Elucidation of molecular basis for the pathogenesis of AA amyloidosis based on the compositional analysis of biomolecules
| Project/Area Number |
15K08436
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Experimental pathology
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| Research Institution | Kobe Pharmaceutical University |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2017: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | アミロイドーシス / 血清アミロイドA / 高密度リポタンパク質 / グリコサミノグリカン / ペプチドライゲーション |
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| Outline of Final Research Achievements |
Human serum amyloid A (SAA) is a precursor protein of AA amyloidosis. Besides an increase in blood levels of SAA, interactions between SAA and other biological components contribute to the onset of AA amyloidosis. However, the molecular basis that directly links these interactions with the onset of disease has not been fully elucidated. In the present study, we aimed to clarify the influence of glycosaminoglycans and lipid constituents in high-density lipoproteins (HDLs) on the pathogenesis of AA amyloidosis. Our research revealed that the highly sulfated domains in heparan sulfate and the concentration of phosphatidic acid in HDLs affect the onset of AA amyloidosis. In the future, we will continue to evaluate the underlying mechanism of AA amyloidosis at the molecular level by evaluating the cytotoxicity of aggregates formed by SAA.
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Report
(4 results)
Research Products
(8 results)
