| Project/Area Number |
11670952
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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 |
Psychiatric science
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| Research Institution | Kyushu University of Health and Welfare (2000-2001)
宮崎医科大学 (1999) |
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Principal Investigator |
TASHIRO Kenichiro Kyushu University of Health ang Welfare, 保健科学部, 教授 (00216954)
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| Co-Investigator(Kenkyū-buntansha) |
MATSUDA Kazanori Miyazaki Medical College, 医学部, 助手 (30311880)
MITSUYAMA Yoshio Miyazaki Medical College, 医学部, 教授 (20112427)
SAWADA Atsushi Kyushu University of health and Welfare, 保健科学部, 教授 (10040247)
林 要人 宮崎医科大学, 医学部, 助手 (20295223)
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| Project Period (FY) |
1999 – 2000
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 2000: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1999: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | Laminin fragment / Laminin peptide / IKVAN / YFQRYLI / IKLLI / integrin / βaryloid / Alzheimer's disease / YFOQRYLI / アルツハイマー |
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| Research Abstract |
Extracellular matrixes containing laminin have posibility that those may induce degeneration (death) of neural cells with senile plaques or neurofibril tangles after age of puberty and may cause Alzheimer's disease (AD). We could not certificate the binding of laminin-fragments to homogenate from normal brain and AD brain in the experiment using an affinity colum of antibodies against active laminin peptide IKVAV and YFQRYLI. Therefore, we recognized a new cell attachment active site which was not masked in laminin. We synsesized a peptide (LAS) containing the IKLLI sequence of laminin α1 chain which has a common motif of IKVAV and certificated the activities of cell attachment, neurite outgrowth, heparin binding and cell proliferation. Furthermore, we proved that the peptide LAS was one of the active sites of laminin same as IKVAV and YFQRYLI because LAS-mediated cell attachment was inhibited by anti-integrin α3 β1 antibodies. However, we have not expected results of purification of specific proteins binding to anti-LAS antibody from human normal brain and AD brain using an anti-LAS antibody affinity chromatography and gel chromatography. In the future, we will investigate the role of peptide LAS related to aggregation of β amyloid.
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