Isolation and Structure of Diapause Hormone of the Silkworm, Bombyx mori.

Imai, Kunio; Konno, Takamichi; Nakazawa, Yoshitaka; Komiya, Takashi; Isobe, Mitsuaki; Koga, Kazushi; Goto, Toshio; Yaginuma, Toshinobu; Sakakibara, Kiyoshi; Hasegawa, Kinsaku; Yamashita, Okitsugu

doi:10.2183/pjab.67.98

Cited by 213 publications

(91 citation statements)

References 5 publications

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“…PBAN-like peptides, found in other insects, have been shown to have other functions (27)(28)(29)(30)(31)(32) indicating the ubiquitous and pleiotropic nature of this peptide family. Therefore, it could also be conceptualized that PBAN in male moth species will have a different function.…”

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confidence: 99%

Gene-silencing reveals the functional significance of pheromone biosynthesis activating neuropeptide receptor (PBAN-R) in a male moth

Bober

Rafaeli

2010

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

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The role of pheromone biosynthesis activating neuropeptide (PBAN) in the regulation of pheromone biosynthesis of several female moth species is well elucidated, but its role in the males has been a mystery for over two decades since its discovery from both male and female central nervous systems. In previous studies we have identified the presence of the gene transcript for the PBAN-G-protein coupled receptor (PBAN-R) in Helicoverpa armigera male hair-pencil-aedaegus complexes (male complexes), a tissue structurally homologous to the female pheromone gland. Moreover, we showed that this transcript is up-regulated during pupal-adult development, analogous to its regulation in the female pheromone-glands, thereby indicating a likely functional gene. Here we argue in favor of PBAN's role in regulating the free fatty-acid components (myristic, palmitic, stearic, and oleic acids) and alcohol components (hexadecanol, cis-11 hexadecanol, and octadecanol) in male complexes. We demonstrate the diel periodicity in levels of male components, with peak titers occurring during the 7th-9th h in the scotophase, coincident with female pheromone production. In addition, we show significant stimulation of component levels by synthetic HezPBAN. Furthermore, we confirm PBAN's function in this tissue through knockdown of the PBAN-R gene using RNAi-mediated gene-silencing. Injections of PBAN-R dsRNA into the male hemocoel significantly inhibited levels of the various male components by 58%-74%. In conclusion, through gain and loss of function we revealed the functionality of the PBAN-R and the key components that are up-regulated by PBAN.aedaegus | hair-pencils | Helicoverpa armigera | male-produced components R eproductive behavior involves the integration of physiological and behavioral events that synchronize male and female encounters. Receptivity in female moths is broadcasted by the release of a blend of volatile sex-pheromones during specific times of the photoperiod when they assume typical calling behaviors.

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confidence: 99%

Gene-silencing reveals the functional significance of pheromone biosynthesis activating neuropeptide receptor (PBAN-R) in a male moth

Bober

Rafaeli

2010

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

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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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“…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.

213

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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“…Peptidergic neurons in the subeosophageal ganglion of the silkworm, Bombyx mori, produce diapause hormone (DH), the initiator of embryonic diapause (Sato et al, 1993). Diapause hormone consists of 24 amino acid residues amidated at the carboxyl terminal, with a molecular weight of 2645 daltons, (Imai et al, 1991), encoded in a polyprotein precursor mRNA that also encodes four other hormones (Sato et al, 1993). This hormone acts on the ovaries, initiating gene transcription that ultimately results in the accumulation of glycerol and sorbitol, characteristics only of eggs in embryonic diapause (reviewed in Yamashita, 1995).…”

Section: Regulation Of Diapause Inductionmentioning

confidence: 99%

Genomic and Hormonal Components of Altered Developmental Pathways in the Annual Killifish, Austrofundulus limnaeus

Pri-Tal¹

2000

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The annual killifish, Austrofundulus limnaeus, may enter embryonic diapause at three distinct points of development, termed diapause I, II, and III. Previous studies suggest a role for steroid hormones in the regulation of diapause in annual killifish.This study concerns the hormonal and genomic components involved in the developmental decision to enter or escape diapause II from both a maternal and embryonic perspective. Steroid hormone levels were measured in tissues isolated from adult female fish that were producing either high or low proportions of escape embryos. Levels of steroid hormones were also measured in new fertilized embryos that were known to be on either an escape or diapausing developmental trajectory. In

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Isolation and Structure of Diapause Hormone of the Silkworm, Bombyx mori.

Abstract: Abstract:The

Cited by 213 publications

References 5 publications

Gene-silencing reveals the functional significance of pheromone biosynthesis activating neuropeptide receptor (PBAN-R) in a male moth

Gene-silencing reveals the functional significance of pheromone biosynthesis activating neuropeptide receptor (PBAN-R) in a male moth

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.

Genomic and Hormonal Components of Altered Developmental Pathways in the Annual Killifish, Austrofundulus limnaeus

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