STUDIES ON THE FUNCTION OF A NOVEL LOWDENSITY LIPOPROTEIN WITH PHOSPHOLIPIDS FOUND IN THE OVARIES FROM CRUSTACEA
| Project/Area Number |
05660236
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Fisheries chemistry
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| Research Institution | KAGOSHIMA UNIVERSITY, |
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Principal Investigator |
ANDO Seichi KAGOSHIMA UNIVERSITY,FACULTY OF FISHERIES,ASSOCIATE PROFESSOR, 水産学部, 助教授 (80131986)
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| Project Period (FY) |
1993 – 1994
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| Project Status |
Completed (Fiscal Year 1994)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1994: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1993: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | Crustacea / Ovary / Hemolymph / Phospholipids / Lipoproteins / Vitellogenin / Proteinase / プロテイナーゼ活性 |
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| Research Abstract |
The major source of such nutrients as protein and lipid for developing embryo of all oviparous animals including crustacea is the egg yolk which constituents the non-organellar content of the oocyte.The crustacean egg yolk protein called lipovitellin is derived from hemolymph precursor, vitellogenin. Vitellogenin is a lipoprotein and functions as carriers of lipid and protein to the egg yolk.
The presence of vitellogenin and lipovitellin was examined in the the hemolymph and ovaries of five species of crustacea, respectively, by differential density gradient ultracentrifugation. Lipovitellin was present in the egg yolk proteins from freshwater prawn, kuruma prawn, striped stone crab, and mitten crab, while low-density (LDL) was isolated from the egg yolk protein of large-toothed sand crayfish as well as lipovitellin. The LDL found in the egg yolk of large-toothed sand crayfish was of interest because it possessed large amounts of phospholipid but not triacylglycerol as a major lipid component.
The differece of apolipoprotein features between vitellogenin and lipovitellin from large-toothed sand crayfish suggested the degradation of vitellogenin. The LDL isolated from the egg yolk of large-toothed sand crayfish proved to possess a vitellogenin-degrading proteinase activity. Vitellogenin was degraded by incubating with LDL at pH 6.0 for 72 hr at 35ﾟC in the presence of calcium ion and apolipoprotein profiles of vitellogenin degraded by LDL were very similar to those of lipovitellin in the egg. Vitellogenin was never cleaved in the presence of EDTA and/or serine proteinase inhibitors such as diisopropyl fluorophosphate and phenylmethanesulfonyl fluoride.
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Report
(3 results)
Research Products
(10 results)
