| Project/Area Number |
12671046
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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 |
Kidney internal medicine
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| Research Institution | Kitasato University |
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Principal Investigator |
IWASE Hitoo Kitasato University, School of Medicine Associate Professor, 医学部, 助教授 (60050663)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥2,800,000 (Direct Cost: ¥2,800,000)
Fiscal Year 2001: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 2000: ¥1,700,000 (Direct Cost: ¥1,700,000)
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| Keywords | IgA1 / Hinge / Mucin-type sugar chain / Sticky IgA1 / IgA nephropathy / Glycoform / C3 / Alteration of sugar chain / IgAl / Sticky IgAl / ヒンジ糖ペプチド / 糖鎖改変モデル / 補体C3 |
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| Research Abstract |
1. Enzymatic removal of sugar portion of IgA1 made it to get "Sticky" characteristics. Asialo-, agalacto-IgA1 acquired the ability of self-aggregation and of binding to IgG1, IgG3, IgM, IgA and C3 in the serum.
2. Among above binding proteins prepared from human serum by asialo- agalacto-IgA1/Sepharose, its IgA content was significantly high in IgA nephropathy patient than in normal control.
3. Polyclonal antibody against synthetic hinge peptide was reacted significantly higher in the IgA nephropathy group than in the other renal disease group and in the healthy control group. Furthermore, IgA1 hinge region of IgA nephropathy patient was abberantly exposed by under-glycosylation could induce the humoral immune response.
4. Mss spectrometry of hinge glycopeptide from IgA1 indicated that there were mutually different 21 glycopeptides. Significant shift of the peaks on mass chromatogram toward low-molecular weight side due to the under-glycosylation of IgA1 was observed in IgA nephropathy patient.
5. The same method proved significant under-glycosylation of glomerular IgA1 in IgA nephropathy patient.
6. Analysis of the hinge glycopeptide by capillary electrophoresis indicated that aggregated IgA1 had a lower number of sialic acid.
7. It was found that the enzymatically deglycosylated human IgA1 molecules accumulated and induce inflammatory cell reaction in rat glomeruli.
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