2012 Fiscal Year Final Research Report
The analysis of altered glycosylation in Alzheimer's disease
| Project/Area Number |
22590933
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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 |
Neurology
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| Research Institution | Tottori University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
TANIGUCHI Miyako 鳥取大学, 医学部, 医学部 (50335527)
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| Project Period (FY) |
2010 – 2012
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| Keywords | アルツハイマー病 / 脳神経疾患 / 糖鎖 / 診断マーカー |
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| Research Abstract |
We measured the contents of the sugar chain in two glycoproteins which has altered glycosylation in Alzheimer’s disease (AD), one is transferrin and another is the protein associated with immune system, temporally named protein X. We indicated both of them had decreased glycosylation in very early stage of AD. The decreased levels of glucosylation of protein X was correlated with the altered levels of cerebrospinal fluid (CSF) amyloid β protein. The altered sugar chain of protein X in Alzheimer’s serum must be a 優秀な biological marker for diagnosis of AD, that monitors the change in the brain or CSF derived from the brain. On the other way, we also found the decreased levels of a-2, 6-sialyltransferase (STase) in Alzheimer’s serum. STase is the enzyme which adds the sialic acid to the transferrin. This indicates the decreased sialylation of Alzheimer’s serum transferrin is 原因であるby the altered STase. These two changes in glycoproteins suggest the 異常なglycosylation 密接にassociates the pathophysiology of AD
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Research Products
(44 results)
