| Project/Area Number |
09460005
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Breeding science
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| Research Institution | Yokohama City University, Kihara Institute for Biological Research |
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Principal Investigator |
HIRANO Hisashi Yokohama City University, Kihara Institute for Biological Research, Professor, 木原生物学研究所, 教授 (00275075)
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| Co-Investigator(Kenkyū-buntansha) |
SASSA Hidenori Yokohama City University, Kihara Institute for Biological Research, Research Assistant, 木原生物学研究所, 助手 (50295507)
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| Project Period (FY) |
1997 – 1999
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| Project Status |
Completed (Fiscal Year 1999)
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| Budget Amount *help |
¥10,800,000 (Direct Cost: ¥10,800,000)
Fiscal Year 1999: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1998: ¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 1997: ¥5,800,000 (Direct Cost: ¥5,800,000)
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| Keywords | Basic 7S globulin / Leginsulin / Transformation / NMR / Carrot / Bird's-foot trefoil / plants / Hormone-like peptide / 遺伝子導入 / 細胞分裂 / 再分化 / 不定芽 / 蛋白質立体構造 / ジスルフィド結合 |
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| Research Abstract |
A basic 7S globulin isolated from plants is capable of binding to the animal insulin and insulin-like growth factors and shows similarity to the insulin receptor in protein structure, protein kinase activity and subcellular localization , suggesting this protein to have insulin receptor-like functions. A 4-kDa peptide, leginsulin isolated from legumes can bind to the basic 7S globulin. Both leginsulin and the basic 7S globulin are localized in the cell walls and plasma membranes. Leginsulin has stimulatory effect on phosphorylation activity of the basic 7S globulin. Cell proliferation and differentiation of in vitro cultured carrot tissues can be stimulated by adding leginsulin to the medium. The callus tissues of carrot and bird's-foot trefoil transfected the sense leginsulin gene using Agrobacterium transformation system showed rapid growth and formed green spots on the surface. It is concluded that leginsulin is a hormone-like peptide functionally related to animal insulins. The geometries of the disulfide bridges are conserved between leginsulin and insulin. The disulfide bridges of leginsulin are indispensable for stimulatory effect on the phosphorylation. Secondary and tertiary structures of leginsulin are apparently different from those of insulin. However, NMR analysis reveals the similarity in the amino acid residues on the surface of both molecules. The specific binding activity to their binding proteins and the stimulatory effect on protein phosphorylation can be attributed to this similarity. Thus, functionally insulin-like peptides are distributed in not only animals but possibly higher plants.
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