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1995 Fiscal Year Final Research Report Summary

Bio-organic Chemistry on Egg Diapause of Silkworm

Research Project

Project/Area Number 05453164
Research Category

Grant-in-Aid for General Scientific Research (B)

Allocation TypeSingle-year Grants
Research Field Bioproduction chemistry/Bioorganic chemistry
Research InstitutionMie University

Principal Investigator

IMAI Kunio  Mie Univ.Fac.Bioresources Associate Professor, 生物資源学部, 助教授 (80109313)

Co-Investigator(Kenkyū-buntansha) YAMASHITA Okitsugu  Nagoya Univ.Fac.Agriculture Professor, 農学部, 教授 (50023411)
Project Period (FY) 1994 – 1995
KeywordsDiapause hormone / Silkworm / Diapause hormone derivatives / Egg diapause / Lipophilic peptides / SGNP / Chemical synthesis
Research Abstract

SEARCH FOR NATURAL SGNPS AND NEW DIAPAUSE INDUCING SUBSTANCES
Natural alpha-, beta- and gamma-SGNP were searched for in the extract of the suboesophageal ganglions of silkworm. alpha- and gamma-SGNP were isolated and identified, and beta-SGNP was speculated to exist.
To investigate the new diapause inducing substances, the heads of male silk moths were collected. They were extrated with water and several organic solvents. Most of the extracts showed the diapause inducing activity, and the result suggested that the organ contains many kinds of active substances. They were purified by repeated chromatography and one of the active substances (VAP peptide) was isolated. It had unique structure, physicochemical feature and biological activity.
PEPTIDE SYNTHESIS AND BIOLOGICAL ACTIVITY OF SYNTHETIC PEPTIDES
Diapause hormone (DH) , SGNPs and a fragment analog of VAP peptide were chemically synthesized and the synthetic peptides were used for preparation of antibodies and for the preparation of derivatives.
A procedure to derivatize the N terminus of DH was developed, as the biological activity was reduced when free DH molecule was simply treated with the derivatizing reagents. Acylated derivatives, fluorescent and pigmented derivative and photoaffinity labeled derivative were successfully prepared.
The C terminal pentapeptides and their analogs were synthesized and their biological activities were compared to each other. The result suggested 1) amide structure at C terminus is important, 2) the tripeptide amide is the smallest unit for biological function, 3)modification of the unit enhances the biological acitivity.
The results of the present research indicated the possiblility to clarify the mechanism for diapause induction and to design and to create the artificial diapause inducing substances.

  • Research Products

    (12 results)

All Other

All Publications (12 results)

  • [Publications] Y.Sato,K.Imai,H.Saito,M.Ikeda,O.Yamashita,et al.: "Precursor Polyprotein for Multiple Neuropeptides Secreted from Suboesop hageal Ganglion of the Silkworm,Bombyx mori : Characterization of cDNA for Diapause Hormone Precursor and Identification of New Peptides." Proc.Natl.Acad.Sci.USA,. 90. 3251-3255 (1993)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] M.Ideda,H.Saito,K.Imai,Y.Sato,O.Yamashita,et al.: "Induction of Embryonic Diapause and Stimulation of Ovary Trehalase Activity in the Silkworm,Bombyx mori,by Synthetic Diapause Hormone." J.Insect.Physiol.39. 889-895 (1993)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] H.Saito,R.Takeda,Y.Hayashi,K.Imai,O.Yamashita,et al.: "The Core and Complimentary Sequence Responsible for Biological Activity of the Diapause Hormone of the Silkworm,Bombyx mori." Peptide. 15. 1173-1178 (1994)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] M.Ikeda,Y.Sato,H.Saito,K.Imai,O.Yamashita et al.: "Molecular Characterization of Ovary Trehalase of the Silkworm,Bombyx mori and lts Transcriptional Activation by Diapause Hormone" Biochim.Biophys.Acta. 1281. 366-374 (1994)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] K.Shiomi,M.Ikeda,Y,Sato,K.Imai,O.Yamashita,et al.: "Induction of Non-diapause Eggs by Anti-diapause Hormone Rabbit Serum Injected into the Diapause Type of the Silkworm,Bombyx mori." J.Insect Physiol.39. 693-699 (1994)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] K.Imai,K.Sugiura,T.Komiya,O.Yamashita: "Isolation and Partial Structure of a Unique Lipophilic Peptide,VAP peptide,from Heads of Male Silkworm Moths" Biosci.Biotech.Biochem.60. 355-357 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Y.Sato, M.Oguchi, N.Menjyo, K.Imai, H.Saito, M.Ikeda, M.Isobe and O.Yamashita: "Precursor Polyprotein for Multiple Neuropeptides Secreted from Suboesophageal Ganglion of the Silkworm, Bombyx mori : Characterization of cDNA for Diapause Hormone Precursor and Identification of New Peptides." Proc.Natl.Acad.Sci.USA. 90. 3251-3255 (1993)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] M.Ikeda, Z.-H.Su, H.Saito, K.Imai, Y.Sato, M.Isobe and O.Yamashita: "Induction of Embryonic Diapause and Stimulation of Ovary Trehalase Activity in the Silkworm, Bombyx mori, by Synthetic Diapause Hormone." J.Insect.Physiol.39. 889-895 (1993)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] H.Saito, Y.Takeuchi, R.Takeda, Y.Hayashi, K.Watanabe, M.Shin, K.Imai, M.Isobe, and O.Yamashita: "The Core and Complimentary Sequence Responsible for Biological Activity of the Diapause Hormone of the Silkworm, Bombyx mori." Peptide. 15. 1173-1178 (1994)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Z-H.Su, M.Ikeda, Y.Sato, H.Saito, K.Imai, M.Isobe and O.Yamashita: "Molecular Characterization of Ovary Trehalase of the Silkworm, Bombyx mori and Its Transcriptional Activation by Diapause Hormone" Biochim.Biophys.Acta. 1281. 366-374 (1994)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] K.Shiomi, Y.Ishida, M.Ikeda, Y,Sato, H.Saito, K.Imai, M.Isobe and O.Yamashita: "Induction of Non-diapause Eggs by Anti-diapause Hormone Rabbit Serum Injected into the Diapause Type of the Silkworm, Bombyx mori." J.Insect Physiol.39. 693-699 (1994)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] K.Imai, K.Sugiura, T.Komiya, and O.Yamashita: "Isolation and Partial Structure of a Unique Lipophilic Peptide, VAP peptide, from Heads of Male Silkworm Moths" Biosci.Biotech.Biochem.60. 355-357 (1996)

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 1997-03-04  

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