| Project/Area Number |
60571060
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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 |
Biological pharmacy
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| Research Institution | Tokyo College of Pharmacy |
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Principal Investigator |
KIKUGAWA Kiyomi Tokyo College of Pharmacy, 薬学部, 教授 (90120146)
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| Co-Investigator(Kenkyū-buntansha) |
BEPPU Masatoshi Tokyo College of Pharmacy, 薬学部, 講師 (60114633)
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| Project Period (FY) |
1985 – 1986
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| Project Status |
Completed (Fiscal Year 1986)
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| Budget Amount *help |
¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 1986: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1985: ¥800,000 (Direct Cost: ¥800,000)
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| Keywords | Erythrocyte / Cell membrane / Lipid oxidation / Membrane damage / Membrane protein / Malonaldehyde / Aldehyde / ケイ光 |
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| Research Abstract |
1. Studies on the molecules of lipid oxidation products involved in erythrocyte membrane damage.
Covalent modification of the membrane components, such as formation of fluorescent proteins and protein cross-linking, by oxidized lipids is a damaging reaction to the membrane and the cells. Malonaldehyde has been believed to be the major causative molecule of oxidized lipids involved in the protein modifications. However, our studies in various amino compounds and erythrocyte membranes have suggested that monofunctional aldehydes but not malonaldehyde are the major molecules involved in the modifications.
2. Factors affecting lipid oxidation of erythrocyte membranes.
We have shown that hemoglobin plays a catalytic role in erythrocyte membrane lipid oxidation, and its effect decreases at high concentrations.
It was also found that periodate, an oxidizing agent known to induce various biological responces of viable cells, induces lipid oxidation of erythrocyte membranes and the oxidation depends on hemoglobin and the sialyl residues of the cell surface.
3. Detection of erythrocyte membrane proteins modified with oxidized lipids.
A method for the selective radiolabeling of the membrane proteins modified with oxidized lipids has been developed. The radiolabeling was achieved by use of tritiated borohydride, and this method permitted detection and identification of the erythrocyte membrane proteins modified with oxidized lipids.
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