1995 Fiscal Year Final Research Report Summary
Mechanism of amyloid formation in amyloidosis : Clinical, biochemical, and pathological study
| Project/Area Number |
06670660
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Neurology
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| Research Institution | KUMAMOTO UNIVERSITY |
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Principal Investigator |
ANDO Yukio Kumamoto University University Hospital Assistant Professor, 医学部・附属病院, 助手 (20253742)
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| Project Period (FY) |
1993 – 1995
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| Keywords | FAP / Amyloidosis / Transthyretin / Liver transplantation / Lipoprotein / LDL / Gene mutation / Polyneuropathy |
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| Research Abstract |
We found out that variant transthyretin (TTR) circulates bound to both HDL and LDL.In HDL from FAP patients, almost the same levels of normal and variant TTR was detected while only variant TTR was observed in extracted LDL : 0.6% of the circulated TTR was associated with LDL.This phenomenon was also seen in LDL from other points of mutation, such as Gln89, Pro36, and Thr34. Incubation of extracted LDL and with variant and normal TTR revealed that variant form of TTR increased the affinity to LDL.
Five FAP patients underwent liver transplantation at Huddinge Hospital, Sweden, and Brisbane Princess Alexandra Hospotal. They all had good clinical couese 5-24 months after the operation. As we reported previously, especially autonomic dysfunction improved significantly.
Gene hunting for TTR mutations in FAP was also tried to perfom using low and high temperature controlling water bath.
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Research Products
(14 results)
