| Project/Area Number |
61440006
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| Research Category |
Grant-in-Aid for General Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
動物発生・生理学
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| Research Institution | Tokyo Institute of Technology |
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Principal Investigator |
HOSHI Motonori Tokyo Institute of Technology, 理学部, 教授 (20012411)
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| Co-Investigator(Kenkyū-buntansha) |
FUJIMOTO Yoshinori Tokyo Institute of Technology, 理学部, 助手 (50173472)
KAKINUMA Katsumi Tokyo Institute of Technology, 理学部, 助教授 (90092543)
SAWADA Hitoshi Tokyo Institute of Technology, 理学部, 助教授 (60158946)
池川 信夫 東京工業大学, 理学部, 教授 (50016119)
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| Project Period (FY) |
1986 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥28,800,000 (Direct Cost: ¥28,800,000)
Fiscal Year 1988: ¥2,500,000 (Direct Cost: ¥2,500,000)
Fiscal Year 1987: ¥10,000,000 (Direct Cost: ¥10,000,000)
Fiscal Year 1986: ¥16,300,000 (Direct Cost: ¥16,300,000)
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| Keywords | Sperm-Egg Interactions / Sperm Receptor / Acrosome Reaction / Lysin / G-Protein / Glycolipid / Glycosidase / プロテアーゼ / Gタンパク / 受精 / 精子一卵相互作用 / 糖タンパク質 / ステロイドサポニン / Nーアセチルヘキソサミニダーゼ / 精子・卵黄膜結合 / フコシダーゼ / 硫酸化糖タンパク質 / 卵黄膜 / 卵ゼリー |
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| Research Abstract |
Molecular mechanisms of the acrosome reaction, sperm-binding to and sperm penteration through the vitelline coat, and membrane fusion were studied by using echinoderms and ascidians.
Starfish egg jelly contains a sulfated glycoprotein (ARIS), a high-mannose glycoprotein with saccharide chains having 0-3 glucose residues at the non-reducing termini, sulfated steroidal saponins including Co-ARIS I, II, and III, and oligopeptides including SAP. In alkaline or high Ca^<++> sea water, ARIS induces the acrosome reaction. In normal sea water, a combination of ARIS and Co-ARIS induces the acrosome reaction whithout incresing PH_i.
Three novel ceramide dihexosides; melibiosyl,gentibiosyl and from echinoderm gametes. Their possible roles in the acrosome reaction and fusion of sperm and egg plasma membranes are under investigation.
N-Acetylhexosaminidase, the most potent glycosidase in the sperm of Halocynthia roretzi, was purified and characterized. The second potent was -L-fucosidase that seems to serve as vitelline coat-binding protein. Sperm receptor in the vitelline coat was suggested to have terminal L-Fuc, D-GalNAc and D-GlcNAc. Indeed, major N-glycoside chains of the vitelline coat have such structures. A 60K protein was suggested to be a physiological substrate of vitelline coat lysin(s).
During the course of oocyte maturation triggered by 1-methyl-adenine in Asterina, a 39K Gi protein and a trypsin-type protease of high substrate specificity participate in the steps befor and after MPF formation, respectively.
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