appropriate behavioral responses in the receiver. The chemicals transmitted downwind have been the most obvious targets for characterization. The code was first broken with the publication in 1959 (3) of the sex pheromone for the domest...

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Comparative aspects of peptidergic signaling pathways in the nervous systems of arthropods

Agricola

Bräunig

1995

Experientia Supplementum

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A New Diapause Hormone Molecule of the Silkworm, Bombyx mori.

Cited by 30 publications

References 7 publications

Precursor polyprotein for multiple neuropeptides secreted from the suboesophageal ganglion of the silkworm Bombyx mori: characterization of the cDNA encoding the diapause hormone precursor and identification of additional peptides.

Precursor polyprotein for multiple neuropeptides secreted from the suboesophageal ganglion of the silkworm Bombyx mori: characterization of the cDNA encoding the diapause hormone precursor and identification of additional peptides.

Chemistry of sex attraction.

Comparative aspects of peptidergic signaling pathways in the nervous systems of arthropods

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