| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2002: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2001: ¥2,100,000 (Direct Cost: ¥2,100,000)
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| Research Abstract |
Establishment of therapeutics and prevention methods of an atherosclerosis is demanded to prevent a cardiac disease. Especially, the preventing method based on decrease in the VLDL secretion from liver into blood is thought effective in both VLDL- and LDL-hyperlipidemia. Based on these ideas, ER-60, which is concerned to the regulatory degradation of apolipoprotein B-100, was studied. The activity of ER-60 is regulated by a binding with the lumen domain of calnexin, which is a lectin-like molecular chaperone of endoplasmic reticulum. To identify the site of ER-60 for the binding with calnexin, the domain structure of ER-60 was determined. ER-60 was shown to be composed of four domains, a, b, b' and a'. Among domains, b' was essential for the binding with calnexin. In previous study, it has been shown that ER-60 bound to both apolopoprotein B-100 and BiP in HepG2 cell. In this study, BiP was shown to have stimulating effect on the activity of ER-60. In addition, we found that a soy 7S globulin, which has a lowering effect on synthesis of apolipoprotein 100-B, depresses the transcription of ER-60.
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