| Project/Area Number |
18580114
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Food science
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| Research Institution | Shinshu University |
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Principal Investigator |
NAKAMURA Soichiro Shinshu University, Faculty of Agriculture, Professor (00105305)
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| Co-Investigator(Kenkyū-buntansha) |
NAKAMURA Kozo Shinshu University, Faculty of Agriculture, Associate Professor (20345763)
TERASHIMA Syoji Shimane University, Faculty og Medicine, Associate Professor (40227517)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥3,660,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥360,000)
Fiscal Year 2007: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2006: ¥2,100,000 (Direct Cost: ¥2,100,000)
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| Keywords | Prion / Human cvstatin C / Amyloid formation / Food materials / Ginsenoside / Chlorogenic acid / Amyloidosis / Animal test / 食原性プリオン / シスタチン / 凝集阻害 / 機能改変 |
|---|
| Research Abstract |
Cystatin C, a cysteine proteinase inhibitor, is ubiquitous in mammalian tissues and body fluids, and plays an important role in extracellular regulation of endogenous cysteine protainases. A human cystatin C has been shown to easily cause amyloid deposits in the brains of patients suffering from Alzheimer's disease or hereditary cystatin C amyloid angiopathy. Since the incidence of the incurable diseases has been steadily on the rise in developed nations, there has been an increased interest in screening for food-grade anti-amyloidgenic compounds in food stuffs. A synthetic gene encoding human cystatin C was constructed and inserted not only into a Pichia pastoris vector, pPCIZa-C (Invitrogen, Carlsbad, CA) but also into a Escherichia colt vectors pQE-30 and pQE-32. The resulting recombinant human cystatin C was used for screening of bioactive compounds with amyloidgenicity in food stuffs. As the result, it was demonstrated that flavonoids and phenolic acids from plants are capable of in vitro inhibition of amyloid-fibril formation of cystatin. Ginsenoside Rg1 with a monosaccharide from gingseng showed strong anti-amyloidgenicity towards cystatin, whereas ginsenoside Re with a disaccharide chain did not. Chlorogenic acid and its derivatives also exhibited anti-amyloidgenicity, although it may have a tendency to be attenuated over a period of digestion in the intestinal tract. These observations can be useful for novel inhibitors' design as therapeutic anents for amyloid-associated diseases.
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